Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/36123
標題: 傳染性華氏囊病病毒VP2蛋白中和性抗原決定區位之分析
Identification of the neutralization epitopes on infectious bursal disease virus capsid protein VP2
作者: 邱芳誼
Chiu, Fang-Yi
關鍵字: infectious bursal disease virus;傳染性華氏囊病病毒
出版社: 生物科技學研究所
引用: 郁筱玲,1992。傳染性華氏囊病毒基因表現。碩士論文。中興大學獸醫學研究所。台中。 Azad, A. A., M. N. Jagadish, M. A. Brown, P. J. Judson, and 1987. Deletion mapping and expression in Escherichia coli of the large genomic segment of a Binavirus. Virology 161:145-152. Azad, A. A., N. M. Mckern, I. G. Macreadie, P. Failla, Heine, H. G., , A. Chapman, C. W. Ward, and K. J. Fahey. 1991. Physicochemical and immunological chaacterization of recombinant host-protective antigen (VP2) of infectious bursal disease virus. Vaccine 9:715-722. Barnes, H. J., J. Wheeler, and D. Reed. 1982. Serological evidence of infectious bursal disease virus infection in Iowa turkey. Avian Dis. 26:560-565. Bayliss, C. D., U. Spies, K. Shaw, R. W. Peters, A. Papageorgiou, H. Muller, and M. E. Boursnell. 1990. A comparison of the sequences of segment A of four infectious bursal disease virus strains and identification of a variable region in VP2. J Gen Virol 71 ( Pt 6):1303-12. Becht, H., H. Muller, and H. K. Muller. 1988. Comparative studies on structural and antigenic properties of two serotypes of infectious bursal disease virus. J Gen Virol 69 ( Pt 3):631-40. Berg van den, T. P. 2000. Acute infectious bursal disease in poultry: a review. Avian Pathol 29:175-194. Berg, v. d. 2000. Acute infectious bursal disease in poultry: a review. Avian Pathology 29:175-194. Böttcher, B., N. A. Kiselev, V. Y. Stel’Mashchuk, and N. A. Perevozchikova. 1997. Three-dimensional structure of infectious bursal disease virus determined by electron cryomicroscopy. J Virol 71:325-330. Castón, J. R., J. L. Martínez-Torrecuadrada, A. Maraver, E. Lombardo, J. F. Rodricuez, C. J. I., and C. J. L. 2001 C terminus of infectious bursal disease virus major capsid protein VP2 is involved in definition of the T number for capsid assembly. J Virol 75:10815- 10828. Chang, H. C., T. L. Lin, and C. C. Wu. 2001. DNA-mediated vaccination against infectious bursal disease in chickens. Vaccine 20:328-35. Charpilienne, A., M. Nejmeddine, M. Berois, N. Parez, E. Neumann, E. Hewat, G. Trugnan, and C. J. 2001. Individual Rotavirus-like particles containing 120 molecules of fluorescent protein are visible in living cell. J Biol Chem 276:29361-29367. Coulibaly, F., C. Chevalier, I. Gutsche, J. Pous, J. Navaza, S. Bressanelli, B. Delmas, and F. A. Rey. 2005. The birnavirus crystal structure reveals structural relationships among icosahedral viruses. Cell 120:761-72. Cui, X., H. S. Nagesha, and I. H. Holmes. 2003. Identification of crucial residues of conformational epitopes on VP2 protein of infectious bursal disease virus by phage display. J Virol Methods 109:75-83. Cui, X., H. S. Nagesha, and I. H. Holmes. 2003. Mapping of conformational epitopes on capsid protein VP2 of infectious bursal disease virus by fd-tet phage display. J Virol Methods 114:109-12. Da Costa, B., S. Soignier, C. Chevalier, C. Henry, C. Thory, J. C. Huet, and B. Delmas. 2003. Blotched snakehead virus is a new aquatic birnavirus that is slightly more related to avibirnavirus than to aquabirnavirus. J Virol 77:719-25. Dobos, P., B. J. Hill, R. Hallett, D. T. Kells, H. Becht, and D. Teninges. 1979. Biophysical and biochemical characterization of five animal viruses with bisegmented double-stranded RNA genomes. J Virol 32:593-605. Fahey, K. J., E. Katrina, and J. C. 1989. A conformational immunogen on VP-2 of Infectious Bursal Disease Viurs that induces virus-neutralizing antibodies that passively protect chickens. J Gen Virol 70:1473-1481. Goldmann, C., H. Petry, S. Frye, Ast, O., , S. Ebitsch , J. D. Jentsch, F. J. Kaup, F. Weber, C. Trebst, T. Nisslein, G. Hunsmann, Weber T., and W. Kűke. 1999. Molecular cloning and expression of major structural protein VP1 of the human Polyomavirus JC virus: formation of virus-like particles useful for immunological and therapeutic studies. J Virol 73:4465-4469. Goldsby, R. A., T. J. Kindt, B. A. Osborne, and J. Kuby. 2003. Immunology W. H. Freeman and Company, New York. Heine, H. G., M. Haritou, P. Failla, K. Fahey, and A. Azad. 1991. Sequence analysis and expression of the host-protective immunogen VP2 of a variant strain of infectious bursal disease virus which can circumvent vaccination with standard type I strains. J Gen Virol 72 ( Pt 8):1835-43. Hudson, P. J., N. M. McKern, K. J. Fahey, and A. A. Azad. 1986. Predicted sequence of the host-protective immunogen of infectious bursal disease virus. FEBS Lett 201:143-6. Hurtado, A., P. Rueda, J. Nowicky, J. Sarraseca, and J. I. Casal. 1996. Identification of domains in canine parvovirus VP2 essential for the assembly of virus-like particles. J Virol 70:5422-9. Jagadish, M. N., and A. A. Azad. 1991. Localization of a VP3 epitope of infectious bursal disease virus. Virology 184:805-7. Jagadish, M. N., V. J. Staton, P. J. Hudson, and A. A. Azad. 1988. Birnavirus precursor polyprotein is processed in Escherichia coli by its own virus-encoded polypeptide. J Virol 62:1084-1087. Kibenge, F. S. B., A. S. Dhillon, and R. G. Russell. 1988. Biochemistry and immunology of infectious bursal disease virus. J Gen Virol 69 1757- 1775. Kochan, G., D. Gonzalez, and J. F. Rodriguez. 2003. Characterization of the RNA-binding activity of VP3, a major structural protein of Infectious bursal disease virus. Arch Virol 148:723-744. Lee, C. C., T. P. Ko, C. C. Chou, M. Yoshimura, S. R. Doong, M. Y. Wang, and A. H. Wang. 2006. Crystal structure of infectious bursal disease virus VP2 subviral particle at 2.6A resolution: Implications in virion assembly and immunogenicity. J Struct Biol 155:74-86. Lee, C. C., T. P. Ko, M. S. Lee, C. C. Chou, S. Y. Lai, A. H. Wang, and M. Y. Wang. 2003. Purification, crystallization and preliminary X-ray analysis of immunogenic virus-like particles formed by infectious bursal disease virus (IBDV) structural protein VP2. Acta Crystallogr D Biol Crystallogr 59:1234-7. Lee, L. H., J. S. Lu, and N. J. Lii. 1988. Characterization of infectious bursal disease virus isolated in Taiwan. J Chin Soc Vet Sc 14:89-100. Lejal, N., B. D. Costa, J. C. Huet, and B. Delmas. 2000. Role of Ser-692 in the protease activity of infectious bursal disease VP4 and identification of its substrate cleavage sites. J Gen Virol 81:983-992. Lim, B. L., Y. Cao, T. Yu, and C. W. Mo. 1999. Adaptation of very virulent infectious bursal disease virus to chicken embryonic fibroblasts by site-directed mutagenesis of residues 279 and 284 of viral coat protein VP2. J Virol 73:2854-62. Maraver, A., R. Clemente, J. F. Rodriguez, and E. Lombardo. 2003. Identification and molecular characterization of the RNA polymerase- binding motif of infectious bursal disease virus inner capsid protein VP3. J Virol 77:2459-68. Martinez-Torrecuadrada, J. L., J. R. Caston, M. Castro, J. L. Carrascosa, J. F. Rodriguez, and J. I. Casal. 2000. Different architectures in the assembly of infectious bursal disease virus capsid proteins expressed in insect cells. Virology 278:322-31. Mcherran, J. B., M. S. Mcnulty, T. J. Connor, C. Mccrackin, D. S., , G. M., and E. R. Mckillop. 1980. Isolation and serological studies with infectious bursal disease virus from fowl turkeys and ducks demonstration of second serotype. Avian Pathol 9:395-404. Morgan, M. M., I. G. Macreadie, V. R. Harley, P. J. Hudson, and A. A. Azad. 1988 Sequence of the small double-stranded RNA genomic segment of infectious bursal disease virus and its deduced 90-kDa product. Virology 163:240-242. Muller, H., and H. Becht. 1982. Biosynthesis of virus-specific proteins in cells infected with infectious bursal disease virus and their significance as structural elements for infectious virus and incomplete particles. J Virol 44:384-392. Mundt, E., B. Köllner, and D. Kretzschmar. 1997. VP5 of infectious bursal disease virus is not essential for viral replication in cell culture. J Virol 71:5647-5651. Okoye, J. O., and M. Uzoukwu. 1981. An outbreak of infectious bursal disease among chickens between 16 and 20 weeks old. Avian Dis 25:1034-8. Pitcovski, J., B. Z. Levi, T. Maray, D. Di-Castro, A. Safadi, S. Krispel, A. Azriel, B. Gutter, and A. Michael. 1999. Failure of viral protein 3 of infectious bursal disease virus produced in prokaryotic and eukaryotic expression systems to protect chickens against the disease. Avian Dis 43:8-15. Rueda, P., A. Hurtado, M. Barrio, J. L. M. Torrecuadrada, S. Kamstrup, C. Leclerc, and J. I. Casal. 1999. Minor displacements in the insertion site provoke major differences in the induction of antibody responses by chimeric parvovirus-like particles. Virology 263:89-99. Schnitzler, D., F. Bernstein, H. Muller, and H. Becht. 1993. The genetic basis for the antigenicity of the VP2 protein of the infectious bursal disease virus. J Gen Virol 74 ( Pt 8):1563-71. Sharma, J. M. 1999. Introduction to poultry vaccines and immunity. Adv Vet Sci Comp Med 41:481-494. Snyder, D. B., D. P. Lana, B. R. Cho, and W. W. Marquardt. 1988. Group and strain-specific neutralization sites of infectious bursal disease virus defined with monoclonal antibodies. Avian Dis 32:527-34. Tacken, M. G. J., P. J. M. Rottier, A. L. J. Gielkens, and B. P. H. Peeters. 2000. Interaction in vivo between the proteins of infectious brusal disease virus: capsid protein VP3 interacts with the RNA-dependent RNA polymerase, VP1. J Gen Virol 81:209-218. van Loon, A. A., N. de Haas, I. Zeyda, and E. Mundt. 2002. Alteration of amino acids in VP2 of very virulent infectious bursal disease virus results in tissue culture adaptation and attenuation in chickens. J Gen Virol 83:121-9. Wang, M. Y., Y. Y. Kuo, M. S. Lee, S. R. Doong, J. Y. Ho, and L. H. Lee. 2000. Self-assembly of the infectious bursal disease virus capsid protein, rVP2, expressed in insect cells and purification of immunogenic chimeric rVP2H particles by immobilized metal-ion affinity chromatography. Biotechnol Bioeng 67:104-11. Wang, X. N., G. P. Zhang, J. Y. Zhou, C. H. Feng, Y. Y. Yang, Q. M. Li, J. Q. Guo, H. X. Qiao, J. Xi, D. Zhao, G. X. Xing, Z. L. Wang, S. H. Wang, Z. J. Xiao, X. W. Li, and R. G. Deng. 2005. Identification of neutralizing epitopes on the VP2 protein of infectious bursal disease virus by phage-displayed heptapeptide library screening and synthetic peptide mapping. Viral Immunol 18:549-57. Wyeth, P. J. 1975. Effect of infectious bursal disease on the response of chickens to S typhimurium and E coli infections. Vet Rec 96:238-43. Wyeth, P. J. 1975. Effect of infectious bursal disease on the response of chickens to S typhimurium and E. coli infections. Vet Rec 96:238-43. Wyeth, P. J., and G. A. Cullen. 1978. Transmission of immunity from inactivated infectious bursal disease oil-emulsion vaccinated parent chickens to their chicks. Vet Rec 102:362-3. Yao, K., and V. N. Vakharia. 2001. Induction of apoptosis of in vitro by the 17-kDa nonstructural protein of infectious bursal disease virus: possible role in viral pathogenesis. Virology 285:50-58.
摘要: 
傳染性華氏囊病病毒(infectious bursal disease virus, IBDV)是造成雞隻傳染性華氏囊病變的病源,感染幼雞後會破壞華氏囊組織中的B淋巴細胞,造成雞隻免疫能力受損。其外鞘蛋白VP2具參與病毒接受體的結合及宿主細胞辨識的功能,其帶有能引發中和病毒之抗體的抗原決定區。若單獨表現VP2蛋白則會形成T=1 之次病毒顆粒(subviral particle, SVP)本研究將由SVP誘導出之單株抗體來找尋IBDV之中和性抗原決定區。先前研究已知VP2胺基酸序列204-344為高度變異區,本實驗依此高度變異區設計出多段VP2重組蛋白及合成胜肽(peptides),並利用單株抗體以病毒中和試驗、免疫連結吸附法、西方轉漬法及免疫沉澱等其他分析法找出IBDV之中和性抗原決定區。結果顯示由多株單株抗體中分別篩選出1株具中和效力之抗體Mab SVP-4及1株不具中和效力之抗體Mab SVP-1,其皆可辨認到VP2似病毒顆粒(SVP)及野生株(wild-type)的病毒(IBDV-P3009),而這2株單株抗體亦可辨識實驗中所構築的一段VP2重組蛋白。未來將於VP2蛋白做適當的截切,更進一步找出中和性抗原決定區。

Infectious bursal disease virus (IBDV) is the causative agent of infectious bursal disease, which is one of the most important and widespread infectious disease in commercial chickens. The structural protein VP2 spontaneously form a T=1 subviral particle (SVP). The conformational epitopes has been reported in the highly variable region of VP2 protein of IBDV. In previously study, the amino acid residues 204 to 344 of VP2 had been reported as hypervariable region, which is responsible to antibody binding. Here, we mainly use the monoclonal antibodies to identify the neutralizing epitopes. In this study, three recombinant proteins (NH61-202, CH196-329, NH291-441) of VP2 and four synthetic 16-mer peptides (PBC, PDE, PFG, PHI) were prepared and using virus neutralization assay、ELISA、western blot and immunoprepicitation to identify the neutralizing epitopes. In our results, two monoclonal antibodies (Mab SVP-1, Mab SVP-4) interact to SVP, wild-type IBDV virion. All monoclonal antibodies (Mabs) bind to the region of VP2 between amino acids ranging from 196 to 329. We investigate the possibility of the existence of linear neutralizing epitopes on IBDV in order to provide information for future development of a safe and effective synthetic peptide vaccine.
URI: http://hdl.handle.net/11455/36123
其他識別: U0005-2408200620113300
Appears in Collections:生物科技學研究所

Show full item record
 

Google ScholarTM

Check


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.