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Hepatitis C virus E2 envelope glycoprotein core structure

Academic Article
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Overview

authors

  • Kong, L.
  • Giang, E.
  • Nieusma, T.
  • Kadam, R. U.
  • Cogburn, K. E.
  • Hua, Y.
  • Dai, X.
  • Stanfield, Robyn
  • Burton, Dennis
  • Ward, Andrew
  • Wilson, Ian
  • Law, Mansun

publication date

  • November 2013

journal

  • Science  Journal

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 ? 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.
  • 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.

subject areas

  • Antibodies, Neutralizing
  • Antigens, CD81
  • Antiviral Agents
  • Binding Sites
  • Crystallography, X-Ray
  • Drug Design
  • Epitopes
  • Humans
  • Immunoglobulin Fab Fragments
  • Mutagenesis, Site-Directed
  • Protein Folding
  • Protein Structure, Tertiary
  • Viral Envelope Proteins
  • Viral Hepatitis Vaccines
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Identity

PubMed Central ID

  • PMC3954638

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1243876

PubMed ID

  • 24288331
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Additional Document Info

start page

  • 1090

end page

  • 1094

volume

  • 342

issue

  • 6162

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