Journal
SCIENCE
Volume 342, Issue 6162, Pages 1090-1094Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1243876
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Funding
- NIH [AI079031, AI080916, AI071084, AI084817, U54 GM094586]
- Skaggs Institute
- American Foundation for AIDS Research
- Swiss National Science Foundation
- NIH through the National Center for Research Resources' P41 program at the National Center for Research Resources [RR017573]
- DOE Office of Biological and Environmental Research
- NIH's National Center for Research Resources, Biomedical Technology Program [P41RR001209]
- National Institute of General Medical Sciences (NIGMS)
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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 fold and therefore provide valuable information for HCV drug and vaccine design.
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