HCV/E2 core structures and mAbs: something is still missing

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Recently described HCV E2 core crystallographic structures greatly improve the knowledge about this elusive protein. However, they partially disagree with immunological and functional data. This paper highlights these discrepancies and proposes an alternative structural arrangement.

The lack of structural information on hepatitis C virus (HCV) surface proteins has so far hampered the development of effective vaccines. Recently, two crystallographic structures have described the core portion (E2c) of E2 surface glycoprotein, the primary mediator of HCV entry. Despite the importance of

these studies, the E2 overall structure is still unknown and, most importantly, several biochemical and functional studies are in disagreement with E2c structures. Here, the main literature will be discussed and an alternative disulfide bridge pattern will be proposed, based on unpublished human monoclonal antibody reactivity. A modeling strategy aiming at recapitulating the available structural and functional studies of E2 will also be proposed.

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