小反刍兽疫病毒西藏株N基因人工合成、表达及检测方法建立的研究
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摘要
小反刍兽疫(peste des petits ruminants, PPR)是由小反刍兽疫病毒引起的一种山羊、绵羊等小反刍兽类的急性接触传染性疾病,特别是山羊易感,具有很高的感染率与致死率。临床上以高热、坏死性胃炎和肺炎为特征。该病首次报道是在西非的科特迪瓦,随后,阿拉伯半岛、以色列、伊拉克、约旦、尼日利亚、塞尔维亚和加纳等国家都报道发生过此病。目前世界各国对此病都予以高度重视,美国、韩国、印度等国家都在积极进行相关方面的研究工作。2007年7月,我国西藏阿里地区的日土、革吉、札达等县暴发了小反刍兽疫疫情,造成当地羊只的大量死亡。对当地的养羊业造成了巨大的经济损失,此病的流行也对我国西藏周边地区的养羊业构成了严重的威胁。我国对该病的研究工作较少,为此,中央政府高度重视,责令相关政府部门和机构对该病进行严格监控并加强相关技术和理论的研究。
目前,该病尚无有效的治疗方法,主要是靠疫苗免疫以及血清学监控来预防此病的蔓延。然而该病属于高致病性传染病,一般实验室无法进行病原操作。并且首次传入我国,缺乏此方面的研究基础。本研究基于建立完善的血清学检测方法,应用化学合成的N蛋白,制备N蛋白单表位抗体,建立两种不同方式的ELISA检测方法。对方法进行了优化,提高其稳定性、重复性和敏感度,样品检测结果表明：方法的实用性强,结果确实可靠,科学有效,能够应用于临床实践中。主要研究内容包括：
1西藏株小反刍兽疫N蛋白的化学合成
首先应用DNAstar和RNA structure等软件对GenBank所发表的西藏株小反刍兽疫N蛋白序列进行了编辑修改,避免了复杂的二级结构,改造了酶切位点,优化了稀有密码子,全基因的核苷酸序列和原序列同源性仅71.9%,氨基酸序列同源性100%,以便于基因序列能够在大肠杆菌中原核表达。然后参考了目前国际较为先进的基因化学合成的方法,设计并合成了20对引物,引物长度大部分在60bp,相邻引物方向相反,并且序列重复21bp。分别以5对引物为材料,在无模板的状态下,通过PCR反应化学合成4段长度在404～414bp的双链DNA片段。然后以上述4段DNA片段为模板,以最外侧引物为引物,通过overlap-PCR法化学合成了可以表达西藏株小反刍兽疫N蛋白的基因。测序比对后,针对在合成过程中出现的定点突变进行了人工回复突变。最后成功克隆入载体simple pMD-19T。再次测序结果表明所合成的基因序列正确,长度1578bp,和预期相符。
2N蛋白基因的克隆、表达、产物纯化纯化及免疫性质鉴定
同源重组法是目前较为流行且便捷的克隆方式；特别适合长片段核苷酸的克隆。本研究运用此方法进行分子克隆,首先设计在原基因片段加入15bp和载体两端重合序列的引物,通过PCR获得克隆所需的外源基因(原N基因两端各加入15bp线性化载体两端的序列),然后把载体酶切线性化,利用同源重组酶的作用,一次性把长达约1600bp的核苷酸片段成功克隆入长达5900bp的表达载体pET-32a。测序后正确的克隆转化入大肠杆菌株Bl21-DE3-plysS。用IPTG进行诱导,尝试了其不同浓度、诱导时间、诱导温度等条件下的表达产量,并且尽量增加可溶性蛋白的表达量。所表达的总蛋白使用N蛋白单克隆抗体进行western-blot检测。最适诱导条件下的表达产物的上清通过离子亲和层析法纯化,优化洗脱液的咪唑含量。研究结果表明：化学合成的长达1600bp的N基因通过同源重组法可以简单而且低背景的克隆入5900bp的表达载体pET-32a；可以通过原核系统正确表达N蛋白；所表达蛋白用HIS标签可以纯化,纯化产物纯度高于95%；表达的蛋白可与此蛋白的单克隆抗体可以较好的结合。
3小反刍兽疫间接ELISA方法的建立及与商品化试剂盒检测对比
为建立特异性强、灵敏度高的PPR间接ELISA方法,本文研究了间接ELISA的抗原包被浓度、血清稀释浓度、封闭液、封闭时间、血清稀释液、血清作用时间、二抗和底物作用时间等参数。在不同的条件下,选择阳性血清OD值：阴性血清OD值比值最大的条件为最适检测条件。降低了阴性背景值,提高了阳性值。在最佳化条件的基础上选择了198份阴性血清的平均P/N值加二倍标准差作为·cut off值。试剂盒批内和批间的变异系数均小于10%,验证了此ELISA方法的稳定性。对比商品化竞争ELISA试剂盒,敏感性和特异性分别为96.7%和96.1%,丰富了国内PPRV血清学的检测。
4单表位多肽抗血清的制备及免疫性质鉴定
化学方法合成了小反刍兽疫N蛋白中4个重要的抗原表位的多肽,以这4段多肽作为抗原分别用PPRV阳性血清和RPV阳性血清进行ELISA检测,结果表明19个氨基酸的多肽RPGRPRGETPGQLLLEIMP可以较好的区分两种血清。然后用此多肽作为抗原免疫了5只家免,制备了抗血清,血清抗体滴度在90d后较高(1：64000滴度)。最后通过ELISA方法继续验证抗体的滴度,分别包被了原核表达的N蛋白和多肽,进行了间接ELISA的测定,结果表明90天后抗体滴度最高,所制备的抗体更适合与原核表达产物N蛋白结合,为建立竞争ELISA检测方法奠定了基础。
5小反刍兽疫抗血清检测的竞争ELISA方法的建立
利用化学合成的多肽免疫兔得到兔单表位抗血清,以N蛋白作为捕获抗原,用兔的高免血清和待检血清竞争,建立竞争ELISA方法以便用于国内小反刍兽疫的血清学监测。研究表明最佳化的检测条件为：包被抗原浓度为320ng/g1,100μl/孔为最适抗原包被浓度；倍比稀释待检阴阳性血清和竞争兔高免血清,测得PI差距最大为50.8,抗原抗体的结合及竞争时间为1小时。选取489份已知PPRV抗体阴性的血清(山羊198份,绵羊291份)用来测定合适的阴阳性阈值。所有样品的平均值为18.07,标准差为8.39,阈值则为35.特异性和敏感性分别为96.18%和91.29%。20份血清的批内重复率从1.9%-5.8%,批间为1.4%-5.0%。所建立的方法具有很好的特异性和敏感性,重复效果好。丰富了国内PPRV血清学检测的研究。相对上述所建立的间接ELISA,具有操作性强、准确性高、适用广泛等特点。
6竞争ELISA检测小反刍兽疫抗体水平
自2007年7月小反刍兽疫在我国西藏地区暴发以来,西藏地区羊只进行了大量的免疫。本研究主要从两个方面对西藏地区和上海市崇明岛的羊只血清样品进行分析,首先用所研制的竞争ELISA试剂盒对西藏部分县和上海市崇明岛的血清样本进行了检测,计算阳性率,显示各地免疫效果。其次对所检测的血清PI值进行统计,显示PPRV抗体水平。为西藏地区免疫计划提供材料。
Peste des petits ruminants (PPR) is a acute infectious disease of small ruminants with a high infection and death rate caused by the PPR virus. It is characterized by high fever, necrotizing gastritis and pneumonia on clinical. The disease was first reported in West Africa, then, the Arabian Peninsula, Israel, Iraq, Jordan, Nigeria, Serbia and Ghana and other countries have reported the disease occurred. At present all countries around the world attach great importance to this disease, and the USA, South Korea, India and other countries are actively carrying on the related research work.
In July,2007, PPR broke out at Ali soil, leather Kyrgyzstan, Zanda and other counties, causing a large number of the local sheep and goat death. Because the disease is new, there is little research on its diagnosis and detection method of infection. This study is to establish ELISA method by chemical synthesis of N protein. The main research includes:
1The chemical synthesis of the Tibetan PPRV-N protein
Firstly, for the purpose of expressing in E.coli, simplifying the complex secondary structure, transforming the restriction enzyme cutting site, and optimizing the rare codons, an overall reconstruction of the Tibetan PPRV-N protein sequence published on GenBank took place by the software such as DNAstar and RNA structure. The homology between the renovated nucleotide sequences and the original sequences is71.9%, and the homology of the both amino acid sequences is100%. Then20pairs of primers were designed and synthesized on the current international advanced chemical synthesis method of gene. Most of the primers were60bp long, and the adjacency opposite primers had21bp repeat sequences. DNA sequences of404bp to414bp were synthesized by polymerase chain reaction (PCR) with5pairs of primers in the non-template condition. Then with the four DNA fragments above as templates, the lateral primers for amplification primers, the gene that expressed the Tibetan PPRV-N protein was synthesized by overlap-PCR method. After comparison, site-directed mutation that appeared in the synthetic process was made a specific modification. Finally the N gene was successfully cloned into the vector simple pMD-19T. The second results showed that the synthetic sequencing of genetic sequences was correct,1578bp length, as expected.
2Cloning, expression, purification and identification of the antigenicity of N gene
Homologous recombination is the most popular and convenient way of cloning, especially for the cloning of long-nucleotide fragment. So in our study this method was used to conduct the molecular cloning. First, the vector primers (15bp) at both ends of coincidence were added into the original gene sequence, and the exogenous genes required for cloning were obtained (Both ends of the original N gene were added into a15bp linearized vector sequence). Close behind acquiring the need genes, linearizing vector occurred, in the role of the homologous recombination enzyme, accompanied with the ribonucleotide sequence (about1600bp) coloned into pET-32a expression vector(5900bp). After sequencing, the correct clone was transformed into E. coli strains B121-DE3-plysS. E. coli bacteria were induced with IPTG to get the expression yields under the conditions of concentration, induction time, induction temperature and the others, and maximized the amount of soluble protein. Total expressed protein bonded to its N monoclonal antibody was detected by western-blot. Under the optimal induction conditions, the supernatant of the expressed product was purified by ion affinity chromatography, which optimized the imidazole content of eluent buffer. The result showed that:the N gene (1600bp) synthesized, was cloned into pET-32a expression vector (5900bp); the N protein could be correctly expressed by prokaryotic; expressed protein could be purified by HIS label, and the purity of purified product can be higher than95%; the expressed protein and its monoclonal antibody could be combined well.
3Establishment of indirect ELISA, and compared with the commercial kit
This study was aimed to measure and ascertain the reaction in PPR indirect ELISA: concentration of coating antibody, dilution of serum, blocking solution, action time of serum, second antibody and substrate. Under different conditions, we chose the max ratio of positive serum OD and negative serum OD as the optimum test conditions to decrease the negative value and increase the positive value. In the optimal conditions we selected the average value of P/N among198negative serum plus two times of the standard deviation as the cut off value. Kit inter and intra coefficients of variation was less than10%, verifying the stability of this ELISA method. Compared with commercial competitive ELISA kit, sensitivity and specificity were96.7%and96.1%, which enrich the serological testing of domestic PPRV.
4Prepration of single epitope peptide antiserum and immune characterization testing
The four major epitope peptides of PPR N protein were chemical synthesized, and the4peptides were used as antigen to be ELISA tested by PPRV-positive serum and RPV-positive serum. The results showed that the19amino acid peptide (RPGRPRGETPGQLLLEIMP) could discriminate the two kinds of serum (PPR and RP) wells. This peptide was used as antigen to immunize5rabbits to produce antibodies. The antibody level significantly raised after90days (titer1:64000). Finally, the antibody titer was verified on ELISA method, and the coated original nuclear proteins and peptides were determined on indirect ELISA. The results indicated that the antibody titers reached its maxlmum after90days, and the prepared antibody was suitable to bind with N protein through prokaryotic expression. This study established the foundation of the competitive ELISA.
5Establishment of competitive ELISA method and comparison with commercial kits
The Nucleocapsid (N) protein of Peste des petits ruminants virus (PPRV) was successfully expressed by prokaryotic as the capture antigen. One epitope (RSGKPRGETPGQLLPEIMQ) of the N protein was chosen and chemically synthesized to immunize rabbits, which showed much higher binding capacity with PPR antibodies than the rinderpest virus (RPV) antibody. The immunized serum was against the single epitope and the tested serum was competitive first antibody. We developed the competitive ELISA(C-ELISA) method to monitor the PPRV antigen in our country. The results of study showed that the optimal antigen concentration is32ng/well, the tested-serum dilution is1:5and the single epitope antibody dilution is1:1000. The cut off value was35, which was derived from mean of negative sera plus diploid standard deviation. Compared with the commercial competitive ELISA test, the sensitivity and specificity of this C-ELISA were96.18%and91.29%respectively by testing1039serum samples.
6Detection of PPR sera
Since PPR outbreak in Tibet in China in July2007, a large number of goats were immunized in Tibet. Three main aspects of Tibetan serum samples were analyzed:Firstly, the competitive ELISA kits were used to test serum samples in some counties of Tibet and the positive rate was calculated, showing the immune effect. Secondly, the calculation of PI value showed PPRV antibody level. The result served for immunization programs in Tibet.
目前,该病尚无有效的治疗方法,主要是靠疫苗免疫以及血清学监控来预防此病的蔓延。然而该病属于高致病性传染病,一般实验室无法进行病原操作。并且首次传入我国,缺乏此方面的研究基础。本研究基于建立完善的血清学检测方法,应用化学合成的N蛋白,制备N蛋白单表位抗体,建立两种不同方式的ELISA检测方法。对方法进行了优化,提高其稳定性、重复性和敏感度,样品检测结果表明：方法的实用性强,结果确实可靠,科学有效,能够应用于临床实践中。主要研究内容包括：
1西藏株小反刍兽疫N蛋白的化学合成
首先应用DNAstar和RNA structure等软件对GenBank所发表的西藏株小反刍兽疫N蛋白序列进行了编辑修改,避免了复杂的二级结构,改造了酶切位点,优化了稀有密码子,全基因的核苷酸序列和原序列同源性仅71.9%,氨基酸序列同源性100%,以便于基因序列能够在大肠杆菌中原核表达。然后参考了目前国际较为先进的基因化学合成的方法,设计并合成了20对引物,引物长度大部分在60bp,相邻引物方向相反,并且序列重复21bp。分别以5对引物为材料,在无模板的状态下,通过PCR反应化学合成4段长度在404～414bp的双链DNA片段。然后以上述4段DNA片段为模板,以最外侧引物为引物,通过overlap-PCR法化学合成了可以表达西藏株小反刍兽疫N蛋白的基因。测序比对后,针对在合成过程中出现的定点突变进行了人工回复突变。最后成功克隆入载体simple pMD-19T。再次测序结果表明所合成的基因序列正确,长度1578bp,和预期相符。
2N蛋白基因的克隆、表达、产物纯化纯化及免疫性质鉴定
同源重组法是目前较为流行且便捷的克隆方式；特别适合长片段核苷酸的克隆。本研究运用此方法进行分子克隆,首先设计在原基因片段加入15bp和载体两端重合序列的引物,通过PCR获得克隆所需的外源基因(原N基因两端各加入15bp线性化载体两端的序列),然后把载体酶切线性化,利用同源重组酶的作用,一次性把长达约1600bp的核苷酸片段成功克隆入长达5900bp的表达载体pET-32a。测序后正确的克隆转化入大肠杆菌株Bl21-DE3-plysS。用IPTG进行诱导,尝试了其不同浓度、诱导时间、诱导温度等条件下的表达产量,并且尽量增加可溶性蛋白的表达量。所表达的总蛋白使用N蛋白单克隆抗体进行western-blot检测。最适诱导条件下的表达产物的上清通过离子亲和层析法纯化,优化洗脱液的咪唑含量。研究结果表明：化学合成的长达1600bp的N基因通过同源重组法可以简单而且低背景的克隆入5900bp的表达载体pET-32a；可以通过原核系统正确表达N蛋白；所表达蛋白用HIS标签可以纯化,纯化产物纯度高于95%；表达的蛋白可与此蛋白的单克隆抗体可以较好的结合。
3小反刍兽疫间接ELISA方法的建立及与商品化试剂盒检测对比
为建立特异性强、灵敏度高的PPR间接ELISA方法,本文研究了间接ELISA的抗原包被浓度、血清稀释浓度、封闭液、封闭时间、血清稀释液、血清作用时间、二抗和底物作用时间等参数。在不同的条件下,选择阳性血清OD值：阴性血清OD值比值最大的条件为最适检测条件。降低了阴性背景值,提高了阳性值。在最佳化条件的基础上选择了198份阴性血清的平均P/N值加二倍标准差作为·cut off值。试剂盒批内和批间的变异系数均小于10%,验证了此ELISA方法的稳定性。对比商品化竞争ELISA试剂盒,敏感性和特异性分别为96.7%和96.1%,丰富了国内PPRV血清学的检测。
4单表位多肽抗血清的制备及免疫性质鉴定
化学方法合成了小反刍兽疫N蛋白中4个重要的抗原表位的多肽,以这4段多肽作为抗原分别用PPRV阳性血清和RPV阳性血清进行ELISA检测,结果表明19个氨基酸的多肽RPGRPRGETPGQLLLEIMP可以较好的区分两种血清。然后用此多肽作为抗原免疫了5只家免,制备了抗血清,血清抗体滴度在90d后较高(1：64000滴度)。最后通过ELISA方法继续验证抗体的滴度,分别包被了原核表达的N蛋白和多肽,进行了间接ELISA的测定,结果表明90天后抗体滴度最高,所制备的抗体更适合与原核表达产物N蛋白结合,为建立竞争ELISA检测方法奠定了基础。
5小反刍兽疫抗血清检测的竞争ELISA方法的建立
利用化学合成的多肽免疫兔得到兔单表位抗血清,以N蛋白作为捕获抗原,用兔的高免血清和待检血清竞争,建立竞争ELISA方法以便用于国内小反刍兽疫的血清学监测。研究表明最佳化的检测条件为：包被抗原浓度为320ng/g1,100μl/孔为最适抗原包被浓度；倍比稀释待检阴阳性血清和竞争兔高免血清,测得PI差距最大为50.8,抗原抗体的结合及竞争时间为1小时。选取489份已知PPRV抗体阴性的血清(山羊198份,绵羊291份)用来测定合适的阴阳性阈值。所有样品的平均值为18.07,标准差为8.39,阈值则为35.特异性和敏感性分别为96.18%和91.29%。20份血清的批内重复率从1.9%-5.8%,批间为1.4%-5.0%。所建立的方法具有很好的特异性和敏感性,重复效果好。丰富了国内PPRV血清学检测的研究。相对上述所建立的间接ELISA,具有操作性强、准确性高、适用广泛等特点。
6竞争ELISA检测小反刍兽疫抗体水平
自2007年7月小反刍兽疫在我国西藏地区暴发以来,西藏地区羊只进行了大量的免疫。本研究主要从两个方面对西藏地区和上海市崇明岛的羊只血清样品进行分析,首先用所研制的竞争ELISA试剂盒对西藏部分县和上海市崇明岛的血清样本进行了检测,计算阳性率,显示各地免疫效果。其次对所检测的血清PI值进行统计,显示PPRV抗体水平。为西藏地区免疫计划提供材料。
Peste des petits ruminants (PPR) is a acute infectious disease of small ruminants with a high infection and death rate caused by the PPR virus. It is characterized by high fever, necrotizing gastritis and pneumonia on clinical. The disease was first reported in West Africa, then, the Arabian Peninsula, Israel, Iraq, Jordan, Nigeria, Serbia and Ghana and other countries have reported the disease occurred. At present all countries around the world attach great importance to this disease, and the USA, South Korea, India and other countries are actively carrying on the related research work.
In July,2007, PPR broke out at Ali soil, leather Kyrgyzstan, Zanda and other counties, causing a large number of the local sheep and goat death. Because the disease is new, there is little research on its diagnosis and detection method of infection. This study is to establish ELISA method by chemical synthesis of N protein. The main research includes:
1The chemical synthesis of the Tibetan PPRV-N protein
Firstly, for the purpose of expressing in E.coli, simplifying the complex secondary structure, transforming the restriction enzyme cutting site, and optimizing the rare codons, an overall reconstruction of the Tibetan PPRV-N protein sequence published on GenBank took place by the software such as DNAstar and RNA structure. The homology between the renovated nucleotide sequences and the original sequences is71.9%, and the homology of the both amino acid sequences is100%. Then20pairs of primers were designed and synthesized on the current international advanced chemical synthesis method of gene. Most of the primers were60bp long, and the adjacency opposite primers had21bp repeat sequences. DNA sequences of404bp to414bp were synthesized by polymerase chain reaction (PCR) with5pairs of primers in the non-template condition. Then with the four DNA fragments above as templates, the lateral primers for amplification primers, the gene that expressed the Tibetan PPRV-N protein was synthesized by overlap-PCR method. After comparison, site-directed mutation that appeared in the synthetic process was made a specific modification. Finally the N gene was successfully cloned into the vector simple pMD-19T. The second results showed that the synthetic sequencing of genetic sequences was correct,1578bp length, as expected.
2Cloning, expression, purification and identification of the antigenicity of N gene
Homologous recombination is the most popular and convenient way of cloning, especially for the cloning of long-nucleotide fragment. So in our study this method was used to conduct the molecular cloning. First, the vector primers (15bp) at both ends of coincidence were added into the original gene sequence, and the exogenous genes required for cloning were obtained (Both ends of the original N gene were added into a15bp linearized vector sequence). Close behind acquiring the need genes, linearizing vector occurred, in the role of the homologous recombination enzyme, accompanied with the ribonucleotide sequence (about1600bp) coloned into pET-32a expression vector(5900bp). After sequencing, the correct clone was transformed into E. coli strains B121-DE3-plysS. E. coli bacteria were induced with IPTG to get the expression yields under the conditions of concentration, induction time, induction temperature and the others, and maximized the amount of soluble protein. Total expressed protein bonded to its N monoclonal antibody was detected by western-blot. Under the optimal induction conditions, the supernatant of the expressed product was purified by ion affinity chromatography, which optimized the imidazole content of eluent buffer. The result showed that:the N gene (1600bp) synthesized, was cloned into pET-32a expression vector (5900bp); the N protein could be correctly expressed by prokaryotic; expressed protein could be purified by HIS label, and the purity of purified product can be higher than95%; the expressed protein and its monoclonal antibody could be combined well.
3Establishment of indirect ELISA, and compared with the commercial kit
This study was aimed to measure and ascertain the reaction in PPR indirect ELISA: concentration of coating antibody, dilution of serum, blocking solution, action time of serum, second antibody and substrate. Under different conditions, we chose the max ratio of positive serum OD and negative serum OD as the optimum test conditions to decrease the negative value and increase the positive value. In the optimal conditions we selected the average value of P/N among198negative serum plus two times of the standard deviation as the cut off value. Kit inter and intra coefficients of variation was less than10%, verifying the stability of this ELISA method. Compared with commercial competitive ELISA kit, sensitivity and specificity were96.7%and96.1%, which enrich the serological testing of domestic PPRV.
4Prepration of single epitope peptide antiserum and immune characterization testing
The four major epitope peptides of PPR N protein were chemical synthesized, and the4peptides were used as antigen to be ELISA tested by PPRV-positive serum and RPV-positive serum. The results showed that the19amino acid peptide (RPGRPRGETPGQLLLEIMP) could discriminate the two kinds of serum (PPR and RP) wells. This peptide was used as antigen to immunize5rabbits to produce antibodies. The antibody level significantly raised after90days (titer1:64000). Finally, the antibody titer was verified on ELISA method, and the coated original nuclear proteins and peptides were determined on indirect ELISA. The results indicated that the antibody titers reached its maxlmum after90days, and the prepared antibody was suitable to bind with N protein through prokaryotic expression. This study established the foundation of the competitive ELISA.
5Establishment of competitive ELISA method and comparison with commercial kits
The Nucleocapsid (N) protein of Peste des petits ruminants virus (PPRV) was successfully expressed by prokaryotic as the capture antigen. One epitope (RSGKPRGETPGQLLPEIMQ) of the N protein was chosen and chemically synthesized to immunize rabbits, which showed much higher binding capacity with PPR antibodies than the rinderpest virus (RPV) antibody. The immunized serum was against the single epitope and the tested serum was competitive first antibody. We developed the competitive ELISA(C-ELISA) method to monitor the PPRV antigen in our country. The results of study showed that the optimal antigen concentration is32ng/well, the tested-serum dilution is1:5and the single epitope antibody dilution is1:1000. The cut off value was35, which was derived from mean of negative sera plus diploid standard deviation. Compared with the commercial competitive ELISA test, the sensitivity and specificity of this C-ELISA were96.18%and91.29%respectively by testing1039serum samples.
6Detection of PPR sera
Since PPR outbreak in Tibet in China in July2007, a large number of goats were immunized in Tibet. Three main aspects of Tibetan serum samples were analyzed:Firstly, the competitive ELISA kits were used to test serum samples in some counties of Tibet and the positive rate was calculated, showing the immune effect. Secondly, the calculation of PI value showed PPRV antibody level. The result served for immunization programs in Tibet.
引文
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[1]Balamurugan V, Sen A, Saravanan P, et al. Development and characterization of a stable vero cell line constitutively expressing Peste des petits ruminants virus (PPRV) hemagglutinin protein and its potential use as antigen in enzyme-linked immunosorbent assay for serosurveillance of PPRV [J]. Clin Vaccine Immunol,2006,13(12):1367-1372.
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[1]Bao J, Li L, Wang Z, Barrett T, et al. Development of one-step real-time RT-PCR assay for detection and quantitation of peste des petits ruminants virus [J]. J Virol Methods,2008, 148(1-2):232-236.
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[1]Balamurugan V, Sen A, Saravanan P, et al. Development and characterization of a stable vero cell line constitutively expressing Peste des petits ruminants virus (PPRV) hemagglutinin protein and its potential use as antigen in enzyme-linked immunosorbent assay for serosurveillance of PPRV [J]. Clin Vaccine Immunol,2006,13(12):1367-1372.
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