RT Journal Article SR Electronic(1) A1 Marc, Daniel A1 Girard, Marc A1 Van Der Werf, SylvieYR 1991 T1 A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly JF Journal of General Virology, VO 72 IS 5 SP 1151 OP 1157 DO https://doi.org/10.1099/0022-1317-72-5-1151 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-72-5-1151