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Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM

TitleMolecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM
Publication TypeJournal Article
Year of Publication2009
AuthorsChen, JZ, Settembre EC, Aoki ST, Zhang X, Bellamy AR, Dormitzer PR, Harrison SC, Grigorieff N
Refereed DesignationRefereed
JournalProc Natl Acad Sci U S A
Volume106
Pagination10644-48
Date PublishedJUN 30
ISSN0027-8424
Abstract

Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 angstrom) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal "arms'' of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca2+-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.

DOI10.1073/pnas.0904024106
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