Antibody-induced uncoating of human rhinovirus B14

Yangchao Dong, Yue Liu, Wen Jiang, Thomas Smith, Zhikai Xu, Michael G. Rossmann

Research output: Contribution to journalArticle

23 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)8017-8022
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume114
Issue number30
DOIs
StatePublished - Jul 25 2017

Keywords

  • Antibody
  • Atomic structure
  • Cryo-electron microscopy
  • Genome release
  • Rhinovirus

ASJC Scopus subject areas

  • General

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