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Article

Cryo-EM maps reveal five-fold channel structures and their modification by gatekeeper mutations in the parvovirus minute virus of mice (MVM) capsid.

Virology - 1 Oct 2017

Subramanian Suriyasri, Organtini Lindsey J, Grossman Alec, Domeier Phillip P, Cifuente Javier O, Makhov Alexander M, Conway James F, D'Abramo Anthony, Cotmore Susan F, Tattersall Peter, Hafenstein Susan

Abstract excerpt

In minute virus of mice (MVM) capsids, icosahedral five-fold channels serve as portals mediating genome packaging, genome release, and the phased extrusion of viral peptides. Previous studies suggest that residues L172 and V40 are essential for channel function. The structures of MVMi wildtype, and mutant L172T and V40A virus-like particles (VLPs) were solved from cryo-EM data. Two constriction points, termed the...

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Identifiers

PMID: 28750325
DOI: 10.1016/j.virol.2017.07.015
PMCID: PMC5601314

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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