Potent neutralization of hepatitis A virus reveals a receptor mimic mechanism and the receptor recognition site.

Abstract:

:Hepatitis A virus (HAV) infects ∼1.4 million people annually and, although there is a vaccine, there are no licensed therapeutic drugs. HAV is unusually stable (making disinfection problematic) and little is known of how it enters cells and releases its RNA. Here we report a potent HAV-specific monoclonal antibody, R10, which neutralizes HAV infection by blocking attachment to the host cell. High-resolution cryo-EM structures of HAV full and empty particles and of the complex of HAV with R10 Fab reveal the atomic details of antibody binding and point to a receptor recognition site at the pentamer interface. These results, together with our observation that the R10 Fab destabilizes the capsid, suggest the use of a receptor mimic mechanism to neutralize virus infection, providing new opportunities for therapeutic intervention.

authors

Wang X,Zhu L,Dang M,Hu Z,Gao Q,Yuan S,Sun Y,Zhang B,Ren J,Kotecha A,Walter TS,Wang J,Fry EE,Stuart DI,Rao Z

doi

10.1073/pnas.1616502114

subject

Has Abstract

pub_date

2017-01-24 00:00:00

pages

770-775

issue

4

eissn

0027-8424

issn

1091-6490

pii

1616502114

journal_volume

114

pub_type

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