학술논문

Hepatitis C virus E2 envelope glycoprotein core structure
REPORTS
Document Type
Author abstract
Report
Source
Science. Nov 29, 2013, Vol. 342 Issue 6162, p1090, 5 p.
Subject
Properties
Health aspects
Glycoproteins -- Properties
Hepatitis C virus -- Health aspects
Crystal structure
Mutagenesis
Crystals -- Structure
Language
English
ISSN
0036-8075
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 [beta] 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 ford and therefore provide valuable information for HCV drug and vaccine design. 10.1126/science.1243876