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Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods
Published on: May 11, 2018
Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33
Leopold Kong1, Erick Giang, Travis Nieusma
1Department 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.
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