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Article

Effect of mutations in VP5 hydrophobic loops on rotavirus cell entry.

Journal of virology - 1 Jun 2010

Kim Irene S, Trask Shane D, Babyonyshev Marina, Dormitzer Philip R, Harrison Stephen C

Abstract excerpt

Experiments in cell-free systems have demonstrated that the VP5 cleavage fragment of the rotavirus spike protein, VP4, undergoes a foldback rearrangement that translocates three clustered hydrophobic loops from one end of the molecule to the other. This conformational change resembles the foldback rearrangements of enveloped virus fusion proteins. By recoating rotavirus subviral particles with recombinant VP4 and...

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Source

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Identifiers

PMID: 20375171
DOI: 10.1128/JVI.02461-09
PMCID: PMC2876642

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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