Journal
JOURNAL OF VIROLOGY
Volume 86, Issue 23, Pages 13085-13088Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01939-12
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Funding
- 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)
- NIH [AI79031, AI84817, GM U54 GM094586]
- Skaggs Institute
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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 beta-hairpin conformation of the epitope. These structures establish two different modes of binding to E2 that antibodies adopt to neutralize diverse HCV.
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