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

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Proceedings of the National Academy of Sciences of the United States of America. 2009 Jun 30;106(26):10644-8. doi: 10.1073/pnas.0904024106

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

Chen JZ, Settembre EC, Aoki ST, Zhang X, Bellamy AR, Dormitzer PR, Harrison SC, Grigorieff N

Note: Research in this publication was not performed at Janelia.

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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 A) 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 Ca(2+)-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.

PMID: 19487668 [PubMed - indexed for MEDLINE]

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

Note: Research in this publication was not performed at Janelia.

Abstract

PMID: 19487668 [PubMed - indexed for MEDLINE]

Janelia Authors