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Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM
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Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM
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Journal Article
Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM
2009
Overview
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 Å) 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.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Antigens, Viral - metabolism
/ Antigens, Viral - ultrastructure
/ Calcium
/ Capsid
/ Capsid Proteins - metabolism
/ Capsid Proteins - ultrastructure
/ Cryoelectron Microscopy - methods
/ epitopes
/ Genes
/ genome
/ Genomics
/ Protein Structure, Quaternary
/ Proteins
/ RNA
/ Trimers
/ Viral Core Proteins - chemistry
/ Viral Core Proteins - metabolism
/ Viral Core Proteins - ultrastructure
/ Virions
/ Viruses
