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

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


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.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Antibodies, Neutralizing / chemistry*
  • Antibodies, Neutralizing / metabolism
  • Epitopes / chemistry
  • Epitopes / genetics
  • Hepacivirus / genetics*
  • Models, Molecular*
  • Protein Conformation*
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / metabolism


  • Antibodies, Neutralizing
  • Epitopes
  • Viral Envelope Proteins
  • glycoprotein E2, Hepatitis C virus