Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Adaptive value of foot-and-mouth disease virus capsid substitutions with opposite effects on particle acid stability.

Scientific reports - 6 Dec 2021

Caridi Flavia, Cañas-Arranz Rodrigo, Vázquez-Calvo Ángela, de León Patricia, Calderón Katherine I, Domingo Esteban, Sobrino Francisco, Martín-Acebes Miguel A

Abstract excerpt

Foot-and-mouth disease virus (FMDV) is a picornavirus that exhibits an extremely acid sensitive capsid. This acid lability is directly related to its mechanism of uncoating triggered by acidification inside cellular endosomes. Using a collection of FMDV mutants we have systematically analyzed the relationship between acid stability and the requirement for acidic endosomes using ammonium chloride (NH4Cl), an...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Capsid Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Line

Share to Cricetinae

Share to Endosomes

Share to Foot-and-Mouth Disease

Share to Foot-and-Mouth Disease Virus

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 34873184
DOI: 10.1038/s41598-021-02757-3
PMCID: PMC8648728

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Adaptive value of foot-and-mouth disease virus capsid substitutions with opposite effects on particle acid stability.PMID 34873184Read ↗

A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid lability and confer resistance to acid-dependent uncoating inhibition.Semantic proximity Read ↗

Role of a single amino acid substitution of VP3 H142D for increased acid resistance of foot-and-mouth disease virus serotype A.Semantic proximity Read ↗

Single amino acid substitution of VP1 N17D or VP2 H145Y confers acid-resistant phenotype of type Asia1 foot-and-mouth disease virus.Semantic proximity Read ↗

Equine Rhinitis A Virus Mutants with Altered Acid Resistance Unveil a Key Role of VP3 and Intrasubunit Interactions in the Control of the pH Stability of the Aphthovirus Capsid.Semantic proximity Read ↗

Chemical Evolution of Rhinovirus Identifies Capsid-Destabilizing Mutations Driving Low-pH-Independent Genome Uncoating.Semantic proximity Read ↗

Engineering viable foot-and-mouth disease viruses with increased acid stability facilitate the development of improved vaccines.Semantic proximity Read ↗

Establishment of persistent infection with foot-and-mouth disease virus in BHK-21 cellsSemantic proximity Read ↗

An increase in acid resistance of foot-and-mouth disease virus capsid is mediated by a tyrosine replacement of the VP2 histidine previously associated with VP0 cleavage.Semantic proximity Read ↗

A West Nile virus mutant with increased resistance to acid-induced inactivationSemantic proximity Read ↗

Targeted Modification of the Foot-And-Mouth Disease Virus Genome for Quick Cell Culture AdaptationSemantic proximity Read ↗

Deterministic, compensatory mutational events in the capsid of foot-and-mouth disease virus in response to the introduction of mutations found in viruses from persistent infections.Semantic proximity Read ↗

Involvement of a joker mutation in a polymerase-independent lethal mutagenesis escape mechanism.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.