HCV Envelope Glycoproteins in Evirion Assembly and Entry

Abstract

ABSTRACT HCV encodes two envelope glycoproteins, E1 and E2, which assemble as a non-covalent heterodimer in infected cells. During HCV morphogenesis, these proteins are incorporated into viral particles and they are the major viral determinants of HCV entry. Functional studies have revealed unique features in these viral envelope glycoproteins. Indeed, E1–E2 interaction, mediated by their transmembrane domain, is essential for HCV assembly and entry. Furthermore, recent data also show that these glycoproteins interact with apolipoproteins. Recent crystallography data provide some structural support to better understand how these proteins interact with the host. In this review, we summarize the biogenesis of HCV envelope glycoproteins and their role in HCV morphogenesis in the context of the hijacking of the very low-density lipoprotein assembly pathway by this virus. We also describe the functions of HCV glycoproteins during virus entry with a special focus on the unexpected structural features of E2 glycoprotein. Finally, we discuss the major neutralizing epitopes in the light of E2 structure.