Identifier to cite or link to this item: http://hdl.handle.net/20.500.13003/11842
Negatively charged amino acids at the foot-and-mouth disease virus capsid reduce the virion-destabilizing effect of viral RNA at acidic pH
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ISSN: 2045-2322
WOS ID: 000562807200005
Scopus EID: 2-s2.0-85078925705
PMID: 32015411
Embase PUI: L630814667
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2020-02-03Document type
research articleCitation
Caridi F, López Arguello SD, Rodriguez-Huete A, Torres E, Bustos MJ, Canas-Arranz R, et al. Negatively charged amino acids at the foot-and-mouth disease virus capsid reduce the virion-destabilizing effect of viral RNA at acidic pH. Sci Rep. 2020 Feb 03;10(1):1657.Abstract
Elucidation of the molecular basis of the stability of foot-and-mouth disease virus (FMDV) particles is relevant to understand key aspects of the virus cycle. Residue N17D in VP1, located at the capsid inner surface, modulates the resistance of FMDV virion to dissociation and inactivation at acidic pH. Here we have studied whether the virion-stabilizing effect of amino acid substitution VP1 N17D may be mediated by the alteration of electrostatic charge at this position and/or the presence of the viral RNA. Substitutions that either introduced a positive charge (R,K) or preserved neutrality (A) at position VP1 17 led to increased sensitivity of virions to inactivation at acidic pH, while replacement by negatively charged residues (D,E) increased the resistance of virions to acidic pH. The role in virion stability of viral RNA was addressed using FMDV empty capsids that have a virtually unchanged structure compared to the capsid in the RNA-filled virion, but that are considerably more resistant to acidic pH than WT virions, supporting a virion-destabilizing effect of the RNA. Remarkably, no differences were observed in the resistance to dissociation at acidic pH between the WT empty capsids and those harboring replacement N17D. Thus, the virion-destabilizing effect of viral RNA at acidic pH can be partially restored by introducing negatively charged residues at position VP1 N17.
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https://dx.doi.org/10.1038/s41598-020-58414-8MeSH
Mutagenesis, Site-DirectedFoot-and-Mouth Disease Virus
Capsid
Cell Line
Amino Acids
Hydrogen-Ion Concentration
RNA Stability
Static Electricity
Animals
Amino Acid Substitution
Capsid Proteins
Virion
RNA, Viral
DeCS
Sustitución de AminoácidosVirión
Animales
Estabilidad del ARN
Línea Celular
Virus de la Fiebre Aftosa
Concentración de Iones de Hidrógeno
Cápside
Aminoácidos
ARN Viral
Proteínas de la Cápside
Electricidad Estática
Mutagénesis Sitio-Dirigida