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J Virol. 2012 Dec;86(23):13085-8. doi: 10.1128/JVI.01939-12. Epub 2012 Sep 12.

Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33.

Author information

1
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, USA.

Abstract

We have determined the crystal structure of the broadly neutralizing antibody (bnAb) AP33, bound to a peptide corresponding to hepatitis C virus (HCV) E2 envelope glycoprotein antigenic site 412 to 423. Comparison with bnAb HCV1 bound to the same epitope reveals a different angle of approach to the antigen by bnAb AP33 and slight variation in its β-hairpin conformation of the epitope. These structures establish two different modes of binding to E2 that antibodies adopt to neutralize diverse HCV.

PMID:
22973046
PMCID:
PMC3497658
DOI:
10.1128/JVI.01939-12
[Indexed for MEDLINE]
Free PMC Article

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