猪链球菌2型抗体检测试纸条的制备及FBPS与宿主蛋白质相互作用研究
|
摘要
猪链球菌(Streptocuccus suis,S.suis)是一种重要的人畜共患病原菌。根据荚膜多糖(capsular polysaccharide，CPS)抗原成分不同，可以将猪链球菌分为35个血清型(1.34型和1／2型)。其中，猪链球菌2型(Streptocuccussuistype 2，SS2)是最常见、也是毒力最强的血清型。
猪链球菌是一种条件致病性病原菌，成年猪感染后一般不表现任何临床症状。但是，受到应激因素的刺激，往往会加剧发病率和死亡率。血清学调查(sero-surveillance)或抗体水平监测(antibody monitoring)有助于了解猪群中链球菌感染状况，为控制猪链球菌病提供科学的依据．目前，有一些方法可以用于SS2抗体检测，如ELISA和琼脂扩散试验等，但这些方法由于费时或成本高等因素的制约，只能用于实验室诊断，不适合用于大量样品的检测。因此，急需研制一种快速检测SS2抗体的方法，对我国SS2血清流行病学进行调查。
本试验应用胶体金标记技术(immunogold labeling technique)，根据免疫层析原理，用胶体金标记葡萄球菌蛋白A(SPA)作为探针，用纯化的SS2 CPS和健康猪IgG分别作为检测线试剂和对照线试剂，研制了一种SS2抗体快速检测试纸条。该试纸条具有检测快速和使用方便等优点，可以适用于临床样品的大量检测，为SS2血清抗体检测提供了有效的工具。
用该试纸条检测16份SS2感染康复猪血清抗体和24份SS2高免猪血清，试纸条检测为100％阳性，与ELISA法检测结果完全一致；检测68份其它细菌高免血清或健康猪血清，结果除一份链球菌1型(SS1)高免血清呈弱阳性外，其余均为阴性。用试纸条检测20份阳性高免血清抗体滴度，结果表明试纸条的敏感性和ELISA相当。用试纸条和ELISA检测486份临床血清样品，结果表明试纸条的特异性(specificity)为94.6％，敏感性(sensitivity)为91.7％，两种方法检测结果的符合度很高(kappa=0.863)。由此表明，试纸条法可以代替ELISA在临床检测中的应用。
深入了解猪链球菌的致病机理，可以为链球菌病的预防和治疗提供科学的依据。病原菌与宿主细胞之间的相互作用，在致病过程中发挥着重要的作用。研究病原与宿主细胞相互作用，可以促进对致病机理的探索。并可以为药物筛选、疫苗设计提供理论依据，以便制定科学的疫病控制措施。
纤连蛋白结合蛋白(FBPS)由链球菌Fbps基因编码，可以与人的纤维结合蛋白和纤维蛋白素原结合。在SS2感染过程中，FBPS与细菌在特定器官中的定殖有密切关系，推测FBPS与SS2的致病性有关。因此，本试验用CytoTrap酵母双杂交技术，研究FBPS与宿主细胞蛋白质相互作用，旨在探索FBPS在SS2致病性中的作用。
用PCR方法扩增SS2 Fbps全长基因，定向克隆到pSos载体多克隆位点中，构建bait载体(pSos-Fbps)。并将Fbps克隆到pET-28c载体中，构建重组表达载体。将pSos-Fbps和鼠cDNA文库(pMyr-cDNA)共转化cdc25H酵母细胞，筛选与FBPS相互作用的克隆。经过筛选和重复验证，得到2个与FBPS相互作用的阳性克隆，并对Target载体插入片段进行测序，经BLAST分析，两个基因分别与凋亡抑制因子5(apoptosis inhibitor 5，API 5)基因和锌指结构FYVE结构域27(zinc finger FYVE domain containing 27，ZFYVE 27)基因的同源性为99％和100％。
将重组原核表达载体pET-28c-Fbps转化BL21大肠杆菌细胞，进行FBPS蛋白质表达。分别用PCR扩增API 5和ZFYVE 27全长基因，定向克隆到pcDNA3.1/myc-His载体中，构建真核表达载体(pcDNA3.1/myc-His-API 5和pcDNA3.1/myc-His-ZFYVE 27)，并分别转染293T细胞进行表达。将细胞裂解后，用兔抗Myc抗体共沉淀FBPS和ZFYVE 27或FBPS和API 5复合物，再用SS2高免血清进行Western-blotting分析。用免疫共沉淀试验分别证了FBPS与API 5和ZFYVE 27之间的相互作用。
Streptococcus suis (S. suis) is a common pathogenic microorganism and can cause avariety of clinical diseases in human and swine. Based on the CPS antigens of S. suis, 35serotypes or capsular types have been characterized. S. suis serotype 2 (SS2) is mostcommonly associated with severe disease and is the serotype most frequently isolatedfrom pigs.
S. suis is an opportunistic bacterium of pigs. Crowding, poor ventilation, suddenweather changes, mixing, relocation, immunization and the presence of concurrentinfections could predispose pigs to SS2 infection and morbidity. Thereforesero-surveillance or antibody monitoring may be useful in determining the infection statusand can play an important role in the control Streptococcosis in pigs.
In this study, an immunochromatographic strip (ICS) was developed for thedetection of antibody against SS2. Colloidal gold particles labeled with staphylococcalprotein A (SPA) were used as the. detector reagent. The capsular polysaccharide (CPS) ofSS2 and affinity purified IgG from a healthy naive pig were immobilized on test andcontrol regions of a nitrocellulose membrane, respectively. An Enzyme linkedimmunosorbent assay (ELISA) for SS2 antibody detection based on purified CPS wasused as a control method.
The ICS was used to (i) detect anti-CPS antibody in 16 sera taken from 4 SS2infected pigs, 24 sera from pigs hyper-immunized with SS2 and 68 sera from pigsinoculated or infected with bacteria other than SS2; (ⅱ) determine anti-CPS antibodytiters of 20 positive sera for comparison with ELISA; (ⅲ) detect anti-CPS antibody in 486clinical sera taken from diseased pigs also for comparison with ELISA.
For 16 sera from pigs that had survived challenge with SS2, both ICS and ELISAgave all samples positive results. For the 24 hyper-immune sera raised against SS2, therewas also a 100% correlation between ELISA and ICS results. All of the 68 sera againstnon-SS2 bacteria, except one antisera against S. suis type 1 determined as weak positiveby both ICS and ELISA, were negative in both ELISA and ICS tests. Antibody titers of 20hyper-immune sera raised against SS2 were tested by ICS and ELISA. The quantifyingtest result indicated that the sensitivity of the strip test is close to or slightly less than thatof ELISA.
Of the 486 clinical sera from sick pigs, 228 were antibody positive and 258 werenegative by ELISA, whereas 223 were positive and 263 were negative by ICS. Additionally 209 were positive in both assays and 244 were negative in both tests. Thus,the specificity and sensitivity of ICS, compared to ELISA, was 96.4% and 91.7%,respectively. There was an excellent agreement (kappa=0.863) between ICS and ELISA.
Although some assays, e.g. the indirect ELISA and agar gel precipitation tests, havebeen developed for antibody detection for S. suis, these methods are not suitable for useoutside of the research laboratory. In contrast, the ICS is easy to use and rapid. In thiscontext, the ICS can be used as a tool for seroepidemiological survey of pigs fromdifferent areas in China. This would in turn facilitate the formulation of effective controlmeasures.
To understand the pathogenesis of S. suis infection contributes to develop strategiesfor prevention or therapy. The interactions between pathogenic microorganism and hostcells may play an important role in its pathogenicity. In this study, the CytoTraptwo-hybrid syste was used to investigate the protein-protein interaction between FBPSand the host cells.
FBPS, which can bind to human FN and FGN, is a protein coded by Fbps gene of S.suis. And Fbps gene is present in all known serotypes of S. suis except serotype 32 andserotype 34. A considerable number of FN and FGN binding proteins of various bacterialspecies have been described. Most of these proteins have been shown to be involved inadhesion to epithelial and/or endothelial cells. FBPS play a role in the SS2 colonization ofspecific organs.
The full length Fbps gene was amplified from chromosomal DNA of SS2 strainSCZY05 by PCR. Fbps gene was unidirectional cloned into pSos after the amplified PCRproduct and pSos vector were digested with BamHⅠand NotⅠ, yielding the bait plasmidpSos-Fbps. The recombinant expression plasmid pET-28c-Fbps was constructed by thesame way.
The library was screened by co-transformation of the pSos-Fbps bait construct into atemperature-sensitive cdc25H yeast strain that can not grow at 37℃. If the bait proteinphysically interacts with the target protein, the hSos protein is recruited to the membraneactivating the Ras signaling pathway and allowing the cdc25H yeast strain to grow at 37℃. The clones growing at 37℃on SD/galactose (-UL) plates but not on SD/glucose(-UL) plates were selected as "putative positive" clones and were analyzed further.
The Target plasmid DNA was isolated from pMyr eDNA putative positive clones andwas transformed into E. coli cells for plasmid amplification. Colonies contains eDNAfragment insertion identified by restriction digest analysis. The positive Target plasmid was sequenced on a 3730 Sequencing system. The sequencing results were sent to NCBIfor BLAST searches on line. In this study, we got two positive target plasmid. One ofthese genes is identical to the apoptosis inhibitor 5 (API 5) gene. The other showedhomology to genes encoding zinc finger FYVE domain containing 27 (ZFYVE 27).
The protein-protein interaction between FBPS and API 5 or ZFYVE 27 wasconfirmed by ProFound Co-immunoprecipation assay. Recombinant plasmid pET-28c-Fbps was transformed into E. coli BL21 cells for protein expression. The full length ofZFYVE 27 and API 5, obtained by PCR from the target vectors were subcloned intopcDNA3.1/myc-His, yielding pcDNA3.1/myc-His-ZFYVE 27 and pcDNA3.1/myc-His-API 5. The recombinant expression plasmids were transfected into 293T cells for proteinexpression. Anti-mye probe antibody was used to immunopreeipitate the expressedprotein (API 5 or ZFYVE 27) from the whole cell lysate and supernatant of BL21transformed with pET-28c-Fbps culture. The complex was then resolved on a 10% SDSpolyacrylamide gel. The separated proteins were transferred to a nitrocellulose membrane.Pig anti-sera against SS2 were used for western-blotting.
猪链球菌是一种条件致病性病原菌，成年猪感染后一般不表现任何临床症状。但是，受到应激因素的刺激，往往会加剧发病率和死亡率。血清学调查(sero-surveillance)或抗体水平监测(antibody monitoring)有助于了解猪群中链球菌感染状况，为控制猪链球菌病提供科学的依据．目前，有一些方法可以用于SS2抗体检测，如ELISA和琼脂扩散试验等，但这些方法由于费时或成本高等因素的制约，只能用于实验室诊断，不适合用于大量样品的检测。因此，急需研制一种快速检测SS2抗体的方法，对我国SS2血清流行病学进行调查。
本试验应用胶体金标记技术(immunogold labeling technique)，根据免疫层析原理，用胶体金标记葡萄球菌蛋白A(SPA)作为探针，用纯化的SS2 CPS和健康猪IgG分别作为检测线试剂和对照线试剂，研制了一种SS2抗体快速检测试纸条。该试纸条具有检测快速和使用方便等优点，可以适用于临床样品的大量检测，为SS2血清抗体检测提供了有效的工具。
用该试纸条检测16份SS2感染康复猪血清抗体和24份SS2高免猪血清，试纸条检测为100％阳性，与ELISA法检测结果完全一致；检测68份其它细菌高免血清或健康猪血清，结果除一份链球菌1型(SS1)高免血清呈弱阳性外，其余均为阴性。用试纸条检测20份阳性高免血清抗体滴度，结果表明试纸条的敏感性和ELISA相当。用试纸条和ELISA检测486份临床血清样品，结果表明试纸条的特异性(specificity)为94.6％，敏感性(sensitivity)为91.7％，两种方法检测结果的符合度很高(kappa=0.863)。由此表明，试纸条法可以代替ELISA在临床检测中的应用。
深入了解猪链球菌的致病机理，可以为链球菌病的预防和治疗提供科学的依据。病原菌与宿主细胞之间的相互作用，在致病过程中发挥着重要的作用。研究病原与宿主细胞相互作用，可以促进对致病机理的探索。并可以为药物筛选、疫苗设计提供理论依据，以便制定科学的疫病控制措施。
纤连蛋白结合蛋白(FBPS)由链球菌Fbps基因编码，可以与人的纤维结合蛋白和纤维蛋白素原结合。在SS2感染过程中，FBPS与细菌在特定器官中的定殖有密切关系，推测FBPS与SS2的致病性有关。因此，本试验用CytoTrap酵母双杂交技术，研究FBPS与宿主细胞蛋白质相互作用，旨在探索FBPS在SS2致病性中的作用。
用PCR方法扩增SS2 Fbps全长基因，定向克隆到pSos载体多克隆位点中，构建bait载体(pSos-Fbps)。并将Fbps克隆到pET-28c载体中，构建重组表达载体。将pSos-Fbps和鼠cDNA文库(pMyr-cDNA)共转化cdc25H酵母细胞，筛选与FBPS相互作用的克隆。经过筛选和重复验证，得到2个与FBPS相互作用的阳性克隆，并对Target载体插入片段进行测序，经BLAST分析，两个基因分别与凋亡抑制因子5(apoptosis inhibitor 5，API 5)基因和锌指结构FYVE结构域27(zinc finger FYVE domain containing 27，ZFYVE 27)基因的同源性为99％和100％。
将重组原核表达载体pET-28c-Fbps转化BL21大肠杆菌细胞，进行FBPS蛋白质表达。分别用PCR扩增API 5和ZFYVE 27全长基因，定向克隆到pcDNA3.1/myc-His载体中，构建真核表达载体(pcDNA3.1/myc-His-API 5和pcDNA3.1/myc-His-ZFYVE 27)，并分别转染293T细胞进行表达。将细胞裂解后，用兔抗Myc抗体共沉淀FBPS和ZFYVE 27或FBPS和API 5复合物，再用SS2高免血清进行Western-blotting分析。用免疫共沉淀试验分别证了FBPS与API 5和ZFYVE 27之间的相互作用。
Streptococcus suis (S. suis) is a common pathogenic microorganism and can cause avariety of clinical diseases in human and swine. Based on the CPS antigens of S. suis, 35serotypes or capsular types have been characterized. S. suis serotype 2 (SS2) is mostcommonly associated with severe disease and is the serotype most frequently isolatedfrom pigs.
S. suis is an opportunistic bacterium of pigs. Crowding, poor ventilation, suddenweather changes, mixing, relocation, immunization and the presence of concurrentinfections could predispose pigs to SS2 infection and morbidity. Thereforesero-surveillance or antibody monitoring may be useful in determining the infection statusand can play an important role in the control Streptococcosis in pigs.
In this study, an immunochromatographic strip (ICS) was developed for thedetection of antibody against SS2. Colloidal gold particles labeled with staphylococcalprotein A (SPA) were used as the. detector reagent. The capsular polysaccharide (CPS) ofSS2 and affinity purified IgG from a healthy naive pig were immobilized on test andcontrol regions of a nitrocellulose membrane, respectively. An Enzyme linkedimmunosorbent assay (ELISA) for SS2 antibody detection based on purified CPS wasused as a control method.
The ICS was used to (i) detect anti-CPS antibody in 16 sera taken from 4 SS2infected pigs, 24 sera from pigs hyper-immunized with SS2 and 68 sera from pigsinoculated or infected with bacteria other than SS2; (ⅱ) determine anti-CPS antibodytiters of 20 positive sera for comparison with ELISA; (ⅲ) detect anti-CPS antibody in 486clinical sera taken from diseased pigs also for comparison with ELISA.
For 16 sera from pigs that had survived challenge with SS2, both ICS and ELISAgave all samples positive results. For the 24 hyper-immune sera raised against SS2, therewas also a 100% correlation between ELISA and ICS results. All of the 68 sera againstnon-SS2 bacteria, except one antisera against S. suis type 1 determined as weak positiveby both ICS and ELISA, were negative in both ELISA and ICS tests. Antibody titers of 20hyper-immune sera raised against SS2 were tested by ICS and ELISA. The quantifyingtest result indicated that the sensitivity of the strip test is close to or slightly less than thatof ELISA.
Of the 486 clinical sera from sick pigs, 228 were antibody positive and 258 werenegative by ELISA, whereas 223 were positive and 263 were negative by ICS. Additionally 209 were positive in both assays and 244 were negative in both tests. Thus,the specificity and sensitivity of ICS, compared to ELISA, was 96.4% and 91.7%,respectively. There was an excellent agreement (kappa=0.863) between ICS and ELISA.
Although some assays, e.g. the indirect ELISA and agar gel precipitation tests, havebeen developed for antibody detection for S. suis, these methods are not suitable for useoutside of the research laboratory. In contrast, the ICS is easy to use and rapid. In thiscontext, the ICS can be used as a tool for seroepidemiological survey of pigs fromdifferent areas in China. This would in turn facilitate the formulation of effective controlmeasures.
To understand the pathogenesis of S. suis infection contributes to develop strategiesfor prevention or therapy. The interactions between pathogenic microorganism and hostcells may play an important role in its pathogenicity. In this study, the CytoTraptwo-hybrid syste was used to investigate the protein-protein interaction between FBPSand the host cells.
FBPS, which can bind to human FN and FGN, is a protein coded by Fbps gene of S.suis. And Fbps gene is present in all known serotypes of S. suis except serotype 32 andserotype 34. A considerable number of FN and FGN binding proteins of various bacterialspecies have been described. Most of these proteins have been shown to be involved inadhesion to epithelial and/or endothelial cells. FBPS play a role in the SS2 colonization ofspecific organs.
The full length Fbps gene was amplified from chromosomal DNA of SS2 strainSCZY05 by PCR. Fbps gene was unidirectional cloned into pSos after the amplified PCRproduct and pSos vector were digested with BamHⅠand NotⅠ, yielding the bait plasmidpSos-Fbps. The recombinant expression plasmid pET-28c-Fbps was constructed by thesame way.
The library was screened by co-transformation of the pSos-Fbps bait construct into atemperature-sensitive cdc25H yeast strain that can not grow at 37℃. If the bait proteinphysically interacts with the target protein, the hSos protein is recruited to the membraneactivating the Ras signaling pathway and allowing the cdc25H yeast strain to grow at 37℃. The clones growing at 37℃on SD/galactose (-UL) plates but not on SD/glucose(-UL) plates were selected as "putative positive" clones and were analyzed further.
The Target plasmid DNA was isolated from pMyr eDNA putative positive clones andwas transformed into E. coli cells for plasmid amplification. Colonies contains eDNAfragment insertion identified by restriction digest analysis. The positive Target plasmid was sequenced on a 3730 Sequencing system. The sequencing results were sent to NCBIfor BLAST searches on line. In this study, we got two positive target plasmid. One ofthese genes is identical to the apoptosis inhibitor 5 (API 5) gene. The other showedhomology to genes encoding zinc finger FYVE domain containing 27 (ZFYVE 27).
The protein-protein interaction between FBPS and API 5 or ZFYVE 27 wasconfirmed by ProFound Co-immunoprecipation assay. Recombinant plasmid pET-28c-Fbps was transformed into E. coli BL21 cells for protein expression. The full length ofZFYVE 27 and API 5, obtained by PCR from the target vectors were subcloned intopcDNA3.1/myc-His, yielding pcDNA3.1/myc-His-ZFYVE 27 and pcDNA3.1/myc-His-API 5. The recombinant expression plasmids were transfected into 293T cells for proteinexpression. Anti-mye probe antibody was used to immunopreeipitate the expressedprotein (API 5 or ZFYVE 27) from the whole cell lysate and supernatant of BL21transformed with pET-28c-Fbps culture. The complex was then resolved on a 10% SDSpolyacrylamide gel. The separated proteins were transferred to a nitrocellulose membrane.Pig anti-sera against SS2 were used for western-blotting.
引文
1．白雪梅，张亚兰，孙娜，周永运，叶长芸，郑瀚，杜华茂，徐建国．100株猪链球菌的生化检测及药物敏感性分析．中国人畜共患病学报，2006，22：396-398．
2．曹三杰，段丽丽，肖驰，文心田．猪2型链球菌毒力因子研究进展．中国人兽共患病学报，2007，23：89-91．
3．韩雪清，林祥梅，吴绍强，贾广乐，刘建，梅琳．猪链球菌2型多重PCR快速检测方法的建立．中国兽医科学，2006，36：112-117．
4．何孔旺，陆承平．猪链球菌2型的致病特性与毒力因子．中国兽医科技，2000，30(9)：17-20．
5．何孔旺，倪艳秀，王继春，何家惠，王伟峰，杨瑛，陆承平，林继煌．猪链球菌2型的分子流行病学研究．中国人畜共患病杂志，2002，18：45-47．
6．李金海，张东，石谦，李春，马孟根，陈斌，吴萱．四川猪2型链球菌病的PCR检测．四川畜牧兽医，2005，9：30-32．
7．李明，何孔旺，陆承平．检测两种猪源链球菌抗体间接ELISA方法的筛选与应用．中国人兽共患病杂志，2005．21：867-870．
8．刘军，冯书章，尹铁勇，孙洋，郭学军，祝令伟．猪链球菌2型和9型菌株的多重PCR检测．中国人畜共患病杂志，2005，21：510-514．
9．陆承平主编，兽医微生物学(第三版)。中国农业出版社，2001，204-212．
10．马清霞，何孔旺，陆承平．猪链球菌2型及其毒力因子检测多重PCR的建立与应用．中国兽医学报，2006，26：28-31．
11．马有智，方维焕．猪链球菌血清2型JX02株溶血素基因的克隆及序列分析．中国兽医杂志，2003，23：460-462．
12．欧瑜，陆承平．猪链球菌2型国内分离株毒力相关蛋白的分析．微生物学报，2002，42：105-109．
13．孙理云，范红结，陆承平．猪链球菌2型FBPS的纤连蛋白结合部位的初步确定．微生物学报，2005，45：753-756．
14．唐家琪，朱进，郭恒彬，胡晓抒，朱凤才，刘光中．猪链球菌引起人中毒性休克综合征和脑膜脑炎的流行病学调查及病原学研究．第三军医大学学报，2001，23：1292-1295．
15．田云，Frank M Aarestrup，陆承平．猪链球菌2型可能的毒力基因的发现．微生物学报，2004，44：613-616．
16．唐家琪，朱进，郭恒彬，胡晓抒，朱凤才，刘光中．猪链球菌引起人中毒性休克综合征和脑膜脑炎的流行病学调查及病原学研究．第三军医大学学报，2001，23：1292-1295．
17．王海丽，王长军，陆承平，潘秀珍，唐家琪．猪链球菌2型人源分离株截短 的溶菌酶释放蛋白基因的克隆及原核表达．细胞与分子免疫学杂志，2006，22：178—180．
18．王花茹，王长军，陆承平，潘秀珍，陶开华，唐家琪．致病性猪链球菌主要毒力因子基因多重PCR检测．中国流行病学杂志，2005，26：640-644．
19．曾巧英，陆承平．溶茵酶释放蛋白介导猪链球菌2型的血凝活性．中国兽医科技，2002，32：24—27．
20．曾巧英，陆承平．猪链球菌2型溶菌酶释放蛋白诱导上皮细胞融合和凋亡．微生物学报，2003，43：407—412．
21．朱进，唐家琪，郭恒彬，张云，陶开华。一起猪链球菌病暴发流行的流行病学及病原学研究．解放军预防医学杂志，2000，18：257-260．
22．朱进，唐家琪，张云，郭恒彬，陶开华．爆发流行中毒性休克综合征病原体生物学特性及鉴定．中华传染病杂志，2001，19：84-86．
23．朱荫昌，余传信，殷旭仁，刘韵娟．胶体染料斑点免疫试验检测血吸虫病人抗体方法的建立及初步应用．中国血吸虫病防治杂志，1995，7：214-218．
24. Aarestrup FM, Jorsal SE, Jensen NE. Serological characterization and antimicrobial susceptibility of Streptococcus suis isolates from diagnostic samples in Denmark during 1995 and 1996. Vet Microbiol, 1998a, 60: 59-66.
25. Aarestrup FM, Rasmussen SR, Artursson K, Jensen NE. Trends in the resistance to antimicrobial agents of Streptococcus suis isolates from Denmark and Sweden. Vet Microbiol, 1998b, 63: 71-80.
26. Allen AG, Bolitho S, Lindsay H, Khan S, Bryant C, Norton P, et al. Generation and characterization of a defined mutant of Streptococcus suis lacking suilysin. Infect Immun, 2001, 69: 2732-2735.
27. Allen AG, Lindsay H, Seilly D, Bolitho A, teters SE, Maskell DJ. Identification and characterisation of hyaluronate lyase from Streptococcus suis. Microbial Pathogenesis, 2004, 36: 327-335.
28. Allgaier A, Goethe R, Wisselink HJ, Smith HE, Valentin-Weigand P. Relatedness of Streptococcus suis Isolates of Various Serotypes and Clinical Backgrounds as Evaluated by Macrorestriction Analysis and Expression of Potential Virulence Traits, J Clin Microbiol, 2001, 39: 445-453.
29. Amass SF, SanMiguel P, Clark LK. Demonstration of vertical transmission of Streptococcus suis in swine by genomic fingerprinting. J Clin Microbiol, 1997, 35: 1595-1596.
30. Arends JP, Zanen HC. Meningitis caused by Streptococcus suis in humans. Rev Infect Dis, 1988, 10: 131-137.
31. Beaudoin M, Harel J, Higgins R, Gottschalk M, Frenette M, MacInnes JI. Molecular analysis of isolates of Streptococcus suis capsular type 2 by restriction-endonuclease-digested DNA separated on SDS-PAGE and by hybridization with an rDNA probe. J Gen Microbiol, 1992, 138:2639-2645.
32. Benga L, Goethe R, Rohde M, Valentin-Weigand P. Non-encapsulated strains reveal novel insights in invasion and survival of Streptococcus suis in epithelial cells. Cell Microbiol, 2004a, 6:867-881.
33. Benga L, Goethe R, Beilage EG, Valentin-Weigand P. Immunogenicity of Murein-associated Proteins from Temperature-stressed Streptococcus suis Cultures. J Vet Med, 2004b, 51,272-277.
34. Bensaid T, Bonnefoi-Kyriacou B, Dupel-Pottier C, Bellon O, Lagier E, Chardon H. Streptococcus suis meningitis after wild boar hunting. Presse Med, 2003, 32:1077-1078.
35. Bentley RW, Leigh JA, Collins M D. Intrageneric structure of Streptococcus based on comparative analysis of small-subunit rRNA sequences. Int J Syst Bacteriol, 1991, 41:487-494.
36. Berry AM, Lock RA, Thomas SM, Rajan DP, Hansman D, Paton JC. Cloning and nucleotide sequence of the Streptococcus pneumoniae hyaluronidase gene and purification of the enzyme from recombinant Escherichia coli. Infect Immun, 1994, 62:1101-1108.
37. Berry AM, Paton JC. Additive attenuation of virulence of Streptococcus pneumoniae by mutation of the genes encoding pneumolysin and other putative Pneumococcal virulence proteins. Infect Immun, 2000,68:133-40.
38. Berthelot-Herault F, Morvan H, Keribin AM, Gottschalk M, Kobisch M. Production of muramidase released protein (MRP ), extracellular factor (EF) and haemolysin by field isolates of Streptococcus suis capsular type 2, 1/2, 9, 7 and 3 isolated from swine in France. Vet Res, 2000, 31:473-479.
39. Berthelot-Herault F, Marois C, Gottschalk M, Kobisch M. Genetic diversity of Streptococcus suis strains isolated from pigs and humans as revealed by pulsed-field gel electrophoresis. J Clin Microbiol, 2002,40:615-619.
40. Berthelot-Herault F, Gottschalk M, Morvan H, Kobisch M. Dilemma of virulence of Streptococcus suis: Canadian isolate 89-1591 characterized as a virulent strain using a standardized experimental model in pigs. Can J Vet Res, 2005,69:236-240.
41. Billington SJ, Jost BH, Songer JG Thiol-activated cytolysins: structure, function and role in pathogenesis. FEMS Microbiol Lett, 2000,182:197-205.
42. Bolken TC, Franke CA, Jones KF, Zeller GO, Jones CH, Dutton EK, Hruby DE. Inactivation of the srtA gene in Streptococcus gordonii inhibits cell wall anchoring of surface proteins and decreases in vitro and in vivo adhesion. Infect Immun, 2001, 69:75-80.
43. Brook I. Bacterial interference. Crit Rev Microbiol, 1999,25:155-172.
44. Brousseau R, Hill JE, Prefontaine G, Goh SH, Harel J, Hemmingsen SM. Streptococcus suis Serotypes Characterized by Analysis of Chaperonin 60 Gene Sequences. Appl Environ Mecrobiol, 2001, 67: 4828-4833.
45. Busque P, Higgins R, Caya F, Quessy S. Immunisation of pigs against Streptococcus suis serotype 2 infection using a live avirulent strain. Can J Vet Res, 1997, 61:275-279.
46. Busque P, Higgins R, Senechal S, Marchand R, Quessy S. Simultaneous flow cytometric measurement of Streptococcus suis phagocytosis by polymorphonuclear and mononuclear blood leukocytes. Vet Microbiol, 1998,63:229-38.
47. Calvinho LF, Almeida RA, Oliver SP. Potential virulence factors of Streptococcus dysgalactiae associated with bovine mastitis. Vet Microbiol, 1998; 61:93-110.
48. Cantin M, Harel J, Higgins R, Gottschalk M. Antimicrobial resistance patterns and plasmid profiles of Streptococcus suis isolates. J Vet Diagn Invest, 1992,4:170-174.
49. Cerami A. Inflammatory cytokines. Clin Immunol Immunopathol, 1992,62:S3-10.
50. Chabot-Roya G, Willsonb P, Seguraa M, Lacouturea S, Gottschalk M. Phagocytosis and killing of Streptococcus suis by porcine neutrophils. Microbial Pathogenesis, 2006,41:21-32.
51. Chanter N, Jones PW, Alexander TJL. Meningitis in pigs caused by Streptococcus suis-a speculative review. Vet Microbiol, 1993, 36:39-55.
52. Chanter N, Collin N, Holmes N, Binns M, Mumford J. Characterization of the Lancefield group C streptococcus 16S-23S RNA gene intergenic spacer and its potential for identification and sub-specific typing. Epidemiol Infect, 1997; 118:125-135.
53. Charland N, Harel J, Kobisch M, Lacasse S, Gottschalk M. Streptococcus suis serotype 2 mutants deficient in capsular expression. Microbiology, 1998, 144:325-332.
54. Charland N, Nizet V, Rubens CE, Kim KS, Lacouture S, Gottschalk M. Streptococcus suis serotype 2 interactions with human brain microvascular endothelial cells. Infect Immun, 2000,68:637-643.
55. Chatellier S, Harel J, Zhang Y, Gottschalk M, Higgins R, Devriese LA, Brousseau R. Phylogenetic diversity of Streptococcus suis strains of various serotypes as revealed by 16S rRNA gene sequence comparison. Int J Syst Bacteriol, 1998,48:581-589.
56. Chatellier S, Gottschalk M, Higgins R, Broussear R, Harel J. Relatedness of Streptococcus suis Serotype 2 Isolates from Different Geographic Origins as Evaluated by Molecular Fingerprinting and Phenotyping, J Clin Microbiol, 1999, 37: 362-366.
57. Chengappa MM, Pace LW, Williams JA, Herrin CH, Ascher SE. Efficacy of tiamulin against experimentally induced Streptococcus suis. J Am Vet Med Assoe, 1990, 197: 1467-1470.
58. Cleary PP. Characterization of prototype and clinically defined strains of Streptococcus suis by genomic fingerprinting. J Clin Microbiol, 1990, 28: 462-2466.
59. Clifton Hadley FA. Streptococcus suis type 2 infections. Br Vet J, 1983, 139: 1-5.
60. Clifton Hadley FA. Studies of Streptococcus suis type 2 infection in pigs. Vet Res Commun, 1984a, 8: 217-227.
61. Clifton Hadley FA, Alexander TJ, Enright MR, Guise J. Monitoring herds for Streptococcus suis type 2 by sampling tonsils of slaughter pigs. Vet Ree, 1984b, 115: 562-564.
62. Cloutier G, D'Allaire S, Martinez G, Surprenant C, Lacouture S, Gottschalk M. Epidemiology of Streptococcus suis serotype 5 infection in a pig herd with and without clinical disease. Vet Microbiol, 2003; 97:135-151.
63. Cohen J. The immunopathogenesis of sepsis. Nature, 2000, 420: 885-891.
64. Confalonieri F, Duguet M. A 200-amino acid ATPase module in search of a basic function. Bioessays, 1995, 17: 639-650.
65. Costa AT, Lobato FC, Abreu VL, Assis RA, Reis R, Uzal FA. Serotyping and evaluation of the virulence in mice of Streptococcus suis strains isolated from diseased pigs. Rev Inst Med Trop Sao Paulo, 2005, 47: 113-115
66. Courtney HS, Li Y, Dale JB, Hasty DL. Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci. Infect Immun, 1994, 62: 3937-3946.
67. Davies PR, Ossowicz CJ. Evaluation of methods used for detecting Streptococcus suis type 2 in tonsils, and investigation of the carrier state in pigs. Res Vet Sci, 1991, 50: 190-194.
68. de Greeff A, van Alphen L, Smith HE. Selection of Recombinant Antibodies Specific for Pathogenic Streptococcus suis by Subtractive Phage Display. Infect Immun, 2000, 68: 3949-3955.
69. de Greeff A, Buys H, Verhaar R, Dijkstra J, van Alphen L, Smith HE. Contribution of Fibronectin-Binding Protein to Pathogenesis of Streptococcus suis Serotype 2. Infect Immun, 2002, 70: 1319-1325.
70. del Campo Sepulveda EM, Altman E, Kobisch M. Detection of antibodies against Streptococcus suis capsular type 2 using a purified capsular polysaccharide antigen-based indirect ELISA. Vet Microbiol, 1996, 52: 113-125.
71. Denchi EL, Helin K. E2F1 is crucial for E2F-dependent apoptosis. EMBO Pep, 2005, 6: 661-668.
72. Devriese LA, Sustronck B, Maenhouth T, Haesebrouck F. Streptococcus suis meningitis in a horse. Vet Rec, 1990, 127: 68.
73. Devriese LA, HaesebrouckF, de Herdt P, Dom P, Ducatelle R, Desmidt M, Messier S, Higgins R. Streptococcus suis infections in birds. Avian Pathol, 1994, 23: 721-724.
74. Didi Baev, Seung-Ho Ohk, Howard K. Kuramitsu. Protein interactions of SGP, an essential Streptococcus mutans GTPase, revealed by biochemical and yeast two-hybrid system analyses. FEMS Microbiology Letters, 2000, 184: 149-153.
75. Dixon EP, Johnstone EM, Lin X, Little SB. An inverse mammalian two-hybrid system for beta secretase and other proteases. Anal Biochem, 1997, 249: 239-241.
76. Fan Z, Zhuo Y, Tan X, Zhou Z, Yuan J, Qiang B, Yan J, Peng X, Gao GF. SARS-CoV Nucleocapsid Protein Binds to hUbe9, a Ubiquitin Conjugating Enzyme of the Sumoylation System. J Med Virol, 2006, 78: 1365-1373.
77. Fashena SJ, Serebriiskii I, Golemis EA. The continued evolution of two-hybrid screening approaches in yeast: how to outwit different preys with different baits. Gene, 2000, 250: 1-14.
78. Feder I, Chengappa MM, Fenwick B, Rider M, Staats J. Partial characterization of Streptococcus suis type 2 hemolysin. J Clin Microbiol, 1994, 32: 1256-1260.
79. Fields, S. and Song, O. A novel genetic system to detect protein-protein interactions. Nature, 1989, 340: 245-246.
80. Fischetti VA, Paneholi V, Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from Grampositive cocci. Mol Microbiol, 1990, 4: 1603-1605.
81. Francois B, Gissot V, Ploy MC, Vignon P. Recurrent Due to Streptococcus suis. J Clin Microbiol, 1998, 36: 2395.
82. Galina L, Vecht U, Wisselink HJ, Pijoan C. Prevalence of various phenotypes of Streptococcus suis isolated from swine in the U. S. A. based on the presence of muraminidase-released protein and extracellular factor. Can J Vet Res, 1996, 60: 72-74.
83. Gogolewski RP, Cook RW, O'Connell CJ. Streptococcus suis serotypes associated with disease in weaned pigs. Aust Vet J, 1990, 67: 202-204.
84. Gottschalk M, Lebrun A, Jacques M, Higgins R. Hemagglutination properties of Streptococcus suis. J Clin Microbiol, 1990, 28: 2156-2158.
85. Gottschalk M, Higgins R, Boudreau M. Use of polyvalent coagglutination reagents for serotyping of Streptococcus suis. J Clin Microbiol, 1993, 31: 2192-2194.
86. Gottschalk M, Lacouture S, Dubreuil JD. Characterization of Streptococcus suis type 2 haemolysin. Microbiol, 1995, 141: 189-195.
87. Gottschalk M, Lebrun A, Wisselink H, Dubreuil JD, Smith H, Vecht U. Production of virulence-related proteins by Canadian strains of Streptococcus suis capsular type 2. Can J Vet Res, 1998; 62: 75-79.
88. Gottschalk M, Segura M. The pathogenesis of the meningitis caused by Streptococcus suis: the unresolved questions. Vet Microbiol, 2000, 76: 259-272.
89. Granlund M, Oberg L, Scum M, Norgren M. Identification of a novel insertion element, IS1548, in group B streptococci, predominantly in strains causing endocarditis. J Infect Dis, 1998, 177: 967-976.
90. Grawunder U, Wilm M, Wu X, Kulesza P, Wilson TE, Mann M, Lieber MR. Activity of DNA ligase IU stimulated by complex formation with XRCC4 protein in mammalian cells. Nature, 1997, 388: 492-495.
91. Grimont F, Grimont PAD. Ribosomal ribonucleic acid gene restriction patterns as potential taxonomic tbols. Ann Inst Pasteur Microbiol, 1986, 137B: 165-175.
92. Gunther B, Ozegowski JH, Kohler W. Occurrence of extracellular hyaluronic acid and hyaluronate lyase in streptococci of groups A, B, C, and G. Zentralbl Bakteriol, 1996, 285: 64-73.
93. Halbur PG, Thanawongnuwech R, Brown G, Kinyon J, Roth J, Thacker E, Thacker B. Efficacy of antimicrobial treatments and vaccination regimens for control of porcine reproductive and respiratory syndrome virus and Streptococcus suis coinfection of nursery pigs. J Clin Microbiol, 2000, 38: 1156-1160.
94. Hara M, Akasaka K, Akinaga S, Okabe M, Nakano H, Gomez R, Wood D, Uh M, Tamanoi F. Identification of Ras Famesyltransferase Inhibitors by Microbial Screening. Proc Natl Acid Sci, USA, 1993, 90: 2281-2285.
95. Harel J, Higgins R, Gottschalk M, Bigras-Ppoulin M. Genomic relatedness among reference strains of different Streptococcus suis serotypes. Can J Vet Res, 1994, 58: 259-262.
96. Harel J, Martinez G, Nassar A, Dezfulian H, Labile SJ, Brousseau R, Moineau S, Gottschalk M. Identification of an Inducible Bacteriophage in a Virulent Strain of Streptococcus suis Serotype 2. Infect Immun, 2003, 71: 6104-6108.
97. Hassan AA, Khan IU, Abdulmawjood A, Lammler C. Inter- and intraspecies variations of the 16S-23S rDNA intergenic spacer region of various streptococcal species. Syst Appl Microbiol, 2003, 26: 97-103.
98. Heath PJ, Hunt BW. Streptococcus suis serotypes 3 to 28 associated with disease in pigs. Vet Rec, 2001, 148: 207-208.
99. Heath PJ, Hunt BW, Duff JP, Wilkinson JD. Streptococcus suis serotype 14 as a cause of pig disease in the UK. Vet Rec, 1996, 139: 450-451.
100. Heidt MC, Mohamed W, Hain T, Vogt PR, Chakraborty T, Domann E. Human Infective Endocarditis Caused by Streptococcus suis Serotype 2. J Clin Microbiol, 2005, 43: 4898-4901.
101. Helin K. Regulation of cell proliferation by the E2F transcription factors. Curr Opin Genet Dev, 1998, 8: 28-35.
102. Hensel M, Shea JE, Gleeson C, Jones MD, Dalton E, Holden DW. Simultaneous identification of bacterial virulence genes by negative selection. Science, 1995, 269: 400-403.
103. Higgins R, Gottschalk M, Beaudoin M, Rawluk SA. Distribution of Streptococcus suis capsular types in Quebec and western Canada. Can Vet J, 1992, 33: 27-30.
104. Higgins R, Gottschalk M. Distribution of the Streptococcus suis capsular types in 1999. Can Vet J, 2000, 41: 414.
105. Hill JE, Gottschalk M, Brousseau R, Harel J, Hemmingsen SM, Goh SH. Biochemical analysis, cpn60 and 16S rDNA sequence data indicate that Streptococcus suis serotypes 32 and 34, isolated from pigs, are Streptococcus orisratti. Vet Microbiol, 2005, 107: 63-69.
106. Holt ME, Enright MR, Alexander TJ. Immunisation of pigs with live cultures of Streptococcus suis type 2. Rev Vet Sci, 1988, 45: 349-352.
107. Holt ME, Enright MR, Alexander TJ. Immunisation of pigs with killed cultures of Streptococcus suis type 2. Rev Vet Sci, 1990, 48:23-27.
108. Homer K, Shain H, Beighton D. The role of hyaluronidase in growth of Streptococcus intermedius on hyaluronate. Adv Exp Med Biol, 1997, 418: 681-683.
109. Homer KA, Denbow L, Whiley R.A, Beighton D. Chondroitin sulfate depolymerase and hyaluronidase activities of viridans streptococci determined by a sensitive spectrophotometric assay. J Clin Microbiol, 1993, 31: 1648-1651.
110. Hommez J, Willepit J, Cassimon O, Castryck F, Ceyssens K, Devriese LA. Streptococcus suis and other streptococcal species as a cause of extramammary infection in ruminants. Vet Rec, 1988, 123: 626-627.
111. Hornish RE, Kotarski SF. Cephalosporins in veterinary medicine-Ceftiofur use in food animals. Curr Top Med Chem, 2002, 2: 717-731.
112. Hu X, Zhu F, Wang H, Chen S, Wang G. Studies on human streptococcal infectious syndrome caused by infected pigs. Zhonghua Yu Fang Yi Xue Za Zhi, 2000, 34: 150-152.
113. Hua SB, Luo Y, Qiu M, Chan E, Zhou H, Zhu L. Construction of a modular yeast two-hybrid cDNA library from human EST clones for the human genome protein linkage map. Gene, 1998, 215: 143-152.
114. Huang J and Schreiber SL. A yeast genetic system for selecting small molecule inhibitors of protein-protein interactions in nanodroplets. Proc Natl Acid Sci USA, 1997, 94: 13396-13401.
115. Huang YT, Teng LJ, Ho SW, Hsueh PR. Streptococcus suis infection. J Microbiol Immunol Infect, 2005, 58: 306-313.
116. Huang SH, Stins MF, Kim KS. Bacterial penetration across the blood-brain barrier during the development of neonatal meningitis. Microbes Infect, 2000, 2: 1237-1244.
117. Hynes WL, Walton SL. Hyaluronidases of Gram-positive bacteria. FEMS Microbiol Lett, 2000, 183: 201-207.
118. Ito T, Chiba T, Ozawa R, Yoshida M, Hattori M, Sakaki Y. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci, 2001, 98: 4569-4574.
119. Jack RW, Tagg JR, Ray B. Bacteriocins of gram-positive bacteria. Microbiol Rev, 1995, 59: 171-200.
120. Jackson MW and Piano GV. Interactions between type Ⅲ secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system. FEMS Microbiology Letters, 2000, 86: 85-90.
121. Jacobs AAC, Loeffen PLW, van den Berg AJG, Storm PK. Identification, purification, and characterization of a thiol-activated hemolysin (suilysin) of Streptococcus suis. Infect Immun, 1994, 62: 1742-1748.
122. Jacobs AAC, van den Berg AJG, Loeffen PLW. Protection of experimentally infected pigs by suilysin, the thiol-activated haemolysin of Streptococcus suis. Vet Rec, 1996, 139: 225-228.
123. Jacques M, Gottschalk M, Foiry B, Higgins R. Ultrastructural study of surface components of Streptococcus suis. J Bacteriol, 1990, 172: 2833-2838.
124. Joh D, Wann ERW, Kreikemeyer B, Speziale P, Hook M. Role of fibronectin-binding MSCRAMMS in bacterial adherence and entry into mammalian cells. Matrix Biol, 1999, 18: 211-223.
125. Karimova G, Pidoux J, Ullmann A, Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. 1998, Proc Natl Acad Sci USA, 95: 5752-5756.
126. Karimova G, Ladant D, Ullmann A. Two-hybrid systems and their usage in infection biology. Int J Med Microbiol, 2002,292:17-25.
127. Kataoka Y, Yoshida T, Sawada T. A 10-year survey of antimicrobial susceptibility of Streptococcus suis isolates from swine in Japan. J Vet Med Sci, 2000, 62:1053-1057.
128. Kim JW, Cho HS, Kim JH, Hur SY, Kim TE, Lee JM, Kim IK, Namkoong SE. AAC-11 overexpression induces invasion and protects cervical cancer cells from apoptosis. Lab Invest, 2000, 80: 587-594.
129. King SJ, Heath PJ, Luque I, Tarradas C, Dowson CG, Whatmore AM. Distribution and Genetic Diversity of Suilysin in Streptococcus suis Isolated from Different Diseases of Pigs and Characterization of the Genetic Basis of Suilysin Absence. Infect Immun, 2001,12: 7572-7582.
130. King SJ, Leigh JA, Heath PJ, Luque I, Tarradas C, Dowson CG, Whatmore AM. Development of a Multilocus Sequence Typing Scheme for the Pig Pathogen Streptococcus suis: Identification of Virulent Clones and Potential Capsular Serotype Exchange. J Clin Microbiol, 2002,40:3671-3680.
131. Kiston J, Raven T, Yingping J, et al. A deathdomain-containing receotor that mediates apoptosis. Nature, 1996,384:372-375.
132. Lalonde M, Segura M, Lacouture S, Gottschalk M. Interactions between Streptococcus suis serotype 2 and different epithelial cell lines. Microbiol, 2000, 146:1913-1921.
133. Li B and Fields S. Identification of mutations in p53 that affect its binding to SV40 large T antigen by using the yeast two-hybrid system. FASEB J, 1993,7:957-963.
134. Ling EWY, Noya FJD, Ricard G, Beharry K, Mills EL, Aranda JV. Biochemical mediators of meningeal inflammatory response to group B Streptococcus in the newborn piglet model. Pediatr Res, 1995,38:981-987.
135. Lun S, Perez-Casal J, Connor W, Willson PJ. Role of suilysin in pathogenesis of Streptococcus suis capsular serotype 2. Microbiol Pathogen, 2003, 34:27-37.
136. Lun S, Willson PJ. Expression of green fluorescent protein and its application in pathogenesis studies of serotype 2 Streptococcus suis. J Microbiol Methods, 2004, 56:401-412.
137. Mannan AU, Krawen P, Sauter SM, Boehm J, Chronowska A, Paulus W, Neesen J, Engel W. ZFYVE 27 (SPG33) , a Novel Spastin-Binding Protein, Is Mutated in Hereditary Spastic Paraplegia. Am J Hum Genet, 2006, 79: 351-357.
138. Marois C, Bougeard S, Gottschalk M, Kobisch M. Multiplex PCR Assay for Detection of Streptococcus suis Species and Serotypes 2 and 1/2 in Tonsils of Live and Dead Pigs. J Clin Microbiol, 2004,42: 3169-3175.
139. Marois C, Devendec LL, Gottschalk M, Kobisch M. Molecular characterization of Streptococcus suis strains by 16S-23S intergenic spacer polymerase chain reaction and restriction fragment length polymorphism analysis. Can J Vet Res, 2006, 70: 94-104.
140. Martel A, Baele M, Devriese LA, Goossens H, Wisselink HJ, Decostere A, Haesebrouck F. Prevalence and mechanism of resistance against macrolides and lincosamides in Streptococcus suis isolates. Vet Microbiol, 2001, 83: 287-297.
141. Martinez G, Harel J, Lacouture S, Gottschalk M. Genetic diversity of Streptococcus suis serotypes 2 and 1/2 isolates recovered from carrier pigs in closed herds. Can J Vet Res, 2002, 66: 240-248.
142. McCraith S, Holtzman T, Moss B, fields S. Genome-wide analysis of vaccine virus protein-protein interactions. Proc Natl Acid Sci USA, 2000, 97: 4879-4884.
143. Melancon D, Grenier D. Production and Properties of Bacteriocin-Like Inhibitory Substances from the Swine Pathogen Streptococcus suis Serotype 2. App Environ Microbiol, 2003, 69: 4482-4488.
144. Melegari M, Scaglionip P, Wands JR. Cloning and characterization of a novel hepatitis B virus X binding protein that inhibits viral replication. J virology, 1998, 72: 1737-1743.
145. Mogollon JD, Pijoan C, Murtaugh MP, Kaplan EL, Collins JE, Cleary PP. Characterization of prototype and clinically defined strains of Streptococcus suis by genomic fingerprinting. J Clin Microbiol, 1990, 28: 2462-2466.
146. Morris EJ, Michaud WA, Ji JY, Moon NS, Rocco JW, Dyson NJ. Functional Identification of Api 5 as a Suppressor of E2F-Dependent Apoptosis In Vivo. Plos Genet, 2006, 2:e196.
147. Muller-Alouf H, Carnoy C, Simonet M, Alouf JE. Superantigen bacterial toxins: state of the art. Toxicon, 2001, 39: 1691-1701.
148. Muller G, Nielsen G, Baigent CL. Electron microscopical particle counting in irology. Ⅲ. Parameters governing the efficiency of sedimentation techniques and its improvement with the application of poly-L-lysine. Arch Virol, 1980, 64: 311-318.
149. Murakami Y, Fukazawa H, Kobatake T, Yamagoe S, Takebe Y, Tobiume M, Matsuda M, Uehara Y. A mammalian two-hybrid screening system for inhibitors of interaction between H1V Nef and the cellular tyrosine kinase Hck. Antiviral Res. 2002, 55: 161-168.
150. Mwaniki CG, Robertson ID, Trott DJ, Atyeo RF, Lee BJ, Hampson DJ. Clonal analysis and virulence of Australian isolates of Streptococcus suis type 2. Epidemiol Infect, 1994, 113: 321-334.
151. Mwaniki CG, Robertson ID, Hampson DJ. The prevalence of Streptococcus suis type 2 in Western Australian piggeries. Aust Vet J, 1994,71:385-386.
152. Norton PM, Rolph C, Ward PN, Bentley RW, Leigh JA. Epithelial invasion and cell lysis by virulent strains of Streptococcus suis is enhanced by the presence of suilysin. FEMS Immunol Med Microbiol, 1999,26:25-35.
153. Okwumabua O, Staats J, Chengappa MM. Detection of genomic heterogeneity in Streptococcus suis isolates by DNA restriction fragment length polymorphisms of rRNA genes (ribotyping) . J Clin Microbiol, 1995,33:968-972.
154. Okwumabua O, Abdelmagid O, Chengappa MM. Hybridization analysis of the gene encoding a hemolysin (suilysin) of Streptococcus suis type 2: evidence for the absence of the gene in some isolates. FEMS Microbiol Lett, 1999, 181:113-121.
155. Oliveira S, Batista L, Torremorell M, Pijoan C. Experimental colonization of piglets and gilts with systemic strains of Haemophilus parasuis and Streptococcus suis to prevent disease. Can J Vet Res, 2001,65:161-167.
156. Osaki M, Takamatsu D, Shimoji Y, Sekizaki T. Characterization of Streptococcus suis Genes Encoding Proteins Homologous to Sortase of Gram-Positive Bacteria. J Bacteriol, 2002,184:971-982.
157. Osikowicz G, Beggs M, Brookhart P, Caplan D, Ching S, Eck P, Gordon J, Richerson R, Sampedro S, Stimpson D, et al. One-step chromatographic immunoassay for qualitative determination of choriogonadotropin in urine. Clin Chem. 1990, 36:1586
158. Owen RJ. Chromosomal DNA fingerprinting: a new method of species and strain identification applicable to microbial pathogens. J Med Microbiol, 1989, 30:89-99.
159. Page AL, Fromont-Racine M, Sansonetti P, Legrain P, Parsot C. Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri. Mol Microbiol, 2001,42:1133 -1145.
160. Pallares FJ, Schmitt CS, Roth JA, Evans RB, Kinyon JM, Halbur PG Evaluation of a ceftiofur-washed whole cell Streptococcus suis bacterin in pigs. Can J Vet Res, 2004, 68:236-240.
161. Pedroli S, Kobisch M, Beauchet O, Chaussinand JP, Lucht F. Streptococcus suis bacteremia. Presse Med, 2003, 32:599-601.
162. Perch B, Kristjansen P, Skadhauge K. Group R Streptococci pathogenic for man: two cases of meningitis and one fatal case of sepsis. Acta Pathol Microbiol Scand, 1968, 74:69-76.
163. Perch B, Pedersen KB, Henrichsen J. Serology of capsulated streptococci pathogenic for pigs: six new serotypes of Streptococcus suis. J Clin Microbiol, 1983, 17:993-996.
164. Rasmussen SR, Aarestrup FM, Jensen NE, Jorsal SE. Associations of Streptococcus suis Serotype 2 Ribotype Profiles with Clinical Disease and Antimicrobial Resistance. J Clin Microbiol, 1999, 37: 404-408.
165. Reid SM, Ferris NP, Bruning A, Hutchings GH, Kowalska Z, kerblom LA. Development of a rapid chromatographic strip test for the pen-side detection of foot-and-mouth disease virus antigen .J Virolog Methods, 2001, 96:189-202.
166. Robertson ID, Blackmore DK. Prevalence of Streptococcus suis types 1 and 2 in domestic pigs in Australia and New Zealand. Vet Rec, 1989, 124:391-394.
167. Rolland K, Marois C, Siquier V, Cattier B, Quentin R. Genetic features of Streptococcus agalactiae strains causing severe neonatal infections, as revealed by pulsed-field gel electrophoresis and hy1B gene analysis. J Clin Microbiol, 1999, 37:1892-1898.
168. Rosenkranz M, Elsner HA, Sturenburg HJ, Weiller C, Rother J, Sobottka I. Streptococcus suis meningitis and septicemia contracted from a wild boar in Germany. J Neurol, 2003, 250: 869-870.
169. Salasia SI, Lammler C. Distribution of serotype, virulence markers and further characteristics of Streptococcus suis isolates from pigs. Zentralbl Veterinarmed B, 1995, 42, 78-83.
1670. Salles MW. Perez-Casal J, Willson P, Middleton DM. Changes in the leucocyte subpopulations of the palatine tonsillar crypt epithelium of pigs in response to Streptococcus suis type 2 infection. Vet Immunol Immunopathol, 2002, 87:51-63.
171. Sanford SE. Gross and histopathological findings in unusual lesions caused by Streptococcus suis in pigs. Ⅱ. Central nervous system lesions. Can J Vet Res, 1987, 51: 486-489.
172. Sasaki H, Moriyama S, Yuldue H, Kobayashi Y, Nakashima Y, Kaji M, Fukai I, Kiriyama M, Yamakawa Y, Fujii Y.. Expression of the antiapoptosis gene, AAC-11, as a prognosis marker in non-small cell lung cancer. Lung Cancer, 2001, 34: 53-57.
173. Saukkonen K, Sande S, Cioffe C, Wolpe S, Sherry B, Cerami A, Tuomanen E. The role of cytokines in the generation of inflammation and tissue damage in experimental gram-positive meningitis. J Exp Med, 1990, 171: 439-448.
174. Schaufuss P, Sting R, Schaeg W, Blobel H. Isolation and characterization of hyaluronidase from Streptococcus uberis. Zentralbl Bakteriol, 1989, 271: 46-53.
175. Schlegel L, Grimont F, Grimont PA, Bouvet A. Identification of major streptococcal species by rrn-amplified ribosomal DNA restriction analysis. J Clin Microbiol, 2003, 41: 657-666.
176. Schneewind O, Model P, Fischetti VA. Sorting of protein A to the staphylococcal cell wall. Cell, 1992,70:267-281.
177. Seddon SV, Hemingway I, Borriello SP. Hydrolytic enzyme production by Clostridium difficile and its relationship to toxin production and virulence in the hamster model. J Med Microbiol, 1990, 31:169-74.
178. Segers RP, Kenter T, de Haan LA, Jacobs AA. Characterisation of the gene encoding suilysin from Streptococcus suis and expression in field strains. FEMS Microbiol Lett, 1998,167:255-61.
179. Segura M, Cleroux P, Gottschalk M. Streptococcus suis and group B Streptococcus differ in their interactions with murine macrophages. FEMS Immunol Med Microbiol, 1998,21:189-195.
180. Segura M, Stankova J, Gottschalk M. Heat-Killed Streptococcus suis Capsular Type 2 Strains Stimulate Tumor Necrosis Factor Alpha and Interleukin-6 Production by Murine Macrophages. Infect Immun, 1999,67:4646-4654.
181. Segura M, Gottschalk M. Streptococcus suis interactions with the murine macrophage cell line J774: adhesion and cytotoxicity. Infect Immun, 2002, 70:4312-4322.
182. Segura M, Gottschalk M. Extracellular virulence factors of streptococci associated with animal diseases. Front Biosci, 2004a, 9:1157-1188.
183. Segura M, Gottschalk M, Olivier M. Encapsulated Streptococcus suis inhibits activation of signaling pathways involved in phagocytosis. Infect Immun, 2004b, 72:5322-5330.
184. Sekizaki T, Otani Y, Osaki M, Takamatsu D, Shimoji Y. Evidence for horizontal transfer of SsuDAT1I restriction-modification genes to the Streptococcus suis genome. J Bacteriol, 2001,183:500-511.
185. Shaver YJ, Nagpal ML, Rudner R, Nakamura LK, Fox KF, Fox A. Restriction fragment length polymorphism of rRNA operons for discrimination and intergenic spacer sequences for cataloging of Bacillus subtilis sub-groups. J Microbiol Methods, 2002,50:215-223.
186. Silva LMG, Baums CG, Rehm T, Wisselink HJ, Goethe R, Valentin-Weigand P. Virulence-associated gene profiling of Streptococcus suis isolates by PCR. Vet Microbiol, 2006,115:117-127.
187. Slater JD, Allen AG, May JP, Bolitho S, Lindsay H, Maskell DJ. Mutagenesis of Streptococcus equi and Streptococcus suis by transposon Tn917. Vet Microbiol, 2003, 93:197-206.
188. Smith HE, Vecht U, Gielkens AL, Smits MA. Cloning and nucleotide sequence of the gene encoding the 136-kilodalton surface protein (muramidase-released protein) of Streptococcus suis type 2. Infect Immun, 1992, 60:2361-2367.
189. Smith HE, Vecht U, Wisselink H J, Stockhofe-Zurwieden N, Biermann Y, Smits MA. Mutants of Streptococcus suis types 1 and 2 impaired in expression of muramidase-released protein and extracellular protein induce disease in newborn germfree pigs. Infect Immun, 1996, 64:4409-4412.
190. Smith HE, Rijnsburger M, Stokhofe-zurwieden N, Wisselink HJ, Vecht U, Smits MA. Virulent Strains of Streptococcus suis Serotype 2 and Highly Virulent Strains of Streptococcus suis Serotype 1 Can Be Recognized by a Unique Ribotype Profile. J Clin Mierobiol, 1997, 35: 1049-1053.
191. Smith HE, Damman M, van der Velde J, Wagenaar F, Wisselind HJ, Stockhofe-zurwieden N, Smits MA. Identification and Characterization of the cps Locus of Streptococcus suis Serotype 2: the Capsule Protects against Phagocytosis and Is an Important Virulence Factor. Infect Immun, 1999, 67: 1750-1756.
192. Smith HE, Buijs H, Wisselink HJ, Stockhofe-Zurwieden N, Smits MA. Selection of Virulence-Associated Determinants of Streptococcus suis Serotype 2 by In Vivo Complementation. Infect Immun, 2001, 69: 1961-1966.
193. Sorensen NS, Tegtmeier Ca, Andresen LO, Pineiro M, Toussaint MJM, Campbell FM, Lampreave F, Heegaard PMH. The porcine acute phase protein response to acute clinical and subclinical experimental infection with Streptococcus suis. Vet Immunol Immunopathol, 2006, 113: 157-168.
194. Sprenger H, Rosier A, Tonn P, Braune HJ, Huffmann G, Gemsa D. Chemokines in the cerebrospinal fluid of patients with meningitis. Clin Immunol Immunopathol, 1996, 80: 155-161.
195. Sriskandan S, Slater JD. Invasive Disease and Toxic Shock due to Zoonotic Streptococcus suis: An Emerging Infection in the East?. Plos Med, 2006, 3:e187.
196. Staats JJ, Plattner BL, Nietfeld J, Dritz S, Chengappa MM. Use of ribotyping and hemolysin activity to identify highly virulent Streptococcus suis type 2 isolates. J Clin Microbiol, 1998, 36: 15-19.
197. Staats JJ, Feder I, Okwumabua O, Chengappa MM. Streptococcus suis: past and present. Vet Res Commun, 1997, 21: 381-407.
198. Staudinger J, Zhou J, Olson EN, et al. PICK1:a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system. J cell Biol, 1995, 128: 263-271.
199. Stein E, Huynh-Do U, Daniel TO. Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase. J Biol Chem, 1998, 273: 1303-1308.
200. Stenmark H, Aasland R. FYVE-finger proteins-effectors of an inositol lipid. J Cell Sci, 1999, 112: 4175-4183.
201. Stenmark H, Aasland R, Driscoll PC. The phosphatidylinositol 3-phosphate-binding FYVE finger. FEBS Lett, 2002, 513: 77-84.
202. Stevens C, La Thangue NB. The emerging role of E2F-1 in the DNA damage response and checkpoint control. DNA Repair (Amst), 2004, 3: 1071-1079.
203. Strangmann E, Froleke H, Kohse KP. Septic shock caused by Streptococcus suis: Case report and investigation of a risk group. Int J Hyg Environ Health, 2002, 205: 385-392.
204. Stull TL, Lilipuma JJ, Edlind TD. A broad spectrum probe for molecular epidemiology of bacteria: ribosomal RNA. J Infect Dis, 1988, 157:280-286.
205. Takamatsu D, Osaki M, Sekizaki T. Evidence for Lateral Transfer of the Suilysin Gene Region of Streptococcus suis. J Bacterial, 2002, 184: 2050-2057.
206. Tang J, Wang C, Feng Y, Yang W, Song H, Chen Z, Yu H, Pan X, Zhou X, Wang H, Wu B, Wang H, Zhao H, Lin Y, Yue J, Wu Z, He X, Gao F, Khan AH, Wang J, Zhao G, Wang Y, Wang X, Chen Z, Gao GF. Streptococcal toxic shock syndrome caused by Streptococcus suis serotype 2. PLoS Med, 2006, 3: e151.
207. Tarradas C, Luque I, de Andres D, Abdel-Aziz Shahein Ye, Pons P, Gonzalez F, Borge C, Perea A. Epidemiologieal relationship of human and swine Streptococcus suis isolates. J Vet Med B Infect Dis Vet Public Health, 2001, 48: 347-355.
208. Tarradas C, Arenas A, Maldonado A, Luque I, Miranda A, Perea A. Identfication of Streptococcus suis isolated from swine: proposal for biochemical parameters. J Clin Microbiol, 1994, 32: 578-580.
209. Tarradas C, Borge C, Arenas A, Maldonado A, Astorga R, Miranda A, Luque I. Suilysin production by Streptococcus suis isolated from diseased and healthy carrier pigs in Spain. Vet Rec, 2001, 148: 183-184.
210. Tewari M, Yu M, Ross B, Dean C, Giordano A, Rubin R. AAC-11, a novel cDNA that inhibits apoptosis after growth factor withdrawal. Cancer Res, 1997, 57: 4063-4069.
211. Thompson C, Merrilf AR, Mangroo D. Identification of peptide inhibitors of Pseudomonas aeruginosa exotoxin A function using a yeast two-hybrid approach. FEMS Microbiol Lett, 2003, 218: 85-92.
212. Tipper DJ, Strominger JL. Biosynthesis of the peptidoglycan of bacterial cell walls. Ⅻ. Inhibition of cross-linking by penieillins and cephalosporins: studies in Staphylococcus aureus in vivo. J Biol Chem, 1968, 243: 3169-3179.
213. Ton-That H, Liu G, Mazmanian SK, Faull KF, Schneewind O. Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proc Natl Acad Sci USA, 1999, 96: 12424-12429.
214. Ton-That H, Mazmanian SK, Faull KF, Schneewind O. Anchoring of surface proteins to the cell wall of Staphylococcus aureus Sortase-catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH2-GIy3 substrates. J Biol Chem, 2000, 275: 9876-9881.
215. Torremorell M, Pijoan C. Prolonged persistence of an epidemic Streptococcus suis strain in a closed pig population. Vet Rec, 1998, 143: 394-395.
216. Townsend GC, Scheld WM. Microbe-endothelium interactions in blood-brain barrier permeability during bacterial meningitis. ASM News, 1995, 61:294-298.
217. Trottier S, Higgins R, Brochu G, Gottschalk M. A case of human endocarditis due to Streptococcus suis in North America. Rev Infect Dis, 1991, 13: 1251-1252.
218. Tuomanen E. Entry of pathogens into the central nervous system. FEMS Microbiol Rev, 1996, 18: 289-299.
219. Turgeon PL, Higgins R, Gottschalk M, Beaudoin M. Antimicrobial susceptibility of Streptococcus suis isolates. Br Vet J, 1994, 50:263-269.
220. Uetz P, Giot L, Cagney G, Mansfield TA, Judson RS, Knight JR, Lockshon D, Narayan V, Srinivasan M, Pochart P, Qureshui-Emili A, Li Y, Godwin B, Conover D, Kalbfleisch T, Vijayadamodar G, Yang M, Johnston M, Fields S, Rothberg JM. A comprehensive analysis of protien-protein interactions in Saccharomyces cerevisiae. Nature, 2000, 403: 623-627.
221. Vanier G, Segura M, Fried P, Lacouture S, Gottschalk M. Invasion of Porcine Brain Microvascular Endothelial Cells by Streptococcus suis Serotype 2. Infect Immun, 2004, 72: 1441-1449.
222. Vecht U, Wisselink HJ, Jellema ML, Smith HE. Identification of two proteins associated with virulence of Streptococcus suis type 2. Infect. Immun, 1991, 59: 3156-3162.
223. Vecht U, Wisselink HJ, van Dijk JE, Smith HE. Virulence of Streptococcus suis type 2 strains in newborn germfree pigs depend on phenotype. Infect Immun, 1992, 60: 550-556.
224. Vecht U, Arends JP, van der Molen EJ, van Leengoed LAMG. Differences in virulence between two strains of Streptococcus suis type 2 after experimentally induced infection of newborn germfree pigs. Am J Vet Res, 1989, 50: 1037-1043.
225. Vela AI, Goyache J, Tarradas C, Luque I, Mateos A, Moreno MA, Borge C, Perea JA, Dominguez L, Femandez-Garayzabal JF. Analysis of genetic diversity of Streptococcus suis clinical isolates from pigs in Spain by pulsed-field gel electrophoresis. J Clin Micmbiol, 2003, 41: 2498-2502.
226. Verhoef J, Mattsson E. The role of cytokines in gram-positive bacterial shock. Trends Mierobiol, 1995, 3: 136-140.
227. Verheijen R, Osswald IK, Dietrich R, Haasnoot W, Development of a One Step Strip Test for the Detection of (Dihydro) streptomycin Residues in Raw Milk. Food Agricul Immunol, 2000, 12: 31-40
228. Victor J. Torres, Mark S, McClain, Timothy L. Cover. Interactions between p-33 and p-55 domains of the Helieobacter pylori Vacuolating Cytotoxin (VacA). J Biol Chem, 2004, 279: 2324-2331.
229. Walhot AJ, Sordella R, Lu X, et al. Protein interaction mapping in C. elegans using protein involved in vulval development. Science, 2000, 287: 116-122.
230. Wen HW, Borejsza-Wysoeki W, Thomas R. DeCory TR, Durst RA. Development of a competitive liposome-based lateral flow assay for the rapid detection of the allergenic peanut protein Ara h1. Anal Bioanal Chem, 2005, 382: 1217-1226.
231. Williams AE, Blakemore WF. Pathogenesis of meningitis caused by Streptococcus suis type 2. J Infect Dis, 1990, 162: 474-481.
232. Wilson TL, Jeffers J, Rapp-Gabrielson VJ, Martin S, Klein LK, Lowery DE, Fuller TE. A novel signature-tagged mutagenesis system for Streptococcus suis serotype 2.Vet Microbiol, 2007, doi: 10.1016/j.vetmic.2006.12.025.
233. Wisselink HJ, Vecht U, Stockhofe-Zurwieden N, Smith HE. Protection of pigs against challenge with virulent Streptococcus suis serotype 2 strains by a muramidase-released protein and extracellular factor vaccine. Vet Rec, 2001, 148: 473-477.
234. Wisselink HJ, Reek FH, Vecht U, Stockhofe-Zurwieden N, Smits MA, Smith HE. Detection of virulent strains of Streptococcus suis type 2 and highly virulent strains of Streptococcus suis type 1 in tonsillar specimens of pigs by PCR. Vet Microbiol, 1999, 67: 143-157.
235. Wisselink HJ, Smith HE, Stockhofe-Zurwieden N, Peperkamp K, Vecht U. Distribution of capsular types and production of muramidase-released protein (MRP) and extracellular factor (EF) of Streptococcus suis strains isolated from diseased pigs in seven European countries. Vet Microbiol, 2000, 74: 237-248.
236. Wisselink HJ, Stockhofe-Zurwieden N, Hilgers L, Smith HE. Assessment of protective efficacy of live and killed vaccines based on a non-encapsulated mutant of Streptococcus suis type 2. Vet Microbiol, 2002, 84: 155-168.
237. Wisselink HJ, Veldman KT, Van den Eede C, Salmon SA, Mevius DJ. Quantitative susceptibility of Streptococcus suis strains isolated from diseased pigs in seven European countries to antimicrobial agents licensed in veterinary medicine. Vet Microbiol, 2006, 113: 73-82.
238. Woese CR. Bacterial evolution. Microbiol Rev, 1987, 51: 221-271.
239. Yang JX, Jin ML, Chen JF, Yang Y, Zheng P, Zhang AD, Song YF, Zhou HB, Chen HC. Development and evaluation of an immunochromatographic strip for detection of Streptococcus suis type 2 antibody. J Vet Diagn Invest, 2007, 19 (in press)
240. Yu H, Jing H, Chen Z, Zheng H, Zhu X, Wang H, Wang S, Liu L, Zu R, Luo L, Xiang N, Liu H, Liu X, Shu Y, Lee S, Chuang S, Wang Y, Xu J, Yang W, China SSG. Human Streptococcus suis outbreak, Sichuan, China. Emerg Infect Dis, 2006, 12: 914-920.
241. Zhang GP, Li QM, Yang YY, Guo JQ, Li XW, Deng RG, Xiao ZJ, Xing GX, Yang JF, Zhao D, Cai S J, Zang WM. Development of a one-step strip test for the diagnosis of chicken infectious bursal disease.Avian Dis. 2005, 49: 177-81.
242. Zhang GP, Guo JQ, Wang XN, Yang JX, Yang YY, Li QM, Li XW, Deng RG, Xiao ZJ, Yang JF, Xing GX, Zhao D. Development and evaluation of an immunochromatographic strip for trichinellosis detection. Vet Parasitol, 2006a, 137: 286-293.
243. Zhang GP, Wang XN, Yang JF, Yang YY, Xing GX, Li QM, Zhao D, Chai SJ, Guo JQ. Development of an immunochromatographic lateral flow test strip for detection of beta-adrenergic agonist Clenbuterol residues. J Immunol Methods, 2006b, 312: 27-33.
2．曹三杰，段丽丽，肖驰，文心田．猪2型链球菌毒力因子研究进展．中国人兽共患病学报，2007，23：89-91．
3．韩雪清，林祥梅，吴绍强，贾广乐，刘建，梅琳．猪链球菌2型多重PCR快速检测方法的建立．中国兽医科学，2006，36：112-117．
4．何孔旺，陆承平．猪链球菌2型的致病特性与毒力因子．中国兽医科技，2000，30(9)：17-20．
5．何孔旺，倪艳秀，王继春，何家惠，王伟峰，杨瑛，陆承平，林继煌．猪链球菌2型的分子流行病学研究．中国人畜共患病杂志，2002，18：45-47．
6．李金海，张东，石谦，李春，马孟根，陈斌，吴萱．四川猪2型链球菌病的PCR检测．四川畜牧兽医，2005，9：30-32．
7．李明，何孔旺，陆承平．检测两种猪源链球菌抗体间接ELISA方法的筛选与应用．中国人兽共患病杂志，2005．21：867-870．
8．刘军，冯书章，尹铁勇，孙洋，郭学军，祝令伟．猪链球菌2型和9型菌株的多重PCR检测．中国人畜共患病杂志，2005，21：510-514．
9．陆承平主编，兽医微生物学(第三版)。中国农业出版社，2001，204-212．
10．马清霞，何孔旺，陆承平．猪链球菌2型及其毒力因子检测多重PCR的建立与应用．中国兽医学报，2006，26：28-31．
11．马有智，方维焕．猪链球菌血清2型JX02株溶血素基因的克隆及序列分析．中国兽医杂志，2003，23：460-462．
12．欧瑜，陆承平．猪链球菌2型国内分离株毒力相关蛋白的分析．微生物学报，2002，42：105-109．
13．孙理云，范红结，陆承平．猪链球菌2型FBPS的纤连蛋白结合部位的初步确定．微生物学报，2005，45：753-756．
14．唐家琪，朱进，郭恒彬，胡晓抒，朱凤才，刘光中．猪链球菌引起人中毒性休克综合征和脑膜脑炎的流行病学调查及病原学研究．第三军医大学学报，2001，23：1292-1295．
15．田云，Frank M Aarestrup，陆承平．猪链球菌2型可能的毒力基因的发现．微生物学报，2004，44：613-616．
16．唐家琪，朱进，郭恒彬，胡晓抒，朱凤才，刘光中．猪链球菌引起人中毒性休克综合征和脑膜脑炎的流行病学调查及病原学研究．第三军医大学学报，2001，23：1292-1295．
17．王海丽，王长军，陆承平，潘秀珍，唐家琪．猪链球菌2型人源分离株截短 的溶菌酶释放蛋白基因的克隆及原核表达．细胞与分子免疫学杂志，2006，22：178—180．
18．王花茹，王长军，陆承平，潘秀珍，陶开华，唐家琪．致病性猪链球菌主要毒力因子基因多重PCR检测．中国流行病学杂志，2005，26：640-644．
19．曾巧英，陆承平．溶茵酶释放蛋白介导猪链球菌2型的血凝活性．中国兽医科技，2002，32：24—27．
20．曾巧英，陆承平．猪链球菌2型溶菌酶释放蛋白诱导上皮细胞融合和凋亡．微生物学报，2003，43：407—412．
21．朱进，唐家琪，郭恒彬，张云，陶开华。一起猪链球菌病暴发流行的流行病学及病原学研究．解放军预防医学杂志，2000，18：257-260．
22．朱进，唐家琪，张云，郭恒彬，陶开华．爆发流行中毒性休克综合征病原体生物学特性及鉴定．中华传染病杂志，2001，19：84-86．
23．朱荫昌，余传信，殷旭仁，刘韵娟．胶体染料斑点免疫试验检测血吸虫病人抗体方法的建立及初步应用．中国血吸虫病防治杂志，1995，7：214-218．
24. Aarestrup FM, Jorsal SE, Jensen NE. Serological characterization and antimicrobial susceptibility of Streptococcus suis isolates from diagnostic samples in Denmark during 1995 and 1996. Vet Microbiol, 1998a, 60: 59-66.
25. Aarestrup FM, Rasmussen SR, Artursson K, Jensen NE. Trends in the resistance to antimicrobial agents of Streptococcus suis isolates from Denmark and Sweden. Vet Microbiol, 1998b, 63: 71-80.
26. Allen AG, Bolitho S, Lindsay H, Khan S, Bryant C, Norton P, et al. Generation and characterization of a defined mutant of Streptococcus suis lacking suilysin. Infect Immun, 2001, 69: 2732-2735.
27. Allen AG, Lindsay H, Seilly D, Bolitho A, teters SE, Maskell DJ. Identification and characterisation of hyaluronate lyase from Streptococcus suis. Microbial Pathogenesis, 2004, 36: 327-335.
28. Allgaier A, Goethe R, Wisselink HJ, Smith HE, Valentin-Weigand P. Relatedness of Streptococcus suis Isolates of Various Serotypes and Clinical Backgrounds as Evaluated by Macrorestriction Analysis and Expression of Potential Virulence Traits, J Clin Microbiol, 2001, 39: 445-453.
29. Amass SF, SanMiguel P, Clark LK. Demonstration of vertical transmission of Streptococcus suis in swine by genomic fingerprinting. J Clin Microbiol, 1997, 35: 1595-1596.
30. Arends JP, Zanen HC. Meningitis caused by Streptococcus suis in humans. Rev Infect Dis, 1988, 10: 131-137.
31. Beaudoin M, Harel J, Higgins R, Gottschalk M, Frenette M, MacInnes JI. Molecular analysis of isolates of Streptococcus suis capsular type 2 by restriction-endonuclease-digested DNA separated on SDS-PAGE and by hybridization with an rDNA probe. J Gen Microbiol, 1992, 138:2639-2645.
32. Benga L, Goethe R, Rohde M, Valentin-Weigand P. Non-encapsulated strains reveal novel insights in invasion and survival of Streptococcus suis in epithelial cells. Cell Microbiol, 2004a, 6:867-881.
33. Benga L, Goethe R, Beilage EG, Valentin-Weigand P. Immunogenicity of Murein-associated Proteins from Temperature-stressed Streptococcus suis Cultures. J Vet Med, 2004b, 51,272-277.
34. Bensaid T, Bonnefoi-Kyriacou B, Dupel-Pottier C, Bellon O, Lagier E, Chardon H. Streptococcus suis meningitis after wild boar hunting. Presse Med, 2003, 32:1077-1078.
35. Bentley RW, Leigh JA, Collins M D. Intrageneric structure of Streptococcus based on comparative analysis of small-subunit rRNA sequences. Int J Syst Bacteriol, 1991, 41:487-494.
36. Berry AM, Lock RA, Thomas SM, Rajan DP, Hansman D, Paton JC. Cloning and nucleotide sequence of the Streptococcus pneumoniae hyaluronidase gene and purification of the enzyme from recombinant Escherichia coli. Infect Immun, 1994, 62:1101-1108.
37. Berry AM, Paton JC. Additive attenuation of virulence of Streptococcus pneumoniae by mutation of the genes encoding pneumolysin and other putative Pneumococcal virulence proteins. Infect Immun, 2000,68:133-40.
38. Berthelot-Herault F, Morvan H, Keribin AM, Gottschalk M, Kobisch M. Production of muramidase released protein (MRP ), extracellular factor (EF) and haemolysin by field isolates of Streptococcus suis capsular type 2, 1/2, 9, 7 and 3 isolated from swine in France. Vet Res, 2000, 31:473-479.
39. Berthelot-Herault F, Marois C, Gottschalk M, Kobisch M. Genetic diversity of Streptococcus suis strains isolated from pigs and humans as revealed by pulsed-field gel electrophoresis. J Clin Microbiol, 2002,40:615-619.
40. Berthelot-Herault F, Gottschalk M, Morvan H, Kobisch M. Dilemma of virulence of Streptococcus suis: Canadian isolate 89-1591 characterized as a virulent strain using a standardized experimental model in pigs. Can J Vet Res, 2005,69:236-240.
41. Billington SJ, Jost BH, Songer JG Thiol-activated cytolysins: structure, function and role in pathogenesis. FEMS Microbiol Lett, 2000,182:197-205.
42. Bolken TC, Franke CA, Jones KF, Zeller GO, Jones CH, Dutton EK, Hruby DE. Inactivation of the srtA gene in Streptococcus gordonii inhibits cell wall anchoring of surface proteins and decreases in vitro and in vivo adhesion. Infect Immun, 2001, 69:75-80.
43. Brook I. Bacterial interference. Crit Rev Microbiol, 1999,25:155-172.
44. Brousseau R, Hill JE, Prefontaine G, Goh SH, Harel J, Hemmingsen SM. Streptococcus suis Serotypes Characterized by Analysis of Chaperonin 60 Gene Sequences. Appl Environ Mecrobiol, 2001, 67: 4828-4833.
45. Busque P, Higgins R, Caya F, Quessy S. Immunisation of pigs against Streptococcus suis serotype 2 infection using a live avirulent strain. Can J Vet Res, 1997, 61:275-279.
46. Busque P, Higgins R, Senechal S, Marchand R, Quessy S. Simultaneous flow cytometric measurement of Streptococcus suis phagocytosis by polymorphonuclear and mononuclear blood leukocytes. Vet Microbiol, 1998,63:229-38.
47. Calvinho LF, Almeida RA, Oliver SP. Potential virulence factors of Streptococcus dysgalactiae associated with bovine mastitis. Vet Microbiol, 1998; 61:93-110.
48. Cantin M, Harel J, Higgins R, Gottschalk M. Antimicrobial resistance patterns and plasmid profiles of Streptococcus suis isolates. J Vet Diagn Invest, 1992,4:170-174.
49. Cerami A. Inflammatory cytokines. Clin Immunol Immunopathol, 1992,62:S3-10.
50. Chabot-Roya G, Willsonb P, Seguraa M, Lacouturea S, Gottschalk M. Phagocytosis and killing of Streptococcus suis by porcine neutrophils. Microbial Pathogenesis, 2006,41:21-32.
51. Chanter N, Jones PW, Alexander TJL. Meningitis in pigs caused by Streptococcus suis-a speculative review. Vet Microbiol, 1993, 36:39-55.
52. Chanter N, Collin N, Holmes N, Binns M, Mumford J. Characterization of the Lancefield group C streptococcus 16S-23S RNA gene intergenic spacer and its potential for identification and sub-specific typing. Epidemiol Infect, 1997; 118:125-135.
53. Charland N, Harel J, Kobisch M, Lacasse S, Gottschalk M. Streptococcus suis serotype 2 mutants deficient in capsular expression. Microbiology, 1998, 144:325-332.
54. Charland N, Nizet V, Rubens CE, Kim KS, Lacouture S, Gottschalk M. Streptococcus suis serotype 2 interactions with human brain microvascular endothelial cells. Infect Immun, 2000,68:637-643.
55. Chatellier S, Harel J, Zhang Y, Gottschalk M, Higgins R, Devriese LA, Brousseau R. Phylogenetic diversity of Streptococcus suis strains of various serotypes as revealed by 16S rRNA gene sequence comparison. Int J Syst Bacteriol, 1998,48:581-589.
56. Chatellier S, Gottschalk M, Higgins R, Broussear R, Harel J. Relatedness of Streptococcus suis Serotype 2 Isolates from Different Geographic Origins as Evaluated by Molecular Fingerprinting and Phenotyping, J Clin Microbiol, 1999, 37: 362-366.
57. Chengappa MM, Pace LW, Williams JA, Herrin CH, Ascher SE. Efficacy of tiamulin against experimentally induced Streptococcus suis. J Am Vet Med Assoe, 1990, 197: 1467-1470.
58. Cleary PP. Characterization of prototype and clinically defined strains of Streptococcus suis by genomic fingerprinting. J Clin Microbiol, 1990, 28: 462-2466.
59. Clifton Hadley FA. Streptococcus suis type 2 infections. Br Vet J, 1983, 139: 1-5.
60. Clifton Hadley FA. Studies of Streptococcus suis type 2 infection in pigs. Vet Res Commun, 1984a, 8: 217-227.
61. Clifton Hadley FA, Alexander TJ, Enright MR, Guise J. Monitoring herds for Streptococcus suis type 2 by sampling tonsils of slaughter pigs. Vet Ree, 1984b, 115: 562-564.
62. Cloutier G, D'Allaire S, Martinez G, Surprenant C, Lacouture S, Gottschalk M. Epidemiology of Streptococcus suis serotype 5 infection in a pig herd with and without clinical disease. Vet Microbiol, 2003; 97:135-151.
63. Cohen J. The immunopathogenesis of sepsis. Nature, 2000, 420: 885-891.
64. Confalonieri F, Duguet M. A 200-amino acid ATPase module in search of a basic function. Bioessays, 1995, 17: 639-650.
65. Costa AT, Lobato FC, Abreu VL, Assis RA, Reis R, Uzal FA. Serotyping and evaluation of the virulence in mice of Streptococcus suis strains isolated from diseased pigs. Rev Inst Med Trop Sao Paulo, 2005, 47: 113-115
66. Courtney HS, Li Y, Dale JB, Hasty DL. Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci. Infect Immun, 1994, 62: 3937-3946.
67. Davies PR, Ossowicz CJ. Evaluation of methods used for detecting Streptococcus suis type 2 in tonsils, and investigation of the carrier state in pigs. Res Vet Sci, 1991, 50: 190-194.
68. de Greeff A, van Alphen L, Smith HE. Selection of Recombinant Antibodies Specific for Pathogenic Streptococcus suis by Subtractive Phage Display. Infect Immun, 2000, 68: 3949-3955.
69. de Greeff A, Buys H, Verhaar R, Dijkstra J, van Alphen L, Smith HE. Contribution of Fibronectin-Binding Protein to Pathogenesis of Streptococcus suis Serotype 2. Infect Immun, 2002, 70: 1319-1325.
70. del Campo Sepulveda EM, Altman E, Kobisch M. Detection of antibodies against Streptococcus suis capsular type 2 using a purified capsular polysaccharide antigen-based indirect ELISA. Vet Microbiol, 1996, 52: 113-125.
71. Denchi EL, Helin K. E2F1 is crucial for E2F-dependent apoptosis. EMBO Pep, 2005, 6: 661-668.
72. Devriese LA, Sustronck B, Maenhouth T, Haesebrouck F. Streptococcus suis meningitis in a horse. Vet Rec, 1990, 127: 68.
73. Devriese LA, HaesebrouckF, de Herdt P, Dom P, Ducatelle R, Desmidt M, Messier S, Higgins R. Streptococcus suis infections in birds. Avian Pathol, 1994, 23: 721-724.
74. Didi Baev, Seung-Ho Ohk, Howard K. Kuramitsu. Protein interactions of SGP, an essential Streptococcus mutans GTPase, revealed by biochemical and yeast two-hybrid system analyses. FEMS Microbiology Letters, 2000, 184: 149-153.
75. Dixon EP, Johnstone EM, Lin X, Little SB. An inverse mammalian two-hybrid system for beta secretase and other proteases. Anal Biochem, 1997, 249: 239-241.
76. Fan Z, Zhuo Y, Tan X, Zhou Z, Yuan J, Qiang B, Yan J, Peng X, Gao GF. SARS-CoV Nucleocapsid Protein Binds to hUbe9, a Ubiquitin Conjugating Enzyme of the Sumoylation System. J Med Virol, 2006, 78: 1365-1373.
77. Fashena SJ, Serebriiskii I, Golemis EA. The continued evolution of two-hybrid screening approaches in yeast: how to outwit different preys with different baits. Gene, 2000, 250: 1-14.
78. Feder I, Chengappa MM, Fenwick B, Rider M, Staats J. Partial characterization of Streptococcus suis type 2 hemolysin. J Clin Microbiol, 1994, 32: 1256-1260.
79. Fields, S. and Song, O. A novel genetic system to detect protein-protein interactions. Nature, 1989, 340: 245-246.
80. Fischetti VA, Paneholi V, Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from Grampositive cocci. Mol Microbiol, 1990, 4: 1603-1605.
81. Francois B, Gissot V, Ploy MC, Vignon P. Recurrent Due to Streptococcus suis. J Clin Microbiol, 1998, 36: 2395.
82. Galina L, Vecht U, Wisselink HJ, Pijoan C. Prevalence of various phenotypes of Streptococcus suis isolated from swine in the U. S. A. based on the presence of muraminidase-released protein and extracellular factor. Can J Vet Res, 1996, 60: 72-74.
83. Gogolewski RP, Cook RW, O'Connell CJ. Streptococcus suis serotypes associated with disease in weaned pigs. Aust Vet J, 1990, 67: 202-204.
84. Gottschalk M, Lebrun A, Jacques M, Higgins R. Hemagglutination properties of Streptococcus suis. J Clin Microbiol, 1990, 28: 2156-2158.
85. Gottschalk M, Higgins R, Boudreau M. Use of polyvalent coagglutination reagents for serotyping of Streptococcus suis. J Clin Microbiol, 1993, 31: 2192-2194.
86. Gottschalk M, Lacouture S, Dubreuil JD. Characterization of Streptococcus suis type 2 haemolysin. Microbiol, 1995, 141: 189-195.
87. Gottschalk M, Lebrun A, Wisselink H, Dubreuil JD, Smith H, Vecht U. Production of virulence-related proteins by Canadian strains of Streptococcus suis capsular type 2. Can J Vet Res, 1998; 62: 75-79.
88. Gottschalk M, Segura M. The pathogenesis of the meningitis caused by Streptococcus suis: the unresolved questions. Vet Microbiol, 2000, 76: 259-272.
89. Granlund M, Oberg L, Scum M, Norgren M. Identification of a novel insertion element, IS1548, in group B streptococci, predominantly in strains causing endocarditis. J Infect Dis, 1998, 177: 967-976.
90. Grawunder U, Wilm M, Wu X, Kulesza P, Wilson TE, Mann M, Lieber MR. Activity of DNA ligase IU stimulated by complex formation with XRCC4 protein in mammalian cells. Nature, 1997, 388: 492-495.
91. Grimont F, Grimont PAD. Ribosomal ribonucleic acid gene restriction patterns as potential taxonomic tbols. Ann Inst Pasteur Microbiol, 1986, 137B: 165-175.
92. Gunther B, Ozegowski JH, Kohler W. Occurrence of extracellular hyaluronic acid and hyaluronate lyase in streptococci of groups A, B, C, and G. Zentralbl Bakteriol, 1996, 285: 64-73.
93. Halbur PG, Thanawongnuwech R, Brown G, Kinyon J, Roth J, Thacker E, Thacker B. Efficacy of antimicrobial treatments and vaccination regimens for control of porcine reproductive and respiratory syndrome virus and Streptococcus suis coinfection of nursery pigs. J Clin Microbiol, 2000, 38: 1156-1160.
94. Hara M, Akasaka K, Akinaga S, Okabe M, Nakano H, Gomez R, Wood D, Uh M, Tamanoi F. Identification of Ras Famesyltransferase Inhibitors by Microbial Screening. Proc Natl Acid Sci, USA, 1993, 90: 2281-2285.
95. Harel J, Higgins R, Gottschalk M, Bigras-Ppoulin M. Genomic relatedness among reference strains of different Streptococcus suis serotypes. Can J Vet Res, 1994, 58: 259-262.
96. Harel J, Martinez G, Nassar A, Dezfulian H, Labile SJ, Brousseau R, Moineau S, Gottschalk M. Identification of an Inducible Bacteriophage in a Virulent Strain of Streptococcus suis Serotype 2. Infect Immun, 2003, 71: 6104-6108.
97. Hassan AA, Khan IU, Abdulmawjood A, Lammler C. Inter- and intraspecies variations of the 16S-23S rDNA intergenic spacer region of various streptococcal species. Syst Appl Microbiol, 2003, 26: 97-103.
98. Heath PJ, Hunt BW. Streptococcus suis serotypes 3 to 28 associated with disease in pigs. Vet Rec, 2001, 148: 207-208.
99. Heath PJ, Hunt BW, Duff JP, Wilkinson JD. Streptococcus suis serotype 14 as a cause of pig disease in the UK. Vet Rec, 1996, 139: 450-451.
100. Heidt MC, Mohamed W, Hain T, Vogt PR, Chakraborty T, Domann E. Human Infective Endocarditis Caused by Streptococcus suis Serotype 2. J Clin Microbiol, 2005, 43: 4898-4901.
101. Helin K. Regulation of cell proliferation by the E2F transcription factors. Curr Opin Genet Dev, 1998, 8: 28-35.
102. Hensel M, Shea JE, Gleeson C, Jones MD, Dalton E, Holden DW. Simultaneous identification of bacterial virulence genes by negative selection. Science, 1995, 269: 400-403.
103. Higgins R, Gottschalk M, Beaudoin M, Rawluk SA. Distribution of Streptococcus suis capsular types in Quebec and western Canada. Can Vet J, 1992, 33: 27-30.
104. Higgins R, Gottschalk M. Distribution of the Streptococcus suis capsular types in 1999. Can Vet J, 2000, 41: 414.
105. Hill JE, Gottschalk M, Brousseau R, Harel J, Hemmingsen SM, Goh SH. Biochemical analysis, cpn60 and 16S rDNA sequence data indicate that Streptococcus suis serotypes 32 and 34, isolated from pigs, are Streptococcus orisratti. Vet Microbiol, 2005, 107: 63-69.
106. Holt ME, Enright MR, Alexander TJ. Immunisation of pigs with live cultures of Streptococcus suis type 2. Rev Vet Sci, 1988, 45: 349-352.
107. Holt ME, Enright MR, Alexander TJ. Immunisation of pigs with killed cultures of Streptococcus suis type 2. Rev Vet Sci, 1990, 48:23-27.
108. Homer K, Shain H, Beighton D. The role of hyaluronidase in growth of Streptococcus intermedius on hyaluronate. Adv Exp Med Biol, 1997, 418: 681-683.
109. Homer KA, Denbow L, Whiley R.A, Beighton D. Chondroitin sulfate depolymerase and hyaluronidase activities of viridans streptococci determined by a sensitive spectrophotometric assay. J Clin Microbiol, 1993, 31: 1648-1651.
110. Hommez J, Willepit J, Cassimon O, Castryck F, Ceyssens K, Devriese LA. Streptococcus suis and other streptococcal species as a cause of extramammary infection in ruminants. Vet Rec, 1988, 123: 626-627.
111. Hornish RE, Kotarski SF. Cephalosporins in veterinary medicine-Ceftiofur use in food animals. Curr Top Med Chem, 2002, 2: 717-731.
112. Hu X, Zhu F, Wang H, Chen S, Wang G. Studies on human streptococcal infectious syndrome caused by infected pigs. Zhonghua Yu Fang Yi Xue Za Zhi, 2000, 34: 150-152.
113. Hua SB, Luo Y, Qiu M, Chan E, Zhou H, Zhu L. Construction of a modular yeast two-hybrid cDNA library from human EST clones for the human genome protein linkage map. Gene, 1998, 215: 143-152.
114. Huang J and Schreiber SL. A yeast genetic system for selecting small molecule inhibitors of protein-protein interactions in nanodroplets. Proc Natl Acid Sci USA, 1997, 94: 13396-13401.
115. Huang YT, Teng LJ, Ho SW, Hsueh PR. Streptococcus suis infection. J Microbiol Immunol Infect, 2005, 58: 306-313.
116. Huang SH, Stins MF, Kim KS. Bacterial penetration across the blood-brain barrier during the development of neonatal meningitis. Microbes Infect, 2000, 2: 1237-1244.
117. Hynes WL, Walton SL. Hyaluronidases of Gram-positive bacteria. FEMS Microbiol Lett, 2000, 183: 201-207.
118. Ito T, Chiba T, Ozawa R, Yoshida M, Hattori M, Sakaki Y. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci, 2001, 98: 4569-4574.
119. Jack RW, Tagg JR, Ray B. Bacteriocins of gram-positive bacteria. Microbiol Rev, 1995, 59: 171-200.
120. Jackson MW and Piano GV. Interactions between type Ⅲ secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system. FEMS Microbiology Letters, 2000, 86: 85-90.
121. Jacobs AAC, Loeffen PLW, van den Berg AJG, Storm PK. Identification, purification, and characterization of a thiol-activated hemolysin (suilysin) of Streptococcus suis. Infect Immun, 1994, 62: 1742-1748.
122. Jacobs AAC, van den Berg AJG, Loeffen PLW. Protection of experimentally infected pigs by suilysin, the thiol-activated haemolysin of Streptococcus suis. Vet Rec, 1996, 139: 225-228.
123. Jacques M, Gottschalk M, Foiry B, Higgins R. Ultrastructural study of surface components of Streptococcus suis. J Bacteriol, 1990, 172: 2833-2838.
124. Joh D, Wann ERW, Kreikemeyer B, Speziale P, Hook M. Role of fibronectin-binding MSCRAMMS in bacterial adherence and entry into mammalian cells. Matrix Biol, 1999, 18: 211-223.
125. Karimova G, Pidoux J, Ullmann A, Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. 1998, Proc Natl Acad Sci USA, 95: 5752-5756.
126. Karimova G, Ladant D, Ullmann A. Two-hybrid systems and their usage in infection biology. Int J Med Microbiol, 2002,292:17-25.
127. Kataoka Y, Yoshida T, Sawada T. A 10-year survey of antimicrobial susceptibility of Streptococcus suis isolates from swine in Japan. J Vet Med Sci, 2000, 62:1053-1057.
128. Kim JW, Cho HS, Kim JH, Hur SY, Kim TE, Lee JM, Kim IK, Namkoong SE. AAC-11 overexpression induces invasion and protects cervical cancer cells from apoptosis. Lab Invest, 2000, 80: 587-594.
129. King SJ, Heath PJ, Luque I, Tarradas C, Dowson CG, Whatmore AM. Distribution and Genetic Diversity of Suilysin in Streptococcus suis Isolated from Different Diseases of Pigs and Characterization of the Genetic Basis of Suilysin Absence. Infect Immun, 2001,12: 7572-7582.
130. King SJ, Leigh JA, Heath PJ, Luque I, Tarradas C, Dowson CG, Whatmore AM. Development of a Multilocus Sequence Typing Scheme for the Pig Pathogen Streptococcus suis: Identification of Virulent Clones and Potential Capsular Serotype Exchange. J Clin Microbiol, 2002,40:3671-3680.
131. Kiston J, Raven T, Yingping J, et al. A deathdomain-containing receotor that mediates apoptosis. Nature, 1996,384:372-375.
132. Lalonde M, Segura M, Lacouture S, Gottschalk M. Interactions between Streptococcus suis serotype 2 and different epithelial cell lines. Microbiol, 2000, 146:1913-1921.
133. Li B and Fields S. Identification of mutations in p53 that affect its binding to SV40 large T antigen by using the yeast two-hybrid system. FASEB J, 1993,7:957-963.
134. Ling EWY, Noya FJD, Ricard G, Beharry K, Mills EL, Aranda JV. Biochemical mediators of meningeal inflammatory response to group B Streptococcus in the newborn piglet model. Pediatr Res, 1995,38:981-987.
135. Lun S, Perez-Casal J, Connor W, Willson PJ. Role of suilysin in pathogenesis of Streptococcus suis capsular serotype 2. Microbiol Pathogen, 2003, 34:27-37.
136. Lun S, Willson PJ. Expression of green fluorescent protein and its application in pathogenesis studies of serotype 2 Streptococcus suis. J Microbiol Methods, 2004, 56:401-412.
137. Mannan AU, Krawen P, Sauter SM, Boehm J, Chronowska A, Paulus W, Neesen J, Engel W. ZFYVE 27 (SPG33) , a Novel Spastin-Binding Protein, Is Mutated in Hereditary Spastic Paraplegia. Am J Hum Genet, 2006, 79: 351-357.
138. Marois C, Bougeard S, Gottschalk M, Kobisch M. Multiplex PCR Assay for Detection of Streptococcus suis Species and Serotypes 2 and 1/2 in Tonsils of Live and Dead Pigs. J Clin Microbiol, 2004,42: 3169-3175.
139. Marois C, Devendec LL, Gottschalk M, Kobisch M. Molecular characterization of Streptococcus suis strains by 16S-23S intergenic spacer polymerase chain reaction and restriction fragment length polymorphism analysis. Can J Vet Res, 2006, 70: 94-104.
140. Martel A, Baele M, Devriese LA, Goossens H, Wisselink HJ, Decostere A, Haesebrouck F. Prevalence and mechanism of resistance against macrolides and lincosamides in Streptococcus suis isolates. Vet Microbiol, 2001, 83: 287-297.
141. Martinez G, Harel J, Lacouture S, Gottschalk M. Genetic diversity of Streptococcus suis serotypes 2 and 1/2 isolates recovered from carrier pigs in closed herds. Can J Vet Res, 2002, 66: 240-248.
142. McCraith S, Holtzman T, Moss B, fields S. Genome-wide analysis of vaccine virus protein-protein interactions. Proc Natl Acid Sci USA, 2000, 97: 4879-4884.
143. Melancon D, Grenier D. Production and Properties of Bacteriocin-Like Inhibitory Substances from the Swine Pathogen Streptococcus suis Serotype 2. App Environ Microbiol, 2003, 69: 4482-4488.
144. Melegari M, Scaglionip P, Wands JR. Cloning and characterization of a novel hepatitis B virus X binding protein that inhibits viral replication. J virology, 1998, 72: 1737-1743.
145. Mogollon JD, Pijoan C, Murtaugh MP, Kaplan EL, Collins JE, Cleary PP. Characterization of prototype and clinically defined strains of Streptococcus suis by genomic fingerprinting. J Clin Microbiol, 1990, 28: 2462-2466.
146. Morris EJ, Michaud WA, Ji JY, Moon NS, Rocco JW, Dyson NJ. Functional Identification of Api 5 as a Suppressor of E2F-Dependent Apoptosis In Vivo. Plos Genet, 2006, 2:e196.
147. Muller-Alouf H, Carnoy C, Simonet M, Alouf JE. Superantigen bacterial toxins: state of the art. Toxicon, 2001, 39: 1691-1701.
148. Muller G, Nielsen G, Baigent CL. Electron microscopical particle counting in irology. Ⅲ. Parameters governing the efficiency of sedimentation techniques and its improvement with the application of poly-L-lysine. Arch Virol, 1980, 64: 311-318.
149. Murakami Y, Fukazawa H, Kobatake T, Yamagoe S, Takebe Y, Tobiume M, Matsuda M, Uehara Y. A mammalian two-hybrid screening system for inhibitors of interaction between H1V Nef and the cellular tyrosine kinase Hck. Antiviral Res. 2002, 55: 161-168.
150. Mwaniki CG, Robertson ID, Trott DJ, Atyeo RF, Lee BJ, Hampson DJ. Clonal analysis and virulence of Australian isolates of Streptococcus suis type 2. Epidemiol Infect, 1994, 113: 321-334.
151. Mwaniki CG, Robertson ID, Hampson DJ. The prevalence of Streptococcus suis type 2 in Western Australian piggeries. Aust Vet J, 1994,71:385-386.
152. Norton PM, Rolph C, Ward PN, Bentley RW, Leigh JA. Epithelial invasion and cell lysis by virulent strains of Streptococcus suis is enhanced by the presence of suilysin. FEMS Immunol Med Microbiol, 1999,26:25-35.
153. Okwumabua O, Staats J, Chengappa MM. Detection of genomic heterogeneity in Streptococcus suis isolates by DNA restriction fragment length polymorphisms of rRNA genes (ribotyping) . J Clin Microbiol, 1995,33:968-972.
154. Okwumabua O, Abdelmagid O, Chengappa MM. Hybridization analysis of the gene encoding a hemolysin (suilysin) of Streptococcus suis type 2: evidence for the absence of the gene in some isolates. FEMS Microbiol Lett, 1999, 181:113-121.
155. Oliveira S, Batista L, Torremorell M, Pijoan C. Experimental colonization of piglets and gilts with systemic strains of Haemophilus parasuis and Streptococcus suis to prevent disease. Can J Vet Res, 2001,65:161-167.
156. Osaki M, Takamatsu D, Shimoji Y, Sekizaki T. Characterization of Streptococcus suis Genes Encoding Proteins Homologous to Sortase of Gram-Positive Bacteria. J Bacteriol, 2002,184:971-982.
157. Osikowicz G, Beggs M, Brookhart P, Caplan D, Ching S, Eck P, Gordon J, Richerson R, Sampedro S, Stimpson D, et al. One-step chromatographic immunoassay for qualitative determination of choriogonadotropin in urine. Clin Chem. 1990, 36:1586
158. Owen RJ. Chromosomal DNA fingerprinting: a new method of species and strain identification applicable to microbial pathogens. J Med Microbiol, 1989, 30:89-99.
159. Page AL, Fromont-Racine M, Sansonetti P, Legrain P, Parsot C. Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri. Mol Microbiol, 2001,42:1133 -1145.
160. Pallares FJ, Schmitt CS, Roth JA, Evans RB, Kinyon JM, Halbur PG Evaluation of a ceftiofur-washed whole cell Streptococcus suis bacterin in pigs. Can J Vet Res, 2004, 68:236-240.
161. Pedroli S, Kobisch M, Beauchet O, Chaussinand JP, Lucht F. Streptococcus suis bacteremia. Presse Med, 2003, 32:599-601.
162. Perch B, Kristjansen P, Skadhauge K. Group R Streptococci pathogenic for man: two cases of meningitis and one fatal case of sepsis. Acta Pathol Microbiol Scand, 1968, 74:69-76.
163. Perch B, Pedersen KB, Henrichsen J. Serology of capsulated streptococci pathogenic for pigs: six new serotypes of Streptococcus suis. J Clin Microbiol, 1983, 17:993-996.
164. Rasmussen SR, Aarestrup FM, Jensen NE, Jorsal SE. Associations of Streptococcus suis Serotype 2 Ribotype Profiles with Clinical Disease and Antimicrobial Resistance. J Clin Microbiol, 1999, 37: 404-408.
165. Reid SM, Ferris NP, Bruning A, Hutchings GH, Kowalska Z, kerblom LA. Development of a rapid chromatographic strip test for the pen-side detection of foot-and-mouth disease virus antigen .J Virolog Methods, 2001, 96:189-202.
166. Robertson ID, Blackmore DK. Prevalence of Streptococcus suis types 1 and 2 in domestic pigs in Australia and New Zealand. Vet Rec, 1989, 124:391-394.
167. Rolland K, Marois C, Siquier V, Cattier B, Quentin R. Genetic features of Streptococcus agalactiae strains causing severe neonatal infections, as revealed by pulsed-field gel electrophoresis and hy1B gene analysis. J Clin Microbiol, 1999, 37:1892-1898.
168. Rosenkranz M, Elsner HA, Sturenburg HJ, Weiller C, Rother J, Sobottka I. Streptococcus suis meningitis and septicemia contracted from a wild boar in Germany. J Neurol, 2003, 250: 869-870.
169. Salasia SI, Lammler C. Distribution of serotype, virulence markers and further characteristics of Streptococcus suis isolates from pigs. Zentralbl Veterinarmed B, 1995, 42, 78-83.
1670. Salles MW. Perez-Casal J, Willson P, Middleton DM. Changes in the leucocyte subpopulations of the palatine tonsillar crypt epithelium of pigs in response to Streptococcus suis type 2 infection. Vet Immunol Immunopathol, 2002, 87:51-63.
171. Sanford SE. Gross and histopathological findings in unusual lesions caused by Streptococcus suis in pigs. Ⅱ. Central nervous system lesions. Can J Vet Res, 1987, 51: 486-489.
172. Sasaki H, Moriyama S, Yuldue H, Kobayashi Y, Nakashima Y, Kaji M, Fukai I, Kiriyama M, Yamakawa Y, Fujii Y.. Expression of the antiapoptosis gene, AAC-11, as a prognosis marker in non-small cell lung cancer. Lung Cancer, 2001, 34: 53-57.
173. Saukkonen K, Sande S, Cioffe C, Wolpe S, Sherry B, Cerami A, Tuomanen E. The role of cytokines in the generation of inflammation and tissue damage in experimental gram-positive meningitis. J Exp Med, 1990, 171: 439-448.
174. Schaufuss P, Sting R, Schaeg W, Blobel H. Isolation and characterization of hyaluronidase from Streptococcus uberis. Zentralbl Bakteriol, 1989, 271: 46-53.
175. Schlegel L, Grimont F, Grimont PA, Bouvet A. Identification of major streptococcal species by rrn-amplified ribosomal DNA restriction analysis. J Clin Microbiol, 2003, 41: 657-666.
176. Schneewind O, Model P, Fischetti VA. Sorting of protein A to the staphylococcal cell wall. Cell, 1992,70:267-281.
177. Seddon SV, Hemingway I, Borriello SP. Hydrolytic enzyme production by Clostridium difficile and its relationship to toxin production and virulence in the hamster model. J Med Microbiol, 1990, 31:169-74.
178. Segers RP, Kenter T, de Haan LA, Jacobs AA. Characterisation of the gene encoding suilysin from Streptococcus suis and expression in field strains. FEMS Microbiol Lett, 1998,167:255-61.
179. Segura M, Cleroux P, Gottschalk M. Streptococcus suis and group B Streptococcus differ in their interactions with murine macrophages. FEMS Immunol Med Microbiol, 1998,21:189-195.
180. Segura M, Stankova J, Gottschalk M. Heat-Killed Streptococcus suis Capsular Type 2 Strains Stimulate Tumor Necrosis Factor Alpha and Interleukin-6 Production by Murine Macrophages. Infect Immun, 1999,67:4646-4654.
181. Segura M, Gottschalk M. Streptococcus suis interactions with the murine macrophage cell line J774: adhesion and cytotoxicity. Infect Immun, 2002, 70:4312-4322.
182. Segura M, Gottschalk M. Extracellular virulence factors of streptococci associated with animal diseases. Front Biosci, 2004a, 9:1157-1188.
183. Segura M, Gottschalk M, Olivier M. Encapsulated Streptococcus suis inhibits activation of signaling pathways involved in phagocytosis. Infect Immun, 2004b, 72:5322-5330.
184. Sekizaki T, Otani Y, Osaki M, Takamatsu D, Shimoji Y. Evidence for horizontal transfer of SsuDAT1I restriction-modification genes to the Streptococcus suis genome. J Bacteriol, 2001,183:500-511.
185. Shaver YJ, Nagpal ML, Rudner R, Nakamura LK, Fox KF, Fox A. Restriction fragment length polymorphism of rRNA operons for discrimination and intergenic spacer sequences for cataloging of Bacillus subtilis sub-groups. J Microbiol Methods, 2002,50:215-223.
186. Silva LMG, Baums CG, Rehm T, Wisselink HJ, Goethe R, Valentin-Weigand P. Virulence-associated gene profiling of Streptococcus suis isolates by PCR. Vet Microbiol, 2006,115:117-127.
187. Slater JD, Allen AG, May JP, Bolitho S, Lindsay H, Maskell DJ. Mutagenesis of Streptococcus equi and Streptococcus suis by transposon Tn917. Vet Microbiol, 2003, 93:197-206.
188. Smith HE, Vecht U, Gielkens AL, Smits MA. Cloning and nucleotide sequence of the gene encoding the 136-kilodalton surface protein (muramidase-released protein) of Streptococcus suis type 2. Infect Immun, 1992, 60:2361-2367.
189. Smith HE, Vecht U, Wisselink H J, Stockhofe-Zurwieden N, Biermann Y, Smits MA. Mutants of Streptococcus suis types 1 and 2 impaired in expression of muramidase-released protein and extracellular protein induce disease in newborn germfree pigs. Infect Immun, 1996, 64:4409-4412.
190. Smith HE, Rijnsburger M, Stokhofe-zurwieden N, Wisselink HJ, Vecht U, Smits MA. Virulent Strains of Streptococcus suis Serotype 2 and Highly Virulent Strains of Streptococcus suis Serotype 1 Can Be Recognized by a Unique Ribotype Profile. J Clin Mierobiol, 1997, 35: 1049-1053.
191. Smith HE, Damman M, van der Velde J, Wagenaar F, Wisselind HJ, Stockhofe-zurwieden N, Smits MA. Identification and Characterization of the cps Locus of Streptococcus suis Serotype 2: the Capsule Protects against Phagocytosis and Is an Important Virulence Factor. Infect Immun, 1999, 67: 1750-1756.
192. Smith HE, Buijs H, Wisselink HJ, Stockhofe-Zurwieden N, Smits MA. Selection of Virulence-Associated Determinants of Streptococcus suis Serotype 2 by In Vivo Complementation. Infect Immun, 2001, 69: 1961-1966.
193. Sorensen NS, Tegtmeier Ca, Andresen LO, Pineiro M, Toussaint MJM, Campbell FM, Lampreave F, Heegaard PMH. The porcine acute phase protein response to acute clinical and subclinical experimental infection with Streptococcus suis. Vet Immunol Immunopathol, 2006, 113: 157-168.
194. Sprenger H, Rosier A, Tonn P, Braune HJ, Huffmann G, Gemsa D. Chemokines in the cerebrospinal fluid of patients with meningitis. Clin Immunol Immunopathol, 1996, 80: 155-161.
195. Sriskandan S, Slater JD. Invasive Disease and Toxic Shock due to Zoonotic Streptococcus suis: An Emerging Infection in the East?. Plos Med, 2006, 3:e187.
196. Staats JJ, Plattner BL, Nietfeld J, Dritz S, Chengappa MM. Use of ribotyping and hemolysin activity to identify highly virulent Streptococcus suis type 2 isolates. J Clin Microbiol, 1998, 36: 15-19.
197. Staats JJ, Feder I, Okwumabua O, Chengappa MM. Streptococcus suis: past and present. Vet Res Commun, 1997, 21: 381-407.
198. Staudinger J, Zhou J, Olson EN, et al. PICK1:a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system. J cell Biol, 1995, 128: 263-271.
199. Stein E, Huynh-Do U, Daniel TO. Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase. J Biol Chem, 1998, 273: 1303-1308.
200. Stenmark H, Aasland R. FYVE-finger proteins-effectors of an inositol lipid. J Cell Sci, 1999, 112: 4175-4183.
201. Stenmark H, Aasland R, Driscoll PC. The phosphatidylinositol 3-phosphate-binding FYVE finger. FEBS Lett, 2002, 513: 77-84.
202. Stevens C, La Thangue NB. The emerging role of E2F-1 in the DNA damage response and checkpoint control. DNA Repair (Amst), 2004, 3: 1071-1079.
203. Strangmann E, Froleke H, Kohse KP. Septic shock caused by Streptococcus suis: Case report and investigation of a risk group. Int J Hyg Environ Health, 2002, 205: 385-392.
204. Stull TL, Lilipuma JJ, Edlind TD. A broad spectrum probe for molecular epidemiology of bacteria: ribosomal RNA. J Infect Dis, 1988, 157:280-286.
205. Takamatsu D, Osaki M, Sekizaki T. Evidence for Lateral Transfer of the Suilysin Gene Region of Streptococcus suis. J Bacterial, 2002, 184: 2050-2057.
206. Tang J, Wang C, Feng Y, Yang W, Song H, Chen Z, Yu H, Pan X, Zhou X, Wang H, Wu B, Wang H, Zhao H, Lin Y, Yue J, Wu Z, He X, Gao F, Khan AH, Wang J, Zhao G, Wang Y, Wang X, Chen Z, Gao GF. Streptococcal toxic shock syndrome caused by Streptococcus suis serotype 2. PLoS Med, 2006, 3: e151.
207. Tarradas C, Luque I, de Andres D, Abdel-Aziz Shahein Ye, Pons P, Gonzalez F, Borge C, Perea A. Epidemiologieal relationship of human and swine Streptococcus suis isolates. J Vet Med B Infect Dis Vet Public Health, 2001, 48: 347-355.
208. Tarradas C, Arenas A, Maldonado A, Luque I, Miranda A, Perea A. Identfication of Streptococcus suis isolated from swine: proposal for biochemical parameters. J Clin Microbiol, 1994, 32: 578-580.
209. Tarradas C, Borge C, Arenas A, Maldonado A, Astorga R, Miranda A, Luque I. Suilysin production by Streptococcus suis isolated from diseased and healthy carrier pigs in Spain. Vet Rec, 2001, 148: 183-184.
210. Tewari M, Yu M, Ross B, Dean C, Giordano A, Rubin R. AAC-11, a novel cDNA that inhibits apoptosis after growth factor withdrawal. Cancer Res, 1997, 57: 4063-4069.
211. Thompson C, Merrilf AR, Mangroo D. Identification of peptide inhibitors of Pseudomonas aeruginosa exotoxin A function using a yeast two-hybrid approach. FEMS Microbiol Lett, 2003, 218: 85-92.
212. Tipper DJ, Strominger JL. Biosynthesis of the peptidoglycan of bacterial cell walls. Ⅻ. Inhibition of cross-linking by penieillins and cephalosporins: studies in Staphylococcus aureus in vivo. J Biol Chem, 1968, 243: 3169-3179.
213. Ton-That H, Liu G, Mazmanian SK, Faull KF, Schneewind O. Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proc Natl Acad Sci USA, 1999, 96: 12424-12429.
214. Ton-That H, Mazmanian SK, Faull KF, Schneewind O. Anchoring of surface proteins to the cell wall of Staphylococcus aureus Sortase-catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH2-GIy3 substrates. J Biol Chem, 2000, 275: 9876-9881.
215. Torremorell M, Pijoan C. Prolonged persistence of an epidemic Streptococcus suis strain in a closed pig population. Vet Rec, 1998, 143: 394-395.
216. Townsend GC, Scheld WM. Microbe-endothelium interactions in blood-brain barrier permeability during bacterial meningitis. ASM News, 1995, 61:294-298.
217. Trottier S, Higgins R, Brochu G, Gottschalk M. A case of human endocarditis due to Streptococcus suis in North America. Rev Infect Dis, 1991, 13: 1251-1252.
218. Tuomanen E. Entry of pathogens into the central nervous system. FEMS Microbiol Rev, 1996, 18: 289-299.
219. Turgeon PL, Higgins R, Gottschalk M, Beaudoin M. Antimicrobial susceptibility of Streptococcus suis isolates. Br Vet J, 1994, 50:263-269.
220. Uetz P, Giot L, Cagney G, Mansfield TA, Judson RS, Knight JR, Lockshon D, Narayan V, Srinivasan M, Pochart P, Qureshui-Emili A, Li Y, Godwin B, Conover D, Kalbfleisch T, Vijayadamodar G, Yang M, Johnston M, Fields S, Rothberg JM. A comprehensive analysis of protien-protein interactions in Saccharomyces cerevisiae. Nature, 2000, 403: 623-627.
221. Vanier G, Segura M, Fried P, Lacouture S, Gottschalk M. Invasion of Porcine Brain Microvascular Endothelial Cells by Streptococcus suis Serotype 2. Infect Immun, 2004, 72: 1441-1449.
222. Vecht U, Wisselink HJ, Jellema ML, Smith HE. Identification of two proteins associated with virulence of Streptococcus suis type 2. Infect. Immun, 1991, 59: 3156-3162.
223. Vecht U, Wisselink HJ, van Dijk JE, Smith HE. Virulence of Streptococcus suis type 2 strains in newborn germfree pigs depend on phenotype. Infect Immun, 1992, 60: 550-556.
224. Vecht U, Arends JP, van der Molen EJ, van Leengoed LAMG. Differences in virulence between two strains of Streptococcus suis type 2 after experimentally induced infection of newborn germfree pigs. Am J Vet Res, 1989, 50: 1037-1043.
225. Vela AI, Goyache J, Tarradas C, Luque I, Mateos A, Moreno MA, Borge C, Perea JA, Dominguez L, Femandez-Garayzabal JF. Analysis of genetic diversity of Streptococcus suis clinical isolates from pigs in Spain by pulsed-field gel electrophoresis. J Clin Micmbiol, 2003, 41: 2498-2502.
226. Verhoef J, Mattsson E. The role of cytokines in gram-positive bacterial shock. Trends Mierobiol, 1995, 3: 136-140.
227. Verheijen R, Osswald IK, Dietrich R, Haasnoot W, Development of a One Step Strip Test for the Detection of (Dihydro) streptomycin Residues in Raw Milk. Food Agricul Immunol, 2000, 12: 31-40
228. Victor J. Torres, Mark S, McClain, Timothy L. Cover. Interactions between p-33 and p-55 domains of the Helieobacter pylori Vacuolating Cytotoxin (VacA). J Biol Chem, 2004, 279: 2324-2331.
229. Walhot AJ, Sordella R, Lu X, et al. Protein interaction mapping in C. elegans using protein involved in vulval development. Science, 2000, 287: 116-122.
230. Wen HW, Borejsza-Wysoeki W, Thomas R. DeCory TR, Durst RA. Development of a competitive liposome-based lateral flow assay for the rapid detection of the allergenic peanut protein Ara h1. Anal Bioanal Chem, 2005, 382: 1217-1226.
231. Williams AE, Blakemore WF. Pathogenesis of meningitis caused by Streptococcus suis type 2. J Infect Dis, 1990, 162: 474-481.
232. Wilson TL, Jeffers J, Rapp-Gabrielson VJ, Martin S, Klein LK, Lowery DE, Fuller TE. A novel signature-tagged mutagenesis system for Streptococcus suis serotype 2.Vet Microbiol, 2007, doi: 10.1016/j.vetmic.2006.12.025.
233. Wisselink HJ, Vecht U, Stockhofe-Zurwieden N, Smith HE. Protection of pigs against challenge with virulent Streptococcus suis serotype 2 strains by a muramidase-released protein and extracellular factor vaccine. Vet Rec, 2001, 148: 473-477.
234. Wisselink HJ, Reek FH, Vecht U, Stockhofe-Zurwieden N, Smits MA, Smith HE. Detection of virulent strains of Streptococcus suis type 2 and highly virulent strains of Streptococcus suis type 1 in tonsillar specimens of pigs by PCR. Vet Microbiol, 1999, 67: 143-157.
235. Wisselink HJ, Smith HE, Stockhofe-Zurwieden N, Peperkamp K, Vecht U. Distribution of capsular types and production of muramidase-released protein (MRP) and extracellular factor (EF) of Streptococcus suis strains isolated from diseased pigs in seven European countries. Vet Microbiol, 2000, 74: 237-248.
236. Wisselink HJ, Stockhofe-Zurwieden N, Hilgers L, Smith HE. Assessment of protective efficacy of live and killed vaccines based on a non-encapsulated mutant of Streptococcus suis type 2. Vet Microbiol, 2002, 84: 155-168.
237. Wisselink HJ, Veldman KT, Van den Eede C, Salmon SA, Mevius DJ. Quantitative susceptibility of Streptococcus suis strains isolated from diseased pigs in seven European countries to antimicrobial agents licensed in veterinary medicine. Vet Microbiol, 2006, 113: 73-82.
238. Woese CR. Bacterial evolution. Microbiol Rev, 1987, 51: 221-271.
239. Yang JX, Jin ML, Chen JF, Yang Y, Zheng P, Zhang AD, Song YF, Zhou HB, Chen HC. Development and evaluation of an immunochromatographic strip for detection of Streptococcus suis type 2 antibody. J Vet Diagn Invest, 2007, 19 (in press)
240. Yu H, Jing H, Chen Z, Zheng H, Zhu X, Wang H, Wang S, Liu L, Zu R, Luo L, Xiang N, Liu H, Liu X, Shu Y, Lee S, Chuang S, Wang Y, Xu J, Yang W, China SSG. Human Streptococcus suis outbreak, Sichuan, China. Emerg Infect Dis, 2006, 12: 914-920.
241. Zhang GP, Li QM, Yang YY, Guo JQ, Li XW, Deng RG, Xiao ZJ, Xing GX, Yang JF, Zhao D, Cai S J, Zang WM. Development of a one-step strip test for the diagnosis of chicken infectious bursal disease.Avian Dis. 2005, 49: 177-81.
242. Zhang GP, Guo JQ, Wang XN, Yang JX, Yang YY, Li QM, Li XW, Deng RG, Xiao ZJ, Yang JF, Xing GX, Zhao D. Development and evaluation of an immunochromatographic strip for trichinellosis detection. Vet Parasitol, 2006a, 137: 286-293.
243. Zhang GP, Wang XN, Yang JF, Yang YY, Xing GX, Li QM, Zhao D, Chai SJ, Guo JQ. Development of an immunochromatographic lateral flow test strip for detection of beta-adrenergic agonist Clenbuterol residues. J Immunol Methods, 2006b, 312: 27-33.