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A slender tract of glycine residues is required for translocation of the VP2 protein N-terminal domain through the parvovirus MVM capsid channel to initiate infection

AutorCastellanos, Milagros; Pérez, Rebeca ; Rodríguez-Huete, Alicia ; Grueso, Esther; Almendral, José M. ; Mateu, Mauricio G.
Palabras claveConformational dynamics
Virus entry and infection
Peptide translocation
Structure–function relationship
Macromolecular assembly
Fecha de publicación2013
EditorPortland Press
CitaciónBiochemical Journal 455: 87- 94 (2013)
ResumenViruses constitute paradigms to study conformational dynamics in biomacromolecular assemblies. Infection by the parvovirusMVM (minute virus of mice) requires a conformational rearrangement that involves the intracellular externalization through capsid channels of the 2Nt (N-terminal region of VP2).We have investigated the role in this process of conserved glycine residues in an extended glycine-rich tract located immediately after 2Nt. Based on the virus structure, residues with hydrophobic side chains of increasing volume were substituted for glycine residues 31 or 33. Mutations had no effect on capsid assembly or stability, but inhibited virus infectivity. All mutations, except those to alanine residues which had minor effects, impaired 2Nt externalization in nuclear maturing virions and in purified virions, to an extent that correlated with the side chain size. Different biochemical and biophysical analyses were consistent with this result. Importantly, all of the tested glycine residue replacements impaired the capacity of the virion to initiate infection, at ratios correlatingwith their restrictive effects on 2Nt externalization. Thus small residues within the evolutionarily conserved glycine-rich tract facilitate 2Nt externalization through the capsid channel, as required by this virus to initiate cell entry. The results demonstrate the exquisite dependence on geometric constraints of a biologically relevant translocation event in a biomolecular complex. © 2013 The Author(s).
URIhttp://hdl.handle.net/10261/95523
DOI10.1042/BJ20130503
Identificadoresdoi: 10.1042/BJ20130503
issn: 0264-6021
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