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J Gen Virol 72 (1991), 1151-1157; DOI 10.1099/0022-1317-72-5-1151
© 1991 Society for General Microbiology
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A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly

Daniel Marc, Marc Girard and Sylvie van der Werf

Unité de Virologie Moléculaire (CNRS UA 545), Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France

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.

Received 3 December 1990; accepted 8 February 1991.


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Copyright © 1991 by the Society for General Microbiology.