猪IgG Fc受体及其介导PRRSV抗体依赖增强作用研究
|
摘要
Fc受体(FcR)为特异亲和免疫球蛋白(Ig) Fc片段的细胞表面分子,广泛表达于免疫细胞表面,具有许多重要的生理功能,是体液免疫与细胞免疫的联系纽带,在机体免疫调控中起关键作用。目前人和小鼠的三类IgG Fc受体(FcγRI、FcγRII和FcγIII)研究最为深入。本研究克隆和鉴定了猪IgG三类Fc受体;研究了PRRSV变异毒株和经典毒株感染后活化性Fc受体和抑制性Fc受体的转录动态差异及与免疫抑制的关系;构建了稳定表达猪FcγRII的Marc-145细胞系,研究了该受体在介导PRRSV ADE中的重要作用。
用人CD64氨基酸序列检索NCBI的EST数据库(包括除人和老鼠以外的所有物种核苷酸序列)(tBLASTn),发现了6个猪的高同源overlapping序列,利用这些序列信息设计引物,采用RT-PCR从猪外周血白细胞中扩增到了猪FcγRI cDNA序列,命名为poFcγRI。poFcγRI ORF全长1038 bp,编码346氨基酸的糖蛋白。胞外区包括三个Ig样结构,有4个N-糖基化位点。poFcγRI和人、牛与老鼠的FcγRI在氨基酸水平上分别有79%、69%和57%的相似性。胞外环区相似性较高,分别为77%、74%和70%,这提示人、牛、猪、鼠的FcγRI和IgG的结合域高度保守。随后,RT-PCR检测到了poFcγRI mRNA在巨噬细胞、单核细胞中表达量较高,在多形核细胞中也有表达,在淋巴细胞中没有表达,和人与小鼠CD64的表达谱类似。将poFcγRI ORF基因亚克隆到真核表达载体pcDNA构建成重组质粒pcDNA/poFcγRI,再用脂质体法转染COS-7细胞,用玫瑰花环实验鉴定了poFcγRI配体亲和特性。
对猪IgG Fc受体的进一步研究发现猪IgG Fc受体共由三类分子组成,即FcγRI、FcγRII和FcγIII,克隆了这三类受体cDNA,其中FcγRII胞内区有保守的ITIM基序,为抑制性受体;FcγRI和FcγRIII胞内区没有发现已知的信号传导基序,通过γ链的ITAM基序进行信号转导,因而这两个受体为活化性受体。发现FcγRII至少存在两个亚类,即FcγRIIB1和FcγRIIB2,FcγRIIB1胞内区有一插入序列,使胞内区由47个氨基酸延长到99个氨基酸。这两个亚类胞内区均存在ITIM基序,因此均为抑制性受体。
活化型受体和抑制型受体共表达于免疫细胞表面,共同调节抗体对免疫细胞的活化作用。抗原抗体复合物和免疫细胞表面的活化型受体给合,能活化免疫效应细胞,诱发多种免疫学效应。抑制型受体的作用刚好相反,通过免疫复合物与抑制型受体交联,抑制活化受体介导的细胞活化。研究PRRSV感染后活化型和抑制型Fc受体的转录动态,对于揭示PRRSV感染引起的免疫抑制有重要意义。通过Real-time PCR检测不同毒株PRRSV感染后猪体活化性和抑制性Fc受体的转录动态,发现PRRSV感染后活化性受体FcγRI和FcγRIII均迅速下调,而抑制性Fc受体FcγRII感染后有轻微上调。PRRSV感染后机体能够快速诱导产生高水平的特异性抗体,但感染后活化性Fc受体下调导致抗体和抗原抗体复合物不能活化免疫效应细胞,从而引起细胞免疫功能下降,这是PRRSV感染引起免疫抑制的分子基础。
抗体依赖增强作用(ADE)是PRRS防控中遇到的最大的难题之一。本研究将猪FcγRII基因转染Marc-145细胞,通过G418连续筛选和克隆获得了稳定表达猪FcγRII的Marc-145细胞系。用PRRSV BJ-4株与1:320稀释的抗PRRSV IgG感染克隆化的Marc-145细胞系,在有抗体存在的情况下PRRSV感染收获的病毒量明显高于对照组,证明了poFcγRII能够介导PRRSV ADE作用。在PRRSV免疫效果评价当中,现有的评价标准是测定疫苗免疫后的PRRSV特异性抗体。但ADE作用的存在使PRRSV特异抗体在特定情况下不仅没有保护作用,反而有助于感染。本研究构建的稳定表达猪FcγRII的Marc-145细胞系能够方便的评价抗体的ADE作用,从而为研制高效PRRSV疫苗提供技术支持。
Fc receptors (FcR) are a group of crucial molecules expressed on the surface of immune cells, which bind the Fc region of immunoglobulins with specific affinities and have a number of important biological functions. FcRs play a critical role in immune regulation by providing a link between the humoral and cellular immune responses. Three classes of FcγR (FcγRI, II, III), present in human and mouse, are the best characterized. In this study, three classes of porcine FcγRs was cloned and characterized. The relationship between immune suppression and dynamic expression of porcine activation and inhibitory FcγRs after infection with PRRSV isolates was investigated. Porccine FcγRII was been proved playing a crucial role in mediation the antibody-dependent enhancement (ADE) of PRRSV infection by construction the Marc-145 cell line with stable poFcγRII expression.
By screening a translated EST database (which is composed of sequences from specieces other than human and mouse) with the protein sequence of the human CD64,we identified six putative overlapping porcine homologues. With this sequence information,a pair of primers was designed and the full-length cDNA encoding porcine FcγRI we isolated (poFcγRI) from peripheral blood leucocyte RNA using RT-PCR. Porcine FcγRI contains an open-reading frame (ORF) of 1038 bp length, encoding a 346 amino acids glycoprotein. Extracellular domain of poFcγRI consists of three Ig-like domains and four N-glycosylation sites. The predicted amino acid sequence of whole poFcγRI was found to be 79%, 69% and 57% identitical with human, bovine and mouse counterpart; however, a comparison of the three extracellular domains alone between the four species shows a higher identity of 77%, 74% and 70% respectively. This is in agreement with the generally highly conserved nature of the individual FcR binding domains. In order to examine the cell distribution of poFcγRI, RT-PCR was performed on mRNA from selective cellular subsets. Porcine FcγRI is expressed in PAM, monocytes, and PMN. A higher abundance of transcripts was found in PAM and monocytes than in PMN, where only a trace transcript was found. Then, a cDNA for the complete coding region of poFcγRI was subcloned into the expression vector pcDNA3, and transfected into COS-7 cells. The COS-7 cells transfected with the poFcγRI cDNA were able to bind chicken erythrocytes sensitized with porcine IgG.
Three classes of porcine FcγR, named FcγRI, FcγRII and FcγIII, was further characterized. Of which, poFcγRII belongs to inhibitory Fc receptor, as an ITIM motif was found in intracellular domain. Whereas, porcine FcγRII and FcγIII, devoid of know signal motif, seem to be activatory Fc receptors and that they may form an activation receptor complex withγchain on the surface of immune cells. Two isoforms of poFcγRII, FcγRIIB1 and FcγRIIB2 were further identified. FcγRIIB1 has an in-frame insertion, which increases the cytoplasmic region from 47 to 99 amino acids. The two isoforms have ITIM motif in the intracellular domain, so they both belong to the inhibitory receptors.
The paired expression of activating and inhibitory molecules on the same cell is the key for the generation of a balanced immune response. After binding with the activating Fc receptor, immune cells can be activated and a variety of immunological effects were induced by antigen-antibody complex. The role of inhibitory receptors is exactly the opposite. Thus, it is important to study the activating and inhibitory Fc receptor transcription dynamicas after PRRSV infection for further invesitgaiton the immune suppression by PRRSV infection. Using real-time PCR, the activating and inhibitory Fc receptor transcription dynamic in porcine peripheral blood leucytes was investigated after infection with PRRSV isolates. The expression of activation receptor, FcγRI and FcγRIII, was found to be rapidly reduced, and the inhibitory Fc receptor, poFcγRII, had a slight increase after infection. PRRSV infection rapidly induced high levels of PRRSV-specific antibodies, but the the immune effector cells were not to be activated by antibody and antigen-antibody complex due to the decreased expression of activating FcγRs. This may be the molecular basis of immunosuppression after PRRSV infection.
Antibody-dependent enhancement (ADE) is one of the major problems in prevention and control PRRS. In this study, poFcγRII gene was transfected to Marc-145 cells. After G418 selection and continuous cloning, construction of Marc-145 cell line with stable expression of poFcγRII was achieved. Then, Marc-145 cell lines with stable poFcγRII expression was infected with PRRSV BJ-4 strain and 1:320 dilution of anti-PRRSV IgG together or PRRSV alone. The harvested virus of Marc-145 cell lines infection with PRRSV and antibody together was significantly higher than that of PRRSV absence of antibody. Thus, poFcγRII mediated the ADE of PRRSV infection. The existing evaluation criteria for the effect of PRRSV vaccine is determined by detection of the PRRSV vaccine specific antibodies. As ADE of PRRSV infection, PRRSV-specific antibodies could not protect pigs from PRRSV infection and contribute to infection in some cases. In this study, Marc-145 cell lines with stable poFcγRII expression can be used for evaluation the ADE effect of antibodies, so it will provide technical support for develop ping efficient PRRSV vaccines.
用人CD64氨基酸序列检索NCBI的EST数据库(包括除人和老鼠以外的所有物种核苷酸序列)(tBLASTn),发现了6个猪的高同源overlapping序列,利用这些序列信息设计引物,采用RT-PCR从猪外周血白细胞中扩增到了猪FcγRI cDNA序列,命名为poFcγRI。poFcγRI ORF全长1038 bp,编码346氨基酸的糖蛋白。胞外区包括三个Ig样结构,有4个N-糖基化位点。poFcγRI和人、牛与老鼠的FcγRI在氨基酸水平上分别有79%、69%和57%的相似性。胞外环区相似性较高,分别为77%、74%和70%,这提示人、牛、猪、鼠的FcγRI和IgG的结合域高度保守。随后,RT-PCR检测到了poFcγRI mRNA在巨噬细胞、单核细胞中表达量较高,在多形核细胞中也有表达,在淋巴细胞中没有表达,和人与小鼠CD64的表达谱类似。将poFcγRI ORF基因亚克隆到真核表达载体pcDNA构建成重组质粒pcDNA/poFcγRI,再用脂质体法转染COS-7细胞,用玫瑰花环实验鉴定了poFcγRI配体亲和特性。
对猪IgG Fc受体的进一步研究发现猪IgG Fc受体共由三类分子组成,即FcγRI、FcγRII和FcγIII,克隆了这三类受体cDNA,其中FcγRII胞内区有保守的ITIM基序,为抑制性受体;FcγRI和FcγRIII胞内区没有发现已知的信号传导基序,通过γ链的ITAM基序进行信号转导,因而这两个受体为活化性受体。发现FcγRII至少存在两个亚类,即FcγRIIB1和FcγRIIB2,FcγRIIB1胞内区有一插入序列,使胞内区由47个氨基酸延长到99个氨基酸。这两个亚类胞内区均存在ITIM基序,因此均为抑制性受体。
活化型受体和抑制型受体共表达于免疫细胞表面,共同调节抗体对免疫细胞的活化作用。抗原抗体复合物和免疫细胞表面的活化型受体给合,能活化免疫效应细胞,诱发多种免疫学效应。抑制型受体的作用刚好相反,通过免疫复合物与抑制型受体交联,抑制活化受体介导的细胞活化。研究PRRSV感染后活化型和抑制型Fc受体的转录动态,对于揭示PRRSV感染引起的免疫抑制有重要意义。通过Real-time PCR检测不同毒株PRRSV感染后猪体活化性和抑制性Fc受体的转录动态,发现PRRSV感染后活化性受体FcγRI和FcγRIII均迅速下调,而抑制性Fc受体FcγRII感染后有轻微上调。PRRSV感染后机体能够快速诱导产生高水平的特异性抗体,但感染后活化性Fc受体下调导致抗体和抗原抗体复合物不能活化免疫效应细胞,从而引起细胞免疫功能下降,这是PRRSV感染引起免疫抑制的分子基础。
抗体依赖增强作用(ADE)是PRRS防控中遇到的最大的难题之一。本研究将猪FcγRII基因转染Marc-145细胞,通过G418连续筛选和克隆获得了稳定表达猪FcγRII的Marc-145细胞系。用PRRSV BJ-4株与1:320稀释的抗PRRSV IgG感染克隆化的Marc-145细胞系,在有抗体存在的情况下PRRSV感染收获的病毒量明显高于对照组,证明了poFcγRII能够介导PRRSV ADE作用。在PRRSV免疫效果评价当中,现有的评价标准是测定疫苗免疫后的PRRSV特异性抗体。但ADE作用的存在使PRRSV特异抗体在特定情况下不仅没有保护作用,反而有助于感染。本研究构建的稳定表达猪FcγRII的Marc-145细胞系能够方便的评价抗体的ADE作用,从而为研制高效PRRSV疫苗提供技术支持。
Fc receptors (FcR) are a group of crucial molecules expressed on the surface of immune cells, which bind the Fc region of immunoglobulins with specific affinities and have a number of important biological functions. FcRs play a critical role in immune regulation by providing a link between the humoral and cellular immune responses. Three classes of FcγR (FcγRI, II, III), present in human and mouse, are the best characterized. In this study, three classes of porcine FcγRs was cloned and characterized. The relationship between immune suppression and dynamic expression of porcine activation and inhibitory FcγRs after infection with PRRSV isolates was investigated. Porccine FcγRII was been proved playing a crucial role in mediation the antibody-dependent enhancement (ADE) of PRRSV infection by construction the Marc-145 cell line with stable poFcγRII expression.
By screening a translated EST database (which is composed of sequences from specieces other than human and mouse) with the protein sequence of the human CD64,we identified six putative overlapping porcine homologues. With this sequence information,a pair of primers was designed and the full-length cDNA encoding porcine FcγRI we isolated (poFcγRI) from peripheral blood leucocyte RNA using RT-PCR. Porcine FcγRI contains an open-reading frame (ORF) of 1038 bp length, encoding a 346 amino acids glycoprotein. Extracellular domain of poFcγRI consists of three Ig-like domains and four N-glycosylation sites. The predicted amino acid sequence of whole poFcγRI was found to be 79%, 69% and 57% identitical with human, bovine and mouse counterpart; however, a comparison of the three extracellular domains alone between the four species shows a higher identity of 77%, 74% and 70% respectively. This is in agreement with the generally highly conserved nature of the individual FcR binding domains. In order to examine the cell distribution of poFcγRI, RT-PCR was performed on mRNA from selective cellular subsets. Porcine FcγRI is expressed in PAM, monocytes, and PMN. A higher abundance of transcripts was found in PAM and monocytes than in PMN, where only a trace transcript was found. Then, a cDNA for the complete coding region of poFcγRI was subcloned into the expression vector pcDNA3, and transfected into COS-7 cells. The COS-7 cells transfected with the poFcγRI cDNA were able to bind chicken erythrocytes sensitized with porcine IgG.
Three classes of porcine FcγR, named FcγRI, FcγRII and FcγIII, was further characterized. Of which, poFcγRII belongs to inhibitory Fc receptor, as an ITIM motif was found in intracellular domain. Whereas, porcine FcγRII and FcγIII, devoid of know signal motif, seem to be activatory Fc receptors and that they may form an activation receptor complex withγchain on the surface of immune cells. Two isoforms of poFcγRII, FcγRIIB1 and FcγRIIB2 were further identified. FcγRIIB1 has an in-frame insertion, which increases the cytoplasmic region from 47 to 99 amino acids. The two isoforms have ITIM motif in the intracellular domain, so they both belong to the inhibitory receptors.
The paired expression of activating and inhibitory molecules on the same cell is the key for the generation of a balanced immune response. After binding with the activating Fc receptor, immune cells can be activated and a variety of immunological effects were induced by antigen-antibody complex. The role of inhibitory receptors is exactly the opposite. Thus, it is important to study the activating and inhibitory Fc receptor transcription dynamicas after PRRSV infection for further invesitgaiton the immune suppression by PRRSV infection. Using real-time PCR, the activating and inhibitory Fc receptor transcription dynamic in porcine peripheral blood leucytes was investigated after infection with PRRSV isolates. The expression of activation receptor, FcγRI and FcγRIII, was found to be rapidly reduced, and the inhibitory Fc receptor, poFcγRII, had a slight increase after infection. PRRSV infection rapidly induced high levels of PRRSV-specific antibodies, but the the immune effector cells were not to be activated by antibody and antigen-antibody complex due to the decreased expression of activating FcγRs. This may be the molecular basis of immunosuppression after PRRSV infection.
Antibody-dependent enhancement (ADE) is one of the major problems in prevention and control PRRS. In this study, poFcγRII gene was transfected to Marc-145 cells. After G418 selection and continuous cloning, construction of Marc-145 cell line with stable expression of poFcγRII was achieved. Then, Marc-145 cell lines with stable poFcγRII expression was infected with PRRSV BJ-4 strain and 1:320 dilution of anti-PRRSV IgG together or PRRSV alone. The harvested virus of Marc-145 cell lines infection with PRRSV and antibody together was significantly higher than that of PRRSV absence of antibody. Thus, poFcγRII mediated the ADE of PRRSV infection. The existing evaluation criteria for the effect of PRRSV vaccine is determined by detection of the PRRSV vaccine specific antibodies. As ADE of PRRSV infection, PRRSV-specific antibodies could not protect pigs from PRRSV infection and contribute to infection in some cases. In this study, Marc-145 cell lines with stable poFcγRII expression can be used for evaluation the ADE effect of antibodies, so it will provide technical support for develop ping efficient PRRSV vaccines.
引文
[1] Zhang G. Bovine IgG Fc Receptors (PhD Thesis), University of Hertfordshire, Hatfield. 1994.
[2] Daeron M. Fc receptor biology. Annu. Rev. Immunol. 1997.15: 203-234.
[3] Ravetch JV. Fc receptors. Curr. Opin. Immunol. 1997. 9: 121-125.
[4] Ravetch JV and Bolland S. IgG Fc receptors. Annu. Rev. Immunol. 2001. 19: 275-290.
[5] Cohen-Solal JF, Cassard L, Fridman WH and Sautes-Fridman C. Fcγreceptors. Immunol. Lett. 2004. 92: 199-205.
[6] Berken A. and Benacerraf B. Properties of antibodies cytophilic for macrophages. J. Exp. Med. 1966. 123: 119-144.
[7] Paraskevas F, Lee ST, Orr KB and Israels LG. A receptor for Fc on mouse B-lymphocytes. J. Immunol. 1972. 108: 1319-1327.
[8] Metzger H, Alcaraz G, Hohman R, et al. The receptor with high affinity for immunoglobulin E. Annu. Rev. Immunol. 1986. 4: 419-470.
[9] Woof JM and Burton DR. Human antibody-Fc receptor interactions illuminated by crystal structures. Nat. Rev. Immunol. 2004. 4: 89-99.
[10] Takai T. Fc receptors and their role in immune regulation and autoimmunity. J. Clin. Immunol. 2005. 25: 1-18.
[11] Kacskovics I. Fc receptors in livestock species. Vet. Immunol. Immunopathol. 2004. 102: 351-362.
[12] Raghavan M and Bjorkman PJ. Fc receptors and their interactions with immunoglobulins. Annu. Rev. Cell Dev. Biol. 1996. 12: 181-220.
[13] Bolland S. A newly discovered Fc receptor that explains IgG-isotype disparities in effector responses. Immunity. 2005. 23: 2-4.
[14] Allen JM, Seed B. Isolation and expression of functional high-affinity Fc receptor complementary DNAs. Science. 1989. 243:378-381
[15] Nimmerjahn F, Bruhns P, Horiuchi K and Ravetch JV. FcγRIV: A novel FcR with distinct IgG subclass specificity. Immunity. 2005. 23: 41-51.
[16] Nimmerjahn F, Ravetch JV. Divergent immunoglobulin G subclass activity through selective Fc receptor binding. Science. 2005. 31: 1510-1512 .
[17] Jefferis R and Lund J. Interaction sites on human IgG-Fc for FcR: current models. Immnunol. Lett. 2002. 82 : 57-65.
[18] Pasquier B, Launay P, Kanamaru Y, et al. Identification of FcαRI as an inhibitory receptor that controls inflammation: dual role of FcRγITAM. Immunity 2005. 22: 31-42.
[19] Ravetch JV and Kinet JP. Fc receptors. Annu. Rev. Immunol. 1991. 9: 475-492.
[20] Hulett MD and Hogarth PM. Molecular basis of Fc receptor function. Adv. Immunol. 1994. 57: 1-127.
[21] Mechetina LV, Najakshin AM, Alabyev BY, et al. Identification of CD16-2, a novel mouse receptor homologous to CD16/Fc gamma RIII. Immunogenetics. 2002.54: 463-468
[22] Davis RS, Dennis GJ, Odom MR, et al. Fc receptor homologs: newest members of a remarkable diverse Fc receptor gene family. Immunol. Rev. 2002.190: 123-136
[23] Symons DB and Clarkson CA. Genomic organisation and sequence of the extracellular domain exons of the bovine FcγRI receptor, and evidence for restricted binding of ruminant IgG to U937 cells. Mol. Immunol. 1992. 29: 1407-1413.
[24] Yan Y, Li X, Wang A and Zhang G. Molecular cloning and identification of full-length cDNA encoding high affinity Fc receptor for bovine IgG (FcγRI). Vet. Immunol. Immunopathol. 2000. 75: 151-159.
[25] Zhang G, Young JR, Tregaskes CR, Howard CJ. Cattle Fc gamma RII: molecular cloning and ligand specificity. Immunogenetics. 1994. 39: 423–427.
[26] Collins RA, Gelder KI and Howard CJ. Nucleotide sequence of cattle FcGRIII: its identification in gammadelta T cells. Immunogenetics. 1997. 45: 440-443.
[27] Yan Y, Zhang G, Chen C, et al. Bovine FcγRIII with a single extracellular domain. Res. Vet. Sci. 2000. 68: 115-118.
[28] Watson JL, Jackson KA, King DP and Stott JL. Molecular cloning and sequencing of the low-affinity IgE receptor (CD23) for horse and cattle. Vet. Immunol. Immunopathol. 2000. 73: 323-329.
[29] Morton HC, Pleass RJ, Storset AK, et al. Cloning and characterization of an immunoglobulin A Fc receptor from cattle. Immunology. 2004. 111: 204-211.
[30] Zhang G, Young JR, Tregaskes CA, et al. Identification of a novel class of mammalian Fcγreceptor. J. Immunol. 1995. 155: 1534-1541.
[31] Morton HC, Storset AK and Brandtzaeg P. Cloning and sequencing of a cDNA encoding the bovine FcRγchain. Vet. Immunol. Immunopathol. 2001. 82: 101-106.
[32] Verbeet MP, Vermeer H, Warmerdam GC, et al. Cloning and characterization of the bovine polymeric immunoglobulin receptor-encoding cDNA. Gene. 1995. 164: 329–333
[33] Kulseth MA, Krajci P, Myklebost O, Rogne S. Cloning and characterization of two forms of bovine polymeric immunoglobulin receptor cDNA. DNA Cell Biol. 1995.14: 251–256.
[34] Kacskovics I, Wu Z, Simister NE, et al. Cloning and characterization of the bovine MHC class I-like Fc receptor. J. Immunol. 2000. 164: 1889-1897.
[35] McAleese SM, Halliwell RE and Miller HR. Cloning and sequencing of the horse and sheep high-affinity IgE receptorαchain cDNA. Immunogenetics. 2000. 51: 878-881.
[36] McAleese SM and Miller HR. Cloning and sequencing of the equine and ovine high-affinity IgE receptorβ- andγ-chain cDNA. Immunogenetics. 2003. 55: 122-125.
[37] Mayer B, Zolnai A, Frenyo LV, et al. Redistribution of the sheep neonatal Fc receptor in the mammary gland around the time of parturition in ewes and its localization in the small intestine of neonatal lambs. Immunology. 2002. 107: 288–296.
[38] Halloran PJ, Sweeney SE, Strohmeier CM and Kim YB. Molecular cloning and identification of the porcine cytolytic trigger molecule G7 as a FcγRIIIα(CD16) homologue. J. Immunol. 1994. 153: 2631-2641.
[39] Yim D, Jie HB, Lanier LL and Kim YB. Molecular cloning, gene structure, and expression pattern of pig immunoreceptor DAP12. Immunogenetics.2000. 51: 436-442.
[40] Kumura BH, Sone T, Shimazaki K, Kobayashi E. Sequence analysis of porcine polymeric immunoglobulin receptor from mammary epithelial cells present in colostrum. J. Dairy Res. 2000. 67: 631–636.
[41] Morton HC, Pleass RJ, Storset AK, et al. Cloning and characterization of equine CD89 and identification of the CD89 gene in chimpanzees and rhesus macaques. Immunology 2005. 115: 74-84.
[42] Flesch BK and Neppert J. Functions of the Fc receptors for immunoglobulin G. J. Clin. Lab. Anal. 2000.14: 141-156.
[43] Fossati G, Bucknall RC and Edwards SW. Fcγreceptors in autoimmune diseases. Eur. J. Clin. Invest. 2001.31: 821-831.
[44] Hogarth PM. Fc receptors are major mediators of antibody based inflammation in autoimmunity. Curr. Opin. Immunol. 2002.14: 798-802.
[45] Klungland H, Gomez-Raya L, Howard CJ, et al. Mapping of bovine FcγR (FcγR) genes by sperm typing allows extended use of human map information. Mamm. Genome. 1997. 8: 573-577.
[46] Sweeney SE, Halloran PJ and Kim YB. Identification of a unique porcine FcγRIIIAαmolecular complex. Cell Immunol. 1996. 172: 92-99.
[47] Qiao S, Zhang G, Xia C, Zhang H, et al. Cloning and characterization of porcine Fc gamma receptor II (FcγRII). Vet Immunol Immunopathol 2006.114: 178-184.
[48] Zhang G, Qiao S, Li Q, Wang X, et al. Molecular cloning and expression of the porcine high-affinity immunoglobulin G Fc receptor (FcγRI). Immunogenetics 2006. 58: 845-849
[49] Kwiatkowska K and Sobota A. The clustered Fcγreceptor II is recruited to Lyn-containing membrane domains and undergoes phosphorylation in a cholesterol- dependent manner. Eur. J. Immunol. 2001. 31: 989-998.
[50] Pricop L, Redecha P, Teillaud JL,et al. Differential modulation of stimulatory and inhibitory Fcγreceptors on human monocytes by TH1 and TH2 cytokines. J. Immunol. 2001. 166: 531-537.
[51] Muta T, Kurosaki T, Misulovin Z, et al. A 13-amino-acid motif in the cytoplasmic domain of FcγRIIB modulates B-cell-receptor signalling. Nature 1994. 368: 70-73.
[52] Tzeng SJ, Bolland S, Inabe K, et al. 2005. The B cell inhibitory Fc receptor triggers apoptosis by a novel c-Abl-family kinase dependent pathway. J. Biol. Chem. 280: 35247–35254.
[53] Ravetch JV, and Lanier L. Immune inhibitory receptors. Science. 2000. 290: 84–89.
[54] McGaha TL, Sorrentino B, and Ravetch JV. Restoration of tolerance in lupus by targeted inhibitory receptor expression. Science. 2005. 307: 590–593.
[55] Blank MC, Stefanescu RN, Masuda E, et al. Decreased transcription of the human FCGR2B gene mediated by the -343 G/C promoter polymorphism and association with systemic lupus erythematosus. Hum. Genet. 2005.117: 220–227.
[56] Fukuyama H, Nimmerjahn F, and Ravetch JV. The inhibitory Fcgamma receptor modulates autoimmunity by limiting the accumulation of immunoglobulin G+ anti-DNA plasma cells. Nat.Immunol. 2005. 6: 99–106.
[57] Okayama Y, Kirshenbaum AS, and Metcalfe, DD. Expression of a functional high-affinity IgG receptor, Fc gamma RI, on human mast cells: up-regulation by IFN-gamma. J. Immunol. 2000. 164: 4332–4339.
[58] Radeke HH, Janssen-Graalfs I, Sowa EN, et al. Opposite regulation of type II and III receptors for immunoglobulin G in mouse glomerular mesangial cells and in the induction of anti-glomerular basement membrane (GBM) nephritis. J. Biol. Chem. 2002. 277: 27535–27544.
[59] Tridandapani S, Wardrop R, Baran CP, et al. TGF-beta 1 suppresses [correction of supresses] myeloid Fc gamma receptor function by regulating the expression and function of the common gamma subunit. J. Immunol. 2003. 170: 4572–4577.
[60] Guyre PM, Morganelli PM, and Miller R. Recombinant immune interferon increases immunoglobulin G Fc receptors on cultured human mononuclear phagocytes. J. Clin. Invest. 1983. 72: 393–397.
[61] Shushakova N, Skokowa J, Schulman J, et al. C5a anaphylatoxin is a major regulator of activating versus inhibitory FcgammaRs in immune complex-induced lung disease. J. Clin. Invest. 2002. 110: 1823–1830.
[62] Garcia-Garcia E and Rosales C. Signal transduction during Fc receptor-mediated phagocytosis. J. Leukoc. Biol. 2002. 72: 1092-1108.
[63] Nakamura A, Akiyama K and Takai T. Fc receptor targeting in the treatment of allergy, autoimmune diseases and cancer. Expert. Opin. Ther. Targets. 2005. 9: 169-190.
[64] van Lent P, Nabbe KC, Boross P, et al. The inhibitory receptor FcγRII reduces joint inflammation and destruction in experimental immune complex-mediated arthritides not only by inhibition of FcγRI/III but also by efficient clearance and endocytosis of immune complexes. Am. J. Pathol. 2003. 163: 1839-1848.
[65] Clynes R, Takechi Y, Moroi Y, et al. Fc receptors are required in passive and active immunity to melanoma. Proc. Natl. Acad. Sci. 1998. 95: 652-656.
[66] Clynes RA, Towers TL, Presta LG and Ravetch JV. Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets. Nat. Med. 2000. 6: 443-446.
[67] Takeda K, Yamaguchi N, Akiba H, et al. Induction of tumor-specific T cell immunity by anti-DR5 antibody therapy. J. Exp. Med. 2004. 199: 437-448.
[68] Rodriguez A, Regnault A, Kleijmeer M, et al. Selective transport of internalized antigens to the cytosol for MHC class I presentation in dendritic cells. Nat. Cell Biol. 1999. 1: 362-368.
[69] Akiyama K, Ebihara S, Yada A, et al. Targeting apoptotic tumor cells to Fc gamma R provides efficient and versatile vaccination against tumors by dendritic cells. J. Immunol. 2003. 170: 1641-1648.
[70] Kalergis AM and Ravetch JV. Inducing tumor immunity through the selective engagement of activating Fcγreceptors on dendritic cells. J. Exp. Med. 2002. 195: 1653-1659.
[71] Boruchov AM, Heller G, Veri MC, et al. Activating and inhibitory IgG Fc receptors on human DCs mediate opposing functions. J. Clin. Invest. 2005. 115: 2914–2923.
[72] Dhodapkar KM, Kaufman JL, Ehlers M, et al. Selective blockade of inhibitory Fcgamma receptor enables human dendritic cell maturation with IL-12p70 production and immunity to antibody-coated tumor cells. Proc. Natl. Acad. Sci. 2005. 102: 2910–2915.
[73] Collins JE, Benfield DA, Christianson WT, et al. Isolation of swine infertility and respiratory syndrome virus (isolate ATCC VR-2332) in North America and experimental reproduction of the disease in gnotobiotic pigs. J. Vet. Diagn. Invest. 1992. 4: 117-126.
[74] Wensvoort G, Tepstra C, Pol JMA, et al. Mystery swine disease in the Netherlands: the isolation of Lelystad virus. Vet. Q. 1991. 13: 121-130.
[75]郭宝清,陈章水,刘文兴,等.从疑似PRRS流产胎儿分离PRRSV的研究.中国畜禽传染病. 1996. 18: 1-4.
[76] Chen J, Liu T, Zhu CG, et al. Genetic variation of Chinese PRRSV strains based on ORF5 sequence. Biochem Genet. 2006. 44: 421-431.
[77] Cancel-Tirado SM, Yoon KJ. Antibody dependent enhancement of virus infection and disease. Viral. Immunol. 2003. 16: 69-86.
[78] Cancel-Tirado SM, Evans RB, Yoon KJ. Monoclonal antibody analysis of porcine reproductive and respiratory syndrome virus epitopes associated with antibody-dependent enhancement and neutralization of virus infection. Vet. Immunol. Immunopathol. 2004. 102: 249-262.
[79] Nelson EA, Christopher-Hennings J, Benfield DA. Serum immune responses to the proteins of porcine and respiratory syndrome (PRRS) virus. J. Vet. Diagn. Invest. 1994. 6: 410 -415.
[80] Oleksiewicz MB, Botner A, Toft P, et al. Epitope mapping porcine reproductive and respiratory syndrome virus by phage display: the nsp2 fragment of the replicase polyprotein contains a cluster of B-cell epitomes. J. Virol. 2001. 75: 3277-3290.
[81] de Lima M, Pattnaik AK, Flores EF, etal. Serologic marker candidates identified among B-cell linear epitopes of Nsp2 andstructural proteins of a North American strain of porcine reproductive and respiratory syndrome virus. Virology. 2006. 353: 410–421.
[82] Takikawa N, Kobayashi S, Ide S, et al. Detection of antibodies against porcine reproductive and respiratory syndrome (PRRS) virus in swine sera by enzyme-linked immunosorbentassay. J. Vet. Med. Sci. 1996. 58: 355–357.
[83] Diaz I, Darwich L, Pappaterra G, et al. Immune responses of pigs after experimental infection with a European strain of porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 2005. 86: 1943–1951.
[84] Diaz I, Darwich L, Pappaterra G, et al. Different European-type vaccines against porcine reproductive and respiratory syndrome virus have different immunological properties and confer different protection to pigs.Virology. 2006. 351: 249–259.
[85] Meier WA, Galeota J, Osorio FA, et al. Gradual development of the interferon-(response of swine to porcine reproductive and respiratory syndrome virus infection or vaccination. Virology. 2003. 309: 18-31.
[86] Pirzadeh B, Dea S. Immune response in pigs vaccinated with plasmid DNA encoding ORF5 of porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 1998. 79: 989–999.
[87] Yoon KJ, Wu LL, Zimmerman JJ. Antibody-dependent enhancement (ADE) of porcine reproductive and respiratory syndrome virus (PRRSV) infection in pigs. Viral Immunology. 1996. 9: 51–63.
[88] Vezina SA, Loemba H, Fournier M, et al. Antibody production and blastogenic response in pigs experimentally infected with porcine reproductive and respiratory syndrome virus. Can. J. Vet. Res. 1996. 60: 94–99.
[89] Delputte PL, Meerts P, Costers S, et al. Effect of virus-specific antibodies on attachment, internalization and infection of porcine reproductive and respiratory syndrome virus in primary macrophages. Vet. Immunol. Immunopathol. 2004. 102: 179–188.
[90] Osorio FA, Galeota JA, Nelson E, et al. Passive transfer of virusspecific antibodies confers protection against reproductive failure induced by a virulent strain of porcine reproductive and respiratory syndrome virus and establishes sterilizing immunity. Virology. 2002. 302: 9–20.
[91] Lopez OJ, Oliveira MF, Garcia EA et al. Protection against porcine reproductive and respiratory syndrome virus (PRRSV) infection through passive transfer of PRRSV-neutralizing antibodies is dose dependent. Clin. Vaccine. Immunol. 2007. 14: 269–275.
[92] Lopez F, Domenech N, Alvarez B, et al. Analysis of cellular immune response in pigs recovered from porcine respiratory and reproductive syndrome infection.Virus Res. 1999. 64: 33–42.
[93] Albina E, Carrat C, Charley B. Interferon-αresponse to swine arterivirus (PoAV), the porcine reproductive and respiratory syndrome virus. J. Interferon Cytokine Res. 1998. 18: 485–490.
[94] Buddaert W, Van Reeth K, Pensaert M. In vivo and in vitro interferon (IFN) studies with the porcine reproductive and respiratory syndrome virus (PRRSV).Advances in Experimental Medicine and Biology. 1998. 440: 461–467.
[95] Royaee AR, Husmann RJ, Dawson HD, et al. Deciphering the involvement of innate immunefactors in the development of the host response to PRRSV vaccination. Vet. Immunol. Immunopathol. 2004. 102: 199–216.
[96] Lee SM, Kleiboeker SB. Porcine arterivirus activates the NF-κB pathway through IκB degradation. Virology. 2005. 342: 47–59.
[97] Lee SM, Schommer SK, Kleiboeker SB. Porcine reproductive and respiratory syndrome virus field isolates differ in in vitro interferon phenotypes.Vet. Immunol. Immunopathol. 2004.102: 217–231.
[98] Suradhat S, Thanawongnuwech R, Poovorawan Y. Upregulation of IL-10 gene expression in porcine peripheral blood mononuclear cells by porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 2003. 84: 453–459.
[99] Charerntantanakul W, Platt R, Roth JA. Effects of porcine reproductive and respiratory syndrome virus-infected antigen-presenting cells on T cell activation and antiviral cytokine production.Viral Immunol. 2006. 19: 646–661.
[100] Loving CL, Brockmeier SL, Sacco RE. Differential type I interferon activation and susceptibility of dendritic cell populations to porcine arterivirus. Immunology. 2007. 120: 217–229.
[101] Wang X, Eaton M, Mayer M, et al. Porcine reproductive and respiratory syndrome virus productively infects monocyte-derived dendritic cells and compromises their antigen-presenting ability. Arch. Virol. 2007. 152: 289–303.
[102] Plagemann PG, Rowland RR, Faaberg KS. The primary neutralization epitope of porcine respiratory and reproductive syndrome virus strain VR-2332 is located in the middle of the GP5 ectodomain. Arch. Virol. 2002. 147: 2327–2347.
[103] Plagemann PG. The primary GP5 neutralization epitope of North American isolates of porcine reproductive and respiratory syndrome virus. Vet. Immunol. Immunopathol. 2004. 102: 263–275.
[104] Wissink EH, van Wijk HA, Kroese MV, et al. The major envelope protein, GP5, of a European porcine reproductive and respiratory syndrome virus contains a neutralization epitope in its N-terminal ectodomain. J. Gen. Virol. 2003. 84: 1535–1543.
[105] Ostrowski M, Galeota JA, Jar AM, et al. Identification of neutralizing and nonneutralizing epitopes in the porcine reproductive and respiratory syndrome virus GP5 ectodomain. J. Virol. 2002. 76: 4241–4250.
[106] Fang L, Jiang Y, Xiao S, et al. Enhanced immunogenicity of the modified GP5 of porcine reproductive and respiratory syndrome virus.Virus. Genes. 2006. 32: 5–11.
[107] Faaberg KS, Hocker JD, Erdman MM, et al. Neutralizing antibody responses of pigs infected with natural GP5 N-glycan mutants of porcine reproductive and respiratory syndrome virus. Viral. Immunol. 2006. 19: 294–304.
[108] Mateu E, Diaz I, Darwich L, et al. Evolution of ORF5 of Spanish porcine reproductive and respiratory syndrome virus strains from 1991 to 2005. Virus. Res. 2006. 115: 198–206.
[109]刘光清,薛强,仇华吉,等.猪繁殖与呼吸综合征病毒CH-la猪非结构基因的分子克隆及其基因特征的研究.中国预防兽医学报. 2002. 24: 81-87.
[110] Kapur V, Elam MK, Pawlovich TM et al. Genetic variation in Porcine reproductive and respiratory Syndrome vlrus isolates in the midwesten UnitedStates. J. Gen. Virol. 1996. 77: 1271-1276
[111] Mardassi H,Mounir S,Dea S. Molecuar analysis of the 0RFs 3 to 7 of porcine reproductive and respiratory Syndrom virus Quebec reference Stain. Arch Virol. 1995. 140: 1405-1418
[112]高志强,郭鑫,杨汉春,等.猪繁殖与呼吸综合征病毒缺失变异株的基因组特征.畜牧兽医学报. 2005. 36: 578-584.
[113]童光志,周艳君,郝晓芳,等.高致病性猪繁殖与呼吸综合征病毒的分离鉴定及其分子流行病学分析.中国预防兽医学报. 2007. 5: 323-326.
[114] Tian K, Yu X, Zhao T. Emergence of Fatal PRRSV Variants: Unparalleled Outbreaks of Atypical PRRS in China and Molecular Dissection of the Unique Hallmark. PLoS. ONE. 2007. 2: 1-10.
[115] Zhou YJ, Hao XF, Tian ZJ, et al. Highly virulent porcine reproductive and respiratory syndrome virus emerged in China. Transboundary and Emerging Disease. 2008. 55: 152-164.
[116] Li Y, Wang X, Bo K, et al. Emergence of a highly pathogenic porcine reproductive and respiratory syndrome virus in the Mid-Eastern region of China. Vet. J. 2007. 174: 577-584.
[117] Johnson C, Wanqin Y, Murtaugh M. Cross-reactive antibody responses to nsp1 and Nsp2 of procine reproductive and respiratory syndrome virus. J. Gen. Virol. 2007. 88: 1184-1195.
[118] Stadejek T, Oleksiewicz MB, Potapchuk D, et al. Porcine reproductive and respiratory syndrome virus strains of exceptional diversity in Eastern Europe support the definition of new genetic subtypes. J. Gen. Virol. 2006. 87: 1835–1841.
[119] Goldberg TL, Lowe JF, Milburn SM, Firkins LD. Quasispecies variation of porcine reproductive and respiratory syndrome virus during natural infection.Virology. 2003. 317: 197–207.
[120] Lager KM, Mengeling WL, Brockmeier SL. Evaluation of protective immunity in gilts inoculated with the NADC-8 isolate of porcine reproductive and respiratory syndrome virus (PRRSV) and challenge-exposed with an antigenically distinct PRRSV isolate. Am. J. Vet. Res. 1999. 60: 1022–1027.
[121] Mengeling WL, Lager KM, Vorwald AC, et al. Strain specificity of the immune response of pigs following vaccination with various strains of porcine reproductive and respiratory syndrome virus.Vet. Microbiol. 2003. 93: 13–24.
[122] Labarque G, Reeth KV, Nauwynck H, et al. Impact of genetic diversity of European-type porcine reproductive and respiratory syndrome virus strains on vaccine efficacy.Vaccine. 2004. 22: 4183–4190.
[123] Bautista EM, Suarez P, Molitor TW. T cell responses to the structural polypeptides ofporcine reproductive and respiratory syndrome virus. Arch. Virol. 1999. 144: 117–134.
[124] Hawkes RA. Enhancement of the infectivity of arboviruses by specific antisera produced in domestic fowls. Aust J Exp Biol Med Sci. 1964. 42: 465-482.
[125] Mahalingam S, Meanger J, Foster PS, et al. The viral manipulation of the host cellular and immune environments to enhance propagation and survival: a focus on RNA viruses. J. Leukoc. Biol. 2002. 72: 429-439.
[126] Choi CS, Christianson WT, Gustafson KV, et al. Antibody-dependent enhancement of PRRS virus replication. Am. Assoc. Swine. Pract. Newsl. 1992. 4: 19-21.
[127] Mahalingam S, Lidbury BA. Suppression of lipopolysaccharide-induced antiviral transcription factor (STAT-1 and NF-kappa B) complexes by antibody-dependent enhancement of macrophage infection by Ross River virus. Proc. Natl. Acad. Sci. 2002. 99: 13819-13824.
[128] Oliphant T, Nybakken GE, Engle M, et al. Antibody Recognition and Neutralization Determinants on Domains I and II of West Nile Virus Envelope Protein. J. Virol. 2006. 15: 12149-12159.
[129] Hohdatsu T, Tokunaga J and Koyama. The role of IgG subclass of mouse monoclonal antibodies in antibody-dependent enhancement of feline infectious peritonitis virus infection of feline macrophages. Arch. Virol. 1994. 139: 273-285.
[130] Huang KJ, Yang YC, Lin YS, et al. The dual-specific binding of dengue virus and target cells for the antibody-dependent enhancement of dengue virus infection. J. Immunol. 2006. 176: 2825-2832.
[131] Lidbury BA and Mahalingam S. Specific ablation of antiviral gene expression in macrophage by antibody-dependent enhancement of Ross River virus infection. J. Virol. 2000. 74: 8376-8381.
[132] Takada A, Kawaoka Y. Antibody-dependent enhancement of viral infection: molecular mechanisms and in vivo implications. Rev. Med. Virol. 2003. 13: 387-398.
[133] Christianso WT, Choi CS, Collins JE, et al. Pathogenesis of porcine reproductive and respiratory syndrome virus infection in mid-gestation sows and fetuses. Can. J. Vet. Res. 1993. 57: 262-268.
[134] Yoon KJ, Wu LL, Zimmerman, et al. Antibody-dependent ehancement (ADE) of porcine reproductive and respiratory syndrome virus (PRRSV) infection in pigs. Viral. Immunol. 1996. 9: 51-63.
[135] Yoon KJ, Wu LL, Zimmerman JJ, et al. Field isolates of porcine reproductive and respiratory syndrome virus (PRRSV) vary in their susceptibility to antibody dependent enhancement (ADE) of infection. Vet. Mircobiol. 1997. 55: 277-287.
[136] Nimmerjahn F, Ravetch JV. Fcγreceptors as regulators of immune responses. Nat. Rev. Immunol. 2008. 8: 34-47.
[137] Nimmerjahn F, Ravetch JV. Anti-inflammatory actions of intravenous immunoglobulin.Annu. Rev. Immunol. 2008. 26: 513-33.
[138] Brady LJ. Antibody-mediated immunomodulation: a strategy to improve host response against microbial antigens. Infect Immun. 2005. 73: 671-678
[139] Rosa, G. T., L. Gillet, et al. IgG fc receptors provide an alternative infection route for murine gamma-herpesvirus-68."PLoS ONE 2007. 2: e560.
[140] Halloran PJ, Sweeney SE, Kim YB.. Biochemical characterization of the porcine Fc gamma RⅢalpha homologue G7. Cell Immunol. 1994. 153: 2631-2641
[141] Sweeney SE, Kim YB. Identification of a novel Fc gamma RⅢa alpha-associated molecule that contains significant homology to porcine cathelin. J. Immunol. 2004. 172: 1203-1212
[142]周顺伍.动物生物物实验指导.中国农业出版社,北京. 2001.
[143] Aasted B, Bach P, Nielsen J, et al. Cytokine profiles in peripheral blood mononuclear cells and lymph node cells from piglets infected in utero with porcine reproductive and respiratory syndrome virus. Clin Diagn Lab Immunol. 2002. 9: 1229-1234.
[144] Argaw T, Colon-Moran W, Wilson CA. Limited infection without evidence of replication by porcine endogenous retrovirus in guinea pigs. J Gen Virol. 2004. 85: 15-19.
[145] Delputte PL, Costers S and Nauwynck HJ. Analysis of porcine reproductive and respiratory syndrome virus attachment and internalization: distinctive roles for heparan sulphate and sialoadhesin. J Gen Virol. 2005. 86: 1441-1445.
[146] Guyre PM, Morganelli PM, Miller R. Recombinant immune interferon increases immunoglobulin G Fc receptors on cultured human mononuclear phagocytes. J. Clin. Invest. 1983. 72: 393-397.
[147] Lemke CD, Haynes JS, Spaete R, et al. Lymphoid hyperplasia resulting in immune dysregulation is caused by porcine reproductive and respiratory syndrome virus infection in neonatal pigs. J Immunol. 2004. 172: 1916-1925.
[148] Olsen CW, Corapi WV, Ngichabe CK, et al. Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages. J Virol. 1992. 66: 956-965.
[149] Rovira A, Balasch M, Segales J, et al. Experimental inoculation of conventional pigs with porcine reproductive and respiratory syndrome virus and porcine circovirus 2. J Virol. 2002. 76: 3232-3239.
[150] Pricop L, Redecha P, Teillaud JL, et al. Differential modulation of stimulatory and inhibitory Fcγreceptors on human monocytes by TH1 and TH2 cytokines. J. Immunol. 2001.166: 531-537.
[151] Radeke HH, Janssen-Graalfs I, Sowa EN, et al. Opposite regulation of type II and III receptors for immunoglobulin G in mouse glomerular mesangial cells and in the induction of anti-glomerular basement membrane (GBM) nephritis. J. Biol. Chem. 2002. 277: 27535-27544.
[152] Shushakova N, Skokowa J, Schulman J, et al. C5a anaphylatoxin is a major regulator of activating versus inhibitory FcgammaRs in immune complex-induced lung disease. J. Clin. Invest. 2002. 110: 1823-1830.
[153] Suradhat S, Thanawongnuwech R and Poovorawan Y. Upregulation of IL-10 gene expression in porcine peripheral blood mononuclear cells by porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 2003. 84: 453-459.
[154] Mateu E, Diaz I. The challenge of PRRS immunology. Vet. J. 2008. 177: 345-51
[155] Hu H, Li X, Zhang Z, Shuai J,et al. Porcine reproductive and respiratory syndrome viruses predominant in southeastern China from 2004 to 2007 were from a common source and underwent further divergence. Arch. Virol. 2009. 154:391-8
[156] Zhou L, Zhang J, Zeng J, Yin S, Li Y, et al. The 30-amino-acid deletion in the Nsp2 of highly pathogenic porcine reproductive and respiratory syndrome virus emerging in China is not related to its virulence. J. Virol. 2009. 83: 5156-67.
[157]田小辉,王爱萍,乔松林,张改平,等.猪繁殖与呼吸障碍综合征病毒ORF5基因的克隆与表达.河南农业科学. 2009. 2: 103-106
[2] Daeron M. Fc receptor biology. Annu. Rev. Immunol. 1997.15: 203-234.
[3] Ravetch JV. Fc receptors. Curr. Opin. Immunol. 1997. 9: 121-125.
[4] Ravetch JV and Bolland S. IgG Fc receptors. Annu. Rev. Immunol. 2001. 19: 275-290.
[5] Cohen-Solal JF, Cassard L, Fridman WH and Sautes-Fridman C. Fcγreceptors. Immunol. Lett. 2004. 92: 199-205.
[6] Berken A. and Benacerraf B. Properties of antibodies cytophilic for macrophages. J. Exp. Med. 1966. 123: 119-144.
[7] Paraskevas F, Lee ST, Orr KB and Israels LG. A receptor for Fc on mouse B-lymphocytes. J. Immunol. 1972. 108: 1319-1327.
[8] Metzger H, Alcaraz G, Hohman R, et al. The receptor with high affinity for immunoglobulin E. Annu. Rev. Immunol. 1986. 4: 419-470.
[9] Woof JM and Burton DR. Human antibody-Fc receptor interactions illuminated by crystal structures. Nat. Rev. Immunol. 2004. 4: 89-99.
[10] Takai T. Fc receptors and their role in immune regulation and autoimmunity. J. Clin. Immunol. 2005. 25: 1-18.
[11] Kacskovics I. Fc receptors in livestock species. Vet. Immunol. Immunopathol. 2004. 102: 351-362.
[12] Raghavan M and Bjorkman PJ. Fc receptors and their interactions with immunoglobulins. Annu. Rev. Cell Dev. Biol. 1996. 12: 181-220.
[13] Bolland S. A newly discovered Fc receptor that explains IgG-isotype disparities in effector responses. Immunity. 2005. 23: 2-4.
[14] Allen JM, Seed B. Isolation and expression of functional high-affinity Fc receptor complementary DNAs. Science. 1989. 243:378-381
[15] Nimmerjahn F, Bruhns P, Horiuchi K and Ravetch JV. FcγRIV: A novel FcR with distinct IgG subclass specificity. Immunity. 2005. 23: 41-51.
[16] Nimmerjahn F, Ravetch JV. Divergent immunoglobulin G subclass activity through selective Fc receptor binding. Science. 2005. 31: 1510-1512 .
[17] Jefferis R and Lund J. Interaction sites on human IgG-Fc for FcR: current models. Immnunol. Lett. 2002. 82 : 57-65.
[18] Pasquier B, Launay P, Kanamaru Y, et al. Identification of FcαRI as an inhibitory receptor that controls inflammation: dual role of FcRγITAM. Immunity 2005. 22: 31-42.
[19] Ravetch JV and Kinet JP. Fc receptors. Annu. Rev. Immunol. 1991. 9: 475-492.
[20] Hulett MD and Hogarth PM. Molecular basis of Fc receptor function. Adv. Immunol. 1994. 57: 1-127.
[21] Mechetina LV, Najakshin AM, Alabyev BY, et al. Identification of CD16-2, a novel mouse receptor homologous to CD16/Fc gamma RIII. Immunogenetics. 2002.54: 463-468
[22] Davis RS, Dennis GJ, Odom MR, et al. Fc receptor homologs: newest members of a remarkable diverse Fc receptor gene family. Immunol. Rev. 2002.190: 123-136
[23] Symons DB and Clarkson CA. Genomic organisation and sequence of the extracellular domain exons of the bovine FcγRI receptor, and evidence for restricted binding of ruminant IgG to U937 cells. Mol. Immunol. 1992. 29: 1407-1413.
[24] Yan Y, Li X, Wang A and Zhang G. Molecular cloning and identification of full-length cDNA encoding high affinity Fc receptor for bovine IgG (FcγRI). Vet. Immunol. Immunopathol. 2000. 75: 151-159.
[25] Zhang G, Young JR, Tregaskes CR, Howard CJ. Cattle Fc gamma RII: molecular cloning and ligand specificity. Immunogenetics. 1994. 39: 423–427.
[26] Collins RA, Gelder KI and Howard CJ. Nucleotide sequence of cattle FcGRIII: its identification in gammadelta T cells. Immunogenetics. 1997. 45: 440-443.
[27] Yan Y, Zhang G, Chen C, et al. Bovine FcγRIII with a single extracellular domain. Res. Vet. Sci. 2000. 68: 115-118.
[28] Watson JL, Jackson KA, King DP and Stott JL. Molecular cloning and sequencing of the low-affinity IgE receptor (CD23) for horse and cattle. Vet. Immunol. Immunopathol. 2000. 73: 323-329.
[29] Morton HC, Pleass RJ, Storset AK, et al. Cloning and characterization of an immunoglobulin A Fc receptor from cattle. Immunology. 2004. 111: 204-211.
[30] Zhang G, Young JR, Tregaskes CA, et al. Identification of a novel class of mammalian Fcγreceptor. J. Immunol. 1995. 155: 1534-1541.
[31] Morton HC, Storset AK and Brandtzaeg P. Cloning and sequencing of a cDNA encoding the bovine FcRγchain. Vet. Immunol. Immunopathol. 2001. 82: 101-106.
[32] Verbeet MP, Vermeer H, Warmerdam GC, et al. Cloning and characterization of the bovine polymeric immunoglobulin receptor-encoding cDNA. Gene. 1995. 164: 329–333
[33] Kulseth MA, Krajci P, Myklebost O, Rogne S. Cloning and characterization of two forms of bovine polymeric immunoglobulin receptor cDNA. DNA Cell Biol. 1995.14: 251–256.
[34] Kacskovics I, Wu Z, Simister NE, et al. Cloning and characterization of the bovine MHC class I-like Fc receptor. J. Immunol. 2000. 164: 1889-1897.
[35] McAleese SM, Halliwell RE and Miller HR. Cloning and sequencing of the horse and sheep high-affinity IgE receptorαchain cDNA. Immunogenetics. 2000. 51: 878-881.
[36] McAleese SM and Miller HR. Cloning and sequencing of the equine and ovine high-affinity IgE receptorβ- andγ-chain cDNA. Immunogenetics. 2003. 55: 122-125.
[37] Mayer B, Zolnai A, Frenyo LV, et al. Redistribution of the sheep neonatal Fc receptor in the mammary gland around the time of parturition in ewes and its localization in the small intestine of neonatal lambs. Immunology. 2002. 107: 288–296.
[38] Halloran PJ, Sweeney SE, Strohmeier CM and Kim YB. Molecular cloning and identification of the porcine cytolytic trigger molecule G7 as a FcγRIIIα(CD16) homologue. J. Immunol. 1994. 153: 2631-2641.
[39] Yim D, Jie HB, Lanier LL and Kim YB. Molecular cloning, gene structure, and expression pattern of pig immunoreceptor DAP12. Immunogenetics.2000. 51: 436-442.
[40] Kumura BH, Sone T, Shimazaki K, Kobayashi E. Sequence analysis of porcine polymeric immunoglobulin receptor from mammary epithelial cells present in colostrum. J. Dairy Res. 2000. 67: 631–636.
[41] Morton HC, Pleass RJ, Storset AK, et al. Cloning and characterization of equine CD89 and identification of the CD89 gene in chimpanzees and rhesus macaques. Immunology 2005. 115: 74-84.
[42] Flesch BK and Neppert J. Functions of the Fc receptors for immunoglobulin G. J. Clin. Lab. Anal. 2000.14: 141-156.
[43] Fossati G, Bucknall RC and Edwards SW. Fcγreceptors in autoimmune diseases. Eur. J. Clin. Invest. 2001.31: 821-831.
[44] Hogarth PM. Fc receptors are major mediators of antibody based inflammation in autoimmunity. Curr. Opin. Immunol. 2002.14: 798-802.
[45] Klungland H, Gomez-Raya L, Howard CJ, et al. Mapping of bovine FcγR (FcγR) genes by sperm typing allows extended use of human map information. Mamm. Genome. 1997. 8: 573-577.
[46] Sweeney SE, Halloran PJ and Kim YB. Identification of a unique porcine FcγRIIIAαmolecular complex. Cell Immunol. 1996. 172: 92-99.
[47] Qiao S, Zhang G, Xia C, Zhang H, et al. Cloning and characterization of porcine Fc gamma receptor II (FcγRII). Vet Immunol Immunopathol 2006.114: 178-184.
[48] Zhang G, Qiao S, Li Q, Wang X, et al. Molecular cloning and expression of the porcine high-affinity immunoglobulin G Fc receptor (FcγRI). Immunogenetics 2006. 58: 845-849
[49] Kwiatkowska K and Sobota A. The clustered Fcγreceptor II is recruited to Lyn-containing membrane domains and undergoes phosphorylation in a cholesterol- dependent manner. Eur. J. Immunol. 2001. 31: 989-998.
[50] Pricop L, Redecha P, Teillaud JL,et al. Differential modulation of stimulatory and inhibitory Fcγreceptors on human monocytes by TH1 and TH2 cytokines. J. Immunol. 2001. 166: 531-537.
[51] Muta T, Kurosaki T, Misulovin Z, et al. A 13-amino-acid motif in the cytoplasmic domain of FcγRIIB modulates B-cell-receptor signalling. Nature 1994. 368: 70-73.
[52] Tzeng SJ, Bolland S, Inabe K, et al. 2005. The B cell inhibitory Fc receptor triggers apoptosis by a novel c-Abl-family kinase dependent pathway. J. Biol. Chem. 280: 35247–35254.
[53] Ravetch JV, and Lanier L. Immune inhibitory receptors. Science. 2000. 290: 84–89.
[54] McGaha TL, Sorrentino B, and Ravetch JV. Restoration of tolerance in lupus by targeted inhibitory receptor expression. Science. 2005. 307: 590–593.
[55] Blank MC, Stefanescu RN, Masuda E, et al. Decreased transcription of the human FCGR2B gene mediated by the -343 G/C promoter polymorphism and association with systemic lupus erythematosus. Hum. Genet. 2005.117: 220–227.
[56] Fukuyama H, Nimmerjahn F, and Ravetch JV. The inhibitory Fcgamma receptor modulates autoimmunity by limiting the accumulation of immunoglobulin G+ anti-DNA plasma cells. Nat.Immunol. 2005. 6: 99–106.
[57] Okayama Y, Kirshenbaum AS, and Metcalfe, DD. Expression of a functional high-affinity IgG receptor, Fc gamma RI, on human mast cells: up-regulation by IFN-gamma. J. Immunol. 2000. 164: 4332–4339.
[58] Radeke HH, Janssen-Graalfs I, Sowa EN, et al. Opposite regulation of type II and III receptors for immunoglobulin G in mouse glomerular mesangial cells and in the induction of anti-glomerular basement membrane (GBM) nephritis. J. Biol. Chem. 2002. 277: 27535–27544.
[59] Tridandapani S, Wardrop R, Baran CP, et al. TGF-beta 1 suppresses [correction of supresses] myeloid Fc gamma receptor function by regulating the expression and function of the common gamma subunit. J. Immunol. 2003. 170: 4572–4577.
[60] Guyre PM, Morganelli PM, and Miller R. Recombinant immune interferon increases immunoglobulin G Fc receptors on cultured human mononuclear phagocytes. J. Clin. Invest. 1983. 72: 393–397.
[61] Shushakova N, Skokowa J, Schulman J, et al. C5a anaphylatoxin is a major regulator of activating versus inhibitory FcgammaRs in immune complex-induced lung disease. J. Clin. Invest. 2002. 110: 1823–1830.
[62] Garcia-Garcia E and Rosales C. Signal transduction during Fc receptor-mediated phagocytosis. J. Leukoc. Biol. 2002. 72: 1092-1108.
[63] Nakamura A, Akiyama K and Takai T. Fc receptor targeting in the treatment of allergy, autoimmune diseases and cancer. Expert. Opin. Ther. Targets. 2005. 9: 169-190.
[64] van Lent P, Nabbe KC, Boross P, et al. The inhibitory receptor FcγRII reduces joint inflammation and destruction in experimental immune complex-mediated arthritides not only by inhibition of FcγRI/III but also by efficient clearance and endocytosis of immune complexes. Am. J. Pathol. 2003. 163: 1839-1848.
[65] Clynes R, Takechi Y, Moroi Y, et al. Fc receptors are required in passive and active immunity to melanoma. Proc. Natl. Acad. Sci. 1998. 95: 652-656.
[66] Clynes RA, Towers TL, Presta LG and Ravetch JV. Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets. Nat. Med. 2000. 6: 443-446.
[67] Takeda K, Yamaguchi N, Akiba H, et al. Induction of tumor-specific T cell immunity by anti-DR5 antibody therapy. J. Exp. Med. 2004. 199: 437-448.
[68] Rodriguez A, Regnault A, Kleijmeer M, et al. Selective transport of internalized antigens to the cytosol for MHC class I presentation in dendritic cells. Nat. Cell Biol. 1999. 1: 362-368.
[69] Akiyama K, Ebihara S, Yada A, et al. Targeting apoptotic tumor cells to Fc gamma R provides efficient and versatile vaccination against tumors by dendritic cells. J. Immunol. 2003. 170: 1641-1648.
[70] Kalergis AM and Ravetch JV. Inducing tumor immunity through the selective engagement of activating Fcγreceptors on dendritic cells. J. Exp. Med. 2002. 195: 1653-1659.
[71] Boruchov AM, Heller G, Veri MC, et al. Activating and inhibitory IgG Fc receptors on human DCs mediate opposing functions. J. Clin. Invest. 2005. 115: 2914–2923.
[72] Dhodapkar KM, Kaufman JL, Ehlers M, et al. Selective blockade of inhibitory Fcgamma receptor enables human dendritic cell maturation with IL-12p70 production and immunity to antibody-coated tumor cells. Proc. Natl. Acad. Sci. 2005. 102: 2910–2915.
[73] Collins JE, Benfield DA, Christianson WT, et al. Isolation of swine infertility and respiratory syndrome virus (isolate ATCC VR-2332) in North America and experimental reproduction of the disease in gnotobiotic pigs. J. Vet. Diagn. Invest. 1992. 4: 117-126.
[74] Wensvoort G, Tepstra C, Pol JMA, et al. Mystery swine disease in the Netherlands: the isolation of Lelystad virus. Vet. Q. 1991. 13: 121-130.
[75]郭宝清,陈章水,刘文兴,等.从疑似PRRS流产胎儿分离PRRSV的研究.中国畜禽传染病. 1996. 18: 1-4.
[76] Chen J, Liu T, Zhu CG, et al. Genetic variation of Chinese PRRSV strains based on ORF5 sequence. Biochem Genet. 2006. 44: 421-431.
[77] Cancel-Tirado SM, Yoon KJ. Antibody dependent enhancement of virus infection and disease. Viral. Immunol. 2003. 16: 69-86.
[78] Cancel-Tirado SM, Evans RB, Yoon KJ. Monoclonal antibody analysis of porcine reproductive and respiratory syndrome virus epitopes associated with antibody-dependent enhancement and neutralization of virus infection. Vet. Immunol. Immunopathol. 2004. 102: 249-262.
[79] Nelson EA, Christopher-Hennings J, Benfield DA. Serum immune responses to the proteins of porcine and respiratory syndrome (PRRS) virus. J. Vet. Diagn. Invest. 1994. 6: 410 -415.
[80] Oleksiewicz MB, Botner A, Toft P, et al. Epitope mapping porcine reproductive and respiratory syndrome virus by phage display: the nsp2 fragment of the replicase polyprotein contains a cluster of B-cell epitomes. J. Virol. 2001. 75: 3277-3290.
[81] de Lima M, Pattnaik AK, Flores EF, etal. Serologic marker candidates identified among B-cell linear epitopes of Nsp2 andstructural proteins of a North American strain of porcine reproductive and respiratory syndrome virus. Virology. 2006. 353: 410–421.
[82] Takikawa N, Kobayashi S, Ide S, et al. Detection of antibodies against porcine reproductive and respiratory syndrome (PRRS) virus in swine sera by enzyme-linked immunosorbentassay. J. Vet. Med. Sci. 1996. 58: 355–357.
[83] Diaz I, Darwich L, Pappaterra G, et al. Immune responses of pigs after experimental infection with a European strain of porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 2005. 86: 1943–1951.
[84] Diaz I, Darwich L, Pappaterra G, et al. Different European-type vaccines against porcine reproductive and respiratory syndrome virus have different immunological properties and confer different protection to pigs.Virology. 2006. 351: 249–259.
[85] Meier WA, Galeota J, Osorio FA, et al. Gradual development of the interferon-(response of swine to porcine reproductive and respiratory syndrome virus infection or vaccination. Virology. 2003. 309: 18-31.
[86] Pirzadeh B, Dea S. Immune response in pigs vaccinated with plasmid DNA encoding ORF5 of porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 1998. 79: 989–999.
[87] Yoon KJ, Wu LL, Zimmerman JJ. Antibody-dependent enhancement (ADE) of porcine reproductive and respiratory syndrome virus (PRRSV) infection in pigs. Viral Immunology. 1996. 9: 51–63.
[88] Vezina SA, Loemba H, Fournier M, et al. Antibody production and blastogenic response in pigs experimentally infected with porcine reproductive and respiratory syndrome virus. Can. J. Vet. Res. 1996. 60: 94–99.
[89] Delputte PL, Meerts P, Costers S, et al. Effect of virus-specific antibodies on attachment, internalization and infection of porcine reproductive and respiratory syndrome virus in primary macrophages. Vet. Immunol. Immunopathol. 2004. 102: 179–188.
[90] Osorio FA, Galeota JA, Nelson E, et al. Passive transfer of virusspecific antibodies confers protection against reproductive failure induced by a virulent strain of porcine reproductive and respiratory syndrome virus and establishes sterilizing immunity. Virology. 2002. 302: 9–20.
[91] Lopez OJ, Oliveira MF, Garcia EA et al. Protection against porcine reproductive and respiratory syndrome virus (PRRSV) infection through passive transfer of PRRSV-neutralizing antibodies is dose dependent. Clin. Vaccine. Immunol. 2007. 14: 269–275.
[92] Lopez F, Domenech N, Alvarez B, et al. Analysis of cellular immune response in pigs recovered from porcine respiratory and reproductive syndrome infection.Virus Res. 1999. 64: 33–42.
[93] Albina E, Carrat C, Charley B. Interferon-αresponse to swine arterivirus (PoAV), the porcine reproductive and respiratory syndrome virus. J. Interferon Cytokine Res. 1998. 18: 485–490.
[94] Buddaert W, Van Reeth K, Pensaert M. In vivo and in vitro interferon (IFN) studies with the porcine reproductive and respiratory syndrome virus (PRRSV).Advances in Experimental Medicine and Biology. 1998. 440: 461–467.
[95] Royaee AR, Husmann RJ, Dawson HD, et al. Deciphering the involvement of innate immunefactors in the development of the host response to PRRSV vaccination. Vet. Immunol. Immunopathol. 2004. 102: 199–216.
[96] Lee SM, Kleiboeker SB. Porcine arterivirus activates the NF-κB pathway through IκB degradation. Virology. 2005. 342: 47–59.
[97] Lee SM, Schommer SK, Kleiboeker SB. Porcine reproductive and respiratory syndrome virus field isolates differ in in vitro interferon phenotypes.Vet. Immunol. Immunopathol. 2004.102: 217–231.
[98] Suradhat S, Thanawongnuwech R, Poovorawan Y. Upregulation of IL-10 gene expression in porcine peripheral blood mononuclear cells by porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 2003. 84: 453–459.
[99] Charerntantanakul W, Platt R, Roth JA. Effects of porcine reproductive and respiratory syndrome virus-infected antigen-presenting cells on T cell activation and antiviral cytokine production.Viral Immunol. 2006. 19: 646–661.
[100] Loving CL, Brockmeier SL, Sacco RE. Differential type I interferon activation and susceptibility of dendritic cell populations to porcine arterivirus. Immunology. 2007. 120: 217–229.
[101] Wang X, Eaton M, Mayer M, et al. Porcine reproductive and respiratory syndrome virus productively infects monocyte-derived dendritic cells and compromises their antigen-presenting ability. Arch. Virol. 2007. 152: 289–303.
[102] Plagemann PG, Rowland RR, Faaberg KS. The primary neutralization epitope of porcine respiratory and reproductive syndrome virus strain VR-2332 is located in the middle of the GP5 ectodomain. Arch. Virol. 2002. 147: 2327–2347.
[103] Plagemann PG. The primary GP5 neutralization epitope of North American isolates of porcine reproductive and respiratory syndrome virus. Vet. Immunol. Immunopathol. 2004. 102: 263–275.
[104] Wissink EH, van Wijk HA, Kroese MV, et al. The major envelope protein, GP5, of a European porcine reproductive and respiratory syndrome virus contains a neutralization epitope in its N-terminal ectodomain. J. Gen. Virol. 2003. 84: 1535–1543.
[105] Ostrowski M, Galeota JA, Jar AM, et al. Identification of neutralizing and nonneutralizing epitopes in the porcine reproductive and respiratory syndrome virus GP5 ectodomain. J. Virol. 2002. 76: 4241–4250.
[106] Fang L, Jiang Y, Xiao S, et al. Enhanced immunogenicity of the modified GP5 of porcine reproductive and respiratory syndrome virus.Virus. Genes. 2006. 32: 5–11.
[107] Faaberg KS, Hocker JD, Erdman MM, et al. Neutralizing antibody responses of pigs infected with natural GP5 N-glycan mutants of porcine reproductive and respiratory syndrome virus. Viral. Immunol. 2006. 19: 294–304.
[108] Mateu E, Diaz I, Darwich L, et al. Evolution of ORF5 of Spanish porcine reproductive and respiratory syndrome virus strains from 1991 to 2005. Virus. Res. 2006. 115: 198–206.
[109]刘光清,薛强,仇华吉,等.猪繁殖与呼吸综合征病毒CH-la猪非结构基因的分子克隆及其基因特征的研究.中国预防兽医学报. 2002. 24: 81-87.
[110] Kapur V, Elam MK, Pawlovich TM et al. Genetic variation in Porcine reproductive and respiratory Syndrome vlrus isolates in the midwesten UnitedStates. J. Gen. Virol. 1996. 77: 1271-1276
[111] Mardassi H,Mounir S,Dea S. Molecuar analysis of the 0RFs 3 to 7 of porcine reproductive and respiratory Syndrom virus Quebec reference Stain. Arch Virol. 1995. 140: 1405-1418
[112]高志强,郭鑫,杨汉春,等.猪繁殖与呼吸综合征病毒缺失变异株的基因组特征.畜牧兽医学报. 2005. 36: 578-584.
[113]童光志,周艳君,郝晓芳,等.高致病性猪繁殖与呼吸综合征病毒的分离鉴定及其分子流行病学分析.中国预防兽医学报. 2007. 5: 323-326.
[114] Tian K, Yu X, Zhao T. Emergence of Fatal PRRSV Variants: Unparalleled Outbreaks of Atypical PRRS in China and Molecular Dissection of the Unique Hallmark. PLoS. ONE. 2007. 2: 1-10.
[115] Zhou YJ, Hao XF, Tian ZJ, et al. Highly virulent porcine reproductive and respiratory syndrome virus emerged in China. Transboundary and Emerging Disease. 2008. 55: 152-164.
[116] Li Y, Wang X, Bo K, et al. Emergence of a highly pathogenic porcine reproductive and respiratory syndrome virus in the Mid-Eastern region of China. Vet. J. 2007. 174: 577-584.
[117] Johnson C, Wanqin Y, Murtaugh M. Cross-reactive antibody responses to nsp1 and Nsp2 of procine reproductive and respiratory syndrome virus. J. Gen. Virol. 2007. 88: 1184-1195.
[118] Stadejek T, Oleksiewicz MB, Potapchuk D, et al. Porcine reproductive and respiratory syndrome virus strains of exceptional diversity in Eastern Europe support the definition of new genetic subtypes. J. Gen. Virol. 2006. 87: 1835–1841.
[119] Goldberg TL, Lowe JF, Milburn SM, Firkins LD. Quasispecies variation of porcine reproductive and respiratory syndrome virus during natural infection.Virology. 2003. 317: 197–207.
[120] Lager KM, Mengeling WL, Brockmeier SL. Evaluation of protective immunity in gilts inoculated with the NADC-8 isolate of porcine reproductive and respiratory syndrome virus (PRRSV) and challenge-exposed with an antigenically distinct PRRSV isolate. Am. J. Vet. Res. 1999. 60: 1022–1027.
[121] Mengeling WL, Lager KM, Vorwald AC, et al. Strain specificity of the immune response of pigs following vaccination with various strains of porcine reproductive and respiratory syndrome virus.Vet. Microbiol. 2003. 93: 13–24.
[122] Labarque G, Reeth KV, Nauwynck H, et al. Impact of genetic diversity of European-type porcine reproductive and respiratory syndrome virus strains on vaccine efficacy.Vaccine. 2004. 22: 4183–4190.
[123] Bautista EM, Suarez P, Molitor TW. T cell responses to the structural polypeptides ofporcine reproductive and respiratory syndrome virus. Arch. Virol. 1999. 144: 117–134.
[124] Hawkes RA. Enhancement of the infectivity of arboviruses by specific antisera produced in domestic fowls. Aust J Exp Biol Med Sci. 1964. 42: 465-482.
[125] Mahalingam S, Meanger J, Foster PS, et al. The viral manipulation of the host cellular and immune environments to enhance propagation and survival: a focus on RNA viruses. J. Leukoc. Biol. 2002. 72: 429-439.
[126] Choi CS, Christianson WT, Gustafson KV, et al. Antibody-dependent enhancement of PRRS virus replication. Am. Assoc. Swine. Pract. Newsl. 1992. 4: 19-21.
[127] Mahalingam S, Lidbury BA. Suppression of lipopolysaccharide-induced antiviral transcription factor (STAT-1 and NF-kappa B) complexes by antibody-dependent enhancement of macrophage infection by Ross River virus. Proc. Natl. Acad. Sci. 2002. 99: 13819-13824.
[128] Oliphant T, Nybakken GE, Engle M, et al. Antibody Recognition and Neutralization Determinants on Domains I and II of West Nile Virus Envelope Protein. J. Virol. 2006. 15: 12149-12159.
[129] Hohdatsu T, Tokunaga J and Koyama. The role of IgG subclass of mouse monoclonal antibodies in antibody-dependent enhancement of feline infectious peritonitis virus infection of feline macrophages. Arch. Virol. 1994. 139: 273-285.
[130] Huang KJ, Yang YC, Lin YS, et al. The dual-specific binding of dengue virus and target cells for the antibody-dependent enhancement of dengue virus infection. J. Immunol. 2006. 176: 2825-2832.
[131] Lidbury BA and Mahalingam S. Specific ablation of antiviral gene expression in macrophage by antibody-dependent enhancement of Ross River virus infection. J. Virol. 2000. 74: 8376-8381.
[132] Takada A, Kawaoka Y. Antibody-dependent enhancement of viral infection: molecular mechanisms and in vivo implications. Rev. Med. Virol. 2003. 13: 387-398.
[133] Christianso WT, Choi CS, Collins JE, et al. Pathogenesis of porcine reproductive and respiratory syndrome virus infection in mid-gestation sows and fetuses. Can. J. Vet. Res. 1993. 57: 262-268.
[134] Yoon KJ, Wu LL, Zimmerman, et al. Antibody-dependent ehancement (ADE) of porcine reproductive and respiratory syndrome virus (PRRSV) infection in pigs. Viral. Immunol. 1996. 9: 51-63.
[135] Yoon KJ, Wu LL, Zimmerman JJ, et al. Field isolates of porcine reproductive and respiratory syndrome virus (PRRSV) vary in their susceptibility to antibody dependent enhancement (ADE) of infection. Vet. Mircobiol. 1997. 55: 277-287.
[136] Nimmerjahn F, Ravetch JV. Fcγreceptors as regulators of immune responses. Nat. Rev. Immunol. 2008. 8: 34-47.
[137] Nimmerjahn F, Ravetch JV. Anti-inflammatory actions of intravenous immunoglobulin.Annu. Rev. Immunol. 2008. 26: 513-33.
[138] Brady LJ. Antibody-mediated immunomodulation: a strategy to improve host response against microbial antigens. Infect Immun. 2005. 73: 671-678
[139] Rosa, G. T., L. Gillet, et al. IgG fc receptors provide an alternative infection route for murine gamma-herpesvirus-68."PLoS ONE 2007. 2: e560.
[140] Halloran PJ, Sweeney SE, Kim YB.. Biochemical characterization of the porcine Fc gamma RⅢalpha homologue G7. Cell Immunol. 1994. 153: 2631-2641
[141] Sweeney SE, Kim YB. Identification of a novel Fc gamma RⅢa alpha-associated molecule that contains significant homology to porcine cathelin. J. Immunol. 2004. 172: 1203-1212
[142]周顺伍.动物生物物实验指导.中国农业出版社,北京. 2001.
[143] Aasted B, Bach P, Nielsen J, et al. Cytokine profiles in peripheral blood mononuclear cells and lymph node cells from piglets infected in utero with porcine reproductive and respiratory syndrome virus. Clin Diagn Lab Immunol. 2002. 9: 1229-1234.
[144] Argaw T, Colon-Moran W, Wilson CA. Limited infection without evidence of replication by porcine endogenous retrovirus in guinea pigs. J Gen Virol. 2004. 85: 15-19.
[145] Delputte PL, Costers S and Nauwynck HJ. Analysis of porcine reproductive and respiratory syndrome virus attachment and internalization: distinctive roles for heparan sulphate and sialoadhesin. J Gen Virol. 2005. 86: 1441-1445.
[146] Guyre PM, Morganelli PM, Miller R. Recombinant immune interferon increases immunoglobulin G Fc receptors on cultured human mononuclear phagocytes. J. Clin. Invest. 1983. 72: 393-397.
[147] Lemke CD, Haynes JS, Spaete R, et al. Lymphoid hyperplasia resulting in immune dysregulation is caused by porcine reproductive and respiratory syndrome virus infection in neonatal pigs. J Immunol. 2004. 172: 1916-1925.
[148] Olsen CW, Corapi WV, Ngichabe CK, et al. Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages. J Virol. 1992. 66: 956-965.
[149] Rovira A, Balasch M, Segales J, et al. Experimental inoculation of conventional pigs with porcine reproductive and respiratory syndrome virus and porcine circovirus 2. J Virol. 2002. 76: 3232-3239.
[150] Pricop L, Redecha P, Teillaud JL, et al. Differential modulation of stimulatory and inhibitory Fcγreceptors on human monocytes by TH1 and TH2 cytokines. J. Immunol. 2001.166: 531-537.
[151] Radeke HH, Janssen-Graalfs I, Sowa EN, et al. Opposite regulation of type II and III receptors for immunoglobulin G in mouse glomerular mesangial cells and in the induction of anti-glomerular basement membrane (GBM) nephritis. J. Biol. Chem. 2002. 277: 27535-27544.
[152] Shushakova N, Skokowa J, Schulman J, et al. C5a anaphylatoxin is a major regulator of activating versus inhibitory FcgammaRs in immune complex-induced lung disease. J. Clin. Invest. 2002. 110: 1823-1830.
[153] Suradhat S, Thanawongnuwech R and Poovorawan Y. Upregulation of IL-10 gene expression in porcine peripheral blood mononuclear cells by porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 2003. 84: 453-459.
[154] Mateu E, Diaz I. The challenge of PRRS immunology. Vet. J. 2008. 177: 345-51
[155] Hu H, Li X, Zhang Z, Shuai J,et al. Porcine reproductive and respiratory syndrome viruses predominant in southeastern China from 2004 to 2007 were from a common source and underwent further divergence. Arch. Virol. 2009. 154:391-8
[156] Zhou L, Zhang J, Zeng J, Yin S, Li Y, et al. The 30-amino-acid deletion in the Nsp2 of highly pathogenic porcine reproductive and respiratory syndrome virus emerging in China is not related to its virulence. J. Virol. 2009. 83: 5156-67.
[157]田小辉,王爱萍,乔松林,张改平,等.猪繁殖与呼吸障碍综合征病毒ORF5基因的克隆与表达.河南农业科学. 2009. 2: 103-106