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Structure-function analysis of the hepatitis C virus (HCV) envelope glycoproteins, E1 and E2, has been difficult due to the unavailability of HCV virions. Truncated soluble forms of E2 have been used as models to study virus interaction with the putative HCV receptor CD81, but they may not fully mimic E2 structures on the virion. Here, we compared the CD81-binding characteristics of truncated E2 (E2(660)) and full-length (FL) E1E2 complex expressed in mammalian cells, and of HCV virus-like particles (VLPs) generated in insect cells. All three glycoprotein forms interacted with human CD81 in an in vitro binding assay, allowing us to test a panel of well-characterized anti-E2 monoclonal antibodies (MAbs) for their ability to inhibit the glycoprotein-CD81 interaction. MAbs specific for E2 amino acid (aa) regions 396-407, 412-423 and 528-535 blocked binding to CD81 of all antigens tested. However, MAbs specific for regions 432-443, 436-443 and 436-447 inhibited the interaction of VLPs, but not of E2(660) or the FL E1E2 complex with CD81, indicating the existence of structural differences amongst the E2 forms. These findings underscore the need to carefully select an appropriate ligand for structure-function analysis.

Original publication




Journal article


J Gen Virol

Publication Date





1877 - 1883


Animals, Antibodies, Monoclonal, Antibodies, Viral, Antigens, CD, Baculoviridae, COS Cells, Cell Line, Cercopithecus aethiops, Epitopes, Genetic Vectors, Glycoproteins, Hepacivirus, Humans, Insecta, Membrane Proteins, Protein Binding, Receptors, Virus, Recombination, Genetic, Tetraspanin 28, Transfection, Vaccinia virus, Viral Envelope Proteins, Viral Proteins