Ontology highlight
ABSTRACT:
SUBMITTER: Kong L
PROVIDER: S-EPMC3497658 | biostudies-literature | 2012 Dec
REPOSITORIES: biostudies-literature
Journal of virology 20120912 23
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. ...[more]