Negatively charged amino acids at the foot-and-mouth disease virus capsid reduce the virion-destabilizing effect of viral RNA at acidic pH
EntityUAM. Departamento de Biología Molecular
PublisherNature Publishing Group
10.1038/s41598-020-58414-8Scientific Reports 2020.10 (2020): 1657
Funded byWork in F.S´s laboratory was funded by grants from MINECO-FEDER EU (AGL2017–84097-C2–1-R), Comunidad de Madrid co-fnanced with ECFEDER funds (P2018/BAA-4370). Work in M.G.M.´s laboratory was funded by grants from MINECO-FEDER EU (BIO2015–69928-R and RTI2018–096635-B-I00). Work by both groups was also funded by an institutional grant from Fundación Ramón Areces M.G.M. is an associate member of the Institute for Biocomputation and Physics of Complex Systems, Zaragoza, Spain
ProjectGobierno de España. AGL2017–84097-C2–1-R; Comunidad de Madrid. P2018/BAA-4370; Gobierno de España. BIO2015–69928-R; Gobierno de España. RTI2018–096635-B-I00
SubjectsBiotechnology; Microbiology; Structural biology; Física
Rights© 2020, The Author(s)
Esta obra está bajo una Licencia Creative Commons Atribución 4.0 Internacional.
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
Google Scholar:Caridi, Flavia - López-Argüello, Silvia - Rodríguez-Huete, Alicia - Torres, Elisa - Bustos, María J. - Cañas-Arranz, Rodrigo - Martín-Acebes, Miguel A. - Mateu, Mauricio G. - Sobrino, Francisco
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A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid resistance Martín-Acebes, Miguel A.; Vázquez-Calvo, Ángela; Rincón Forero, Verónica; Mateu, Mauricio G.; Sobrino, Francisco