Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins

被引：110

作者：

Garry, RF

Dash, S

机构：

[1] Tulane Univ, Hlth Sci Ctr, Dept Microbiol & Immunol, New Orleans, LA 70112 USA

[2] Tulane Univ, Hlth Sci Ctr, Dept Lab Med & Pathol, New Orleans, LA 70112 USA

来源：

VIROLOGY | 2003年 / 307卷 / 02期

关键词：

viral fusion proteins; hepatitis C virus envelope glycoproteins; pestivirus; proteomics; glycoprotein structure; virus evolution;

D O I：

10.1016/S0042-6822(02)00065-X

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Class 11 fusion proteins encoded by tick-borne encephalitis virus (TBEV), dengue virus, and Semliki Forest virus have a fusion peptide located at the end of a rod-like molecule comprised of three antiparallel beta sheet domains. Proteomics computational analyses suggest that hepatitis C virus (HCV) envelope glycoprotein E1 and pestivirus envelope glycoprotein E2 are truncated class 11 fusion proteins. Similarities were also detected between the receptor-binding portion of TBEV E and HCV E2, and between TBEV small membrane protein precursor prM and pestivirus El. The proposed models of Flaviviridae envelope proteins can facilitate drug and vaccine development. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：255 / 265

页数：11

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