skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Hepatitis C Virus E2 Envelope Glycoprotein Core Structure

Abstract

Hepatitis C virus (HCV), a Hepacivirus, is a major cause of viral hepatitis, liver cirrhosis, and hepatocellular carcinoma. HCV envelope glycoproteins E1 and E2 mediate fusion and entry into host cells and are the primary targets of the humoral immune response. The crystal structure of the E2 core bound to broadly neutralizing antibody AR3C at 2.65 angstroms reveals a compact architecture composed of a central immunoglobulin-fold β sandwich flanked by two additional protein layers. The CD81 receptor binding site was identified by electron microscopy and site-directed mutagenesis and overlaps with the AR3C epitope. The x-ray and electron microscopy E2 structures differ markedly from predictions of an extended, three-domain, class II fusion protein fold and therefore provide valuable information for HCV drug and vaccine design.

Authors:
 [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1]
  1. The Scripps Research Inst., La Jolla, CA (United States)
Publication Date:
Research Org.:
SLAC National Accelerator Lab., Menlo Park, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1154700
Report Number(s):
SLAC-REPRINT-2014-279
Journal ID: ISSN 0036-8075
DOE Contract Number:  
AC02-76SF00515
Resource Type:
Journal Article
Resource Relation:
Journal Name: Science; Journal Volume: 342; Journal Issue: 6162
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; CHEM

Citation Formats

Kong, Leopold, Giang, Erick, Nieusma, Travis, Kadam, Rameshwar U., Cogburn, Kristin E., Hua, Yuanzi, Dai, Xiaoping, Stanfield, Robyn L., Burton, Dennis R., Ward, Andrew B., Wilson, Ian A., and Law, Mansun. Hepatitis C Virus E2 Envelope Glycoprotein Core Structure. United States: N. p., 2014. Web. doi:10.1126/science.1243876.
Kong, Leopold, Giang, Erick, Nieusma, Travis, Kadam, Rameshwar U., Cogburn, Kristin E., Hua, Yuanzi, Dai, Xiaoping, Stanfield, Robyn L., Burton, Dennis R., Ward, Andrew B., Wilson, Ian A., & Law, Mansun. Hepatitis C Virus E2 Envelope Glycoprotein Core Structure. United States. doi:10.1126/science.1243876.
Kong, Leopold, Giang, Erick, Nieusma, Travis, Kadam, Rameshwar U., Cogburn, Kristin E., Hua, Yuanzi, Dai, Xiaoping, Stanfield, Robyn L., Burton, Dennis R., Ward, Andrew B., Wilson, Ian A., and Law, Mansun. Tue . "Hepatitis C Virus E2 Envelope Glycoprotein Core Structure". United States. doi:10.1126/science.1243876.
@article{osti_1154700,
title = {Hepatitis C Virus E2 Envelope Glycoprotein Core Structure},
author = {Kong, Leopold and Giang, Erick and Nieusma, Travis and Kadam, Rameshwar U. and Cogburn, Kristin E. and Hua, Yuanzi and Dai, Xiaoping and Stanfield, Robyn L. and Burton, Dennis R. and Ward, Andrew B. and Wilson, Ian A. and Law, Mansun},
abstractNote = {Hepatitis C virus (HCV), a Hepacivirus, is a major cause of viral hepatitis, liver cirrhosis, and hepatocellular carcinoma. HCV envelope glycoproteins E1 and E2 mediate fusion and entry into host cells and are the primary targets of the humoral immune response. The crystal structure of the E2 core bound to broadly neutralizing antibody AR3C at 2.65 angstroms reveals a compact architecture composed of a central immunoglobulin-fold β sandwich flanked by two additional protein layers. The CD81 receptor binding site was identified by electron microscopy and site-directed mutagenesis and overlaps with the AR3C epitope. The x-ray and electron microscopy E2 structures differ markedly from predictions of an extended, three-domain, class II fusion protein fold and therefore provide valuable information for HCV drug and vaccine design.},
doi = {10.1126/science.1243876},
journal = {Science},
number = 6162,
volume = 342,
place = {United States},
year = {Tue Aug 26 00:00:00 EDT 2014},
month = {Tue Aug 26 00:00:00 EDT 2014}
}