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Article

Identification of the structural basis of thermal lability of a virus provides a rationale for improved vaccines.

Structure (London, England : 1993) - 4 Nov 2014

Rincón Verónica, Rodríguez-Huete Alicia, López-Argüello Silvia, Ibarra-Molero Beatriz, Sanchez-Ruiz Jose M, Harmsen Michiel M, Mateu Mauricio G

Abstract excerpt

Virus stability and dynamics play critical roles during infection. Some viruses, including foot-and-mouth disease virus (FMDV), are surprisingly prone to thermal dissociation outside the cell. The structural bases and functional implications of this distinctive trait were essentially unknown. This study (1) uncovers the structural determinants of FMDV thermolability, (2) investigates the relationship between...

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Source

Identifiers

PMID: 25308865
DOI: 10.1016/j.str.2014.08.019

Provenance

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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