A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Accéder directement au contenu
Article Dans Une Revue Journal of General Virology Année : 1991

A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly

Daniel Marc
Sylvie van Der Werf

Résumé

Capsid protein VP4 of poliovirus is acylated with myristic acid via an amide linkage to its N-terminal glycine residue. Our previous studies suggested that myristic acid plays a role in poliovirus assembly and in the early events of infection. In order to understand better its role in the assembly process, we introduced a Gly1 to Ala amino acid substitution in the myristoylation signal sequence of VP4. This substitution prevented VP0 myristoylation in vivo and abolished the infectivity of genomic transcripts harbouring the mutation. These mutated RNAs were still able to replicate in the transfected cells but the assembly processes were inefficient and no mature virions could be detected.

Dates et versions

hal-02715046 , version 1 (01-06-2020)

Identifiants

Citer

Daniel Marc, Marc Girard, Sylvie van Der Werf. A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly. Journal of General Virology, 1991, 72 (5), pp.1151-1157. ⟨10.1099/0022-1317-72-5-1151⟩. ⟨hal-02715046⟩

Collections

PASTEUR INRAE
7 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More