期刊
VIROLOGY
卷 448, 期 -, 页码 229-237出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2013.10.020
关键词
Hepatitis C virus; Envelope protein 2; Cysteine; Disulfide bond; CD81 binding; E1E2 heterodimers; HCVpp; Antigenicity
类别
资金
- 973 Program of China [2009CB522501, 2009CB522503]
- National S&T Major Project for Infectious Diseases Control [2012ZX10002003-004-010]
- Natural Science Foundation of China [81071364, 31170150, 81373235]
- Shanghai Leading Academic Discipline Project [B901]
Envelope glycoprotein 2 (E2) of hepatitis C virus contains 18 conserved cysteine (Cys) residues in its ectodomain. By cysteine-alanine mutagenesis and function analysis, six Cys in H77 E2 (C494, C508, C552, C564, C607 and C644) were found to be indispensable for recognition by conformation-dependent mAb H53. Removal of any of these Cys residues did not affect E2 heterodimerization with El, but notably reduced E1E2 transmembrane transportation. These Cys together with C429 and C503 were required for conformation-dependent mAb H48 recognition. All of the above Cys except C607 were required for H77 and Con1 E2 binding to CD81. None of individual mutation of above Cys affected the ability of E2 to induce neutralizing antibodies in mice. Mouse antibodies mainly recognize E2 linear epitopes and are unrelated to epitopes recognized by human E2 antibodies. The findings provide new insights for understanding the biogenesis of functional HCV envelope proteins and HCV neutralizing immunity. (C) 2013 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据