IR@PKUHSC  > 北京大学基础医学院  > 病原生物学系
学科主题基础医学
Analysis of hepatitis E virus neutralization sites using monoclonal antibodies directed against a virus capsid protein
Zhang, J; Gu, Y; Ge, SX; Li, SW; He, ZQ; Huang, GY; Zhuang, H; Ng, MH; Xia, NS
关键词hepatitis E virus neutralization sites monoclonal antibodies
刊名VACCINE
2005-04-22
DOI10.1016/j.vaccine.2004.11.065
23期:22页:2881-2892
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Immunology ; Medicine, Research & Experimental
研究领域[WOS]Immunology ; Research & Experimental Medicine
关键词[WOS]IMMUNODEFICIENCY VIRUSES ; VIRAL-HEPATITIS ; UNITED-STATES ; RISK-FACTORS ; HEV ; IDENTIFICATION ; CHALLENGE ; INFECTION ; SEROREACTIVITY ; POLIOVIRUS
英文摘要

The dimeric form of the recombinant peptide (E2), comprising amino acid 394-606 of the capsid protein of hepatitis E virus (HEV), is strongly recognized by HEV reactive human serum, and when used as a vaccine, it protects rhesus monkeys against experimental HEV infection. In this work, the relationship of E2 to HEV has been probed using three murine monoclonal antibodies, 8C11, 13D8 and 8H3, all of which react predominantly against the E2 dimer, and can effect immune capture of the virus as well. 8C11 and 8H3 were further found to neutralize HEV infectivity in animals. Cross-blocking patterns between these antibodies discerned two spatially separate antigenic domains, one identified by 8C11 and 13D8, and the other, by 8H3. Kinetic studies using BIAcore biosensor suggest that the epitope to which 8H3 is directed is partially masked, and thus has limited access by the native antibody. However, this is not the case with the smaller Fab. Access to the 8H3 epitope was enhanced by the binding of 8C11, and inhibited by the binding of 13D8 to a distal site on the peptide. Similar to the effects of binding 8H3 to E2, 8C11 was found to enhance immune capture by 8H3, while 13D8 was inhibitory. Moreover, 8C11 and 8H3 act synergistically to neutralize HEV infectivity. The parallel cross-reaction patterns that these antibodies exhibit against the peptide and the virus, respectively, implicate two interacting conformationally dependent neutralization sites on the HEV particle. These sites might cooperate in the adsorption and penetration of the HEV virus. (c) 2004 Elsevier Ltd. All rights reserved.

语种英语
WOS记录号WOS:000228318800008
Citation statistics
Cited Times:59[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/56787
Collection北京大学基础医学院_病原生物学系
作者单位1.Guangxi Autonomous Reg, Ctr Dis Control, Nanning 430021, Peoples R China
2.Xiamen Univ, Sch Life Sci, Key Lab Minist Educ Cell Biol & Tumor Cell Engn, Xiamen 361005, Peoples R China
3.Xiamen Univ, Res Ctr Med Mol Virol Fujian Province, Xiamen 361005, Peoples R China
4.Peking Univ, Hlth Sci Ctr, Dept Microbiol, Beijing 100083, Peoples R China
Recommended Citation
GB/T 7714
Zhang, J,Gu, Y,Ge, SX,et al. Analysis of hepatitis E virus neutralization sites using monoclonal antibodies directed against a virus capsid protein[J]. VACCINE,2005,23(22):2881-2892.
APA Zhang, J.,Gu, Y.,Ge, SX.,Li, SW.,He, ZQ.,...&Xia, NS.(2005).Analysis of hepatitis E virus neutralization sites using monoclonal antibodies directed against a virus capsid protein.VACCINE,23(22),2881-2892.
MLA Zhang, J,et al."Analysis of hepatitis E virus neutralization sites using monoclonal antibodies directed against a virus capsid protein".VACCINE 23.22(2005):2881-2892.
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