Antibody-induced Uncoating of Human Rhinovirus B14

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2017 Jul 12

PMID 28696310

Citations 30

Authors

Yangchao Dong

Yue Liu

Wen Jiang

Thomas J Smith

Zhikai Xu

Michael G Rossmann

Affiliations

Soon will be listed here.

Abstract

Rhinoviruses (RVs) are the major causes of common colds in humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 Å and 3.0 Å resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody-virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.

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