Marc D, Girard M, van der Werf S
Unité de Virologie Moléculaire (CNRS UA 545), Institut Pasteur, Paris, France.
J Gen Virol. 1991 May;72 ( Pt 5):1151-7. doi: 10.1099/0022-1317-72-5-1151.
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.
脊髓灰质炎病毒的衣壳蛋白VP4通过酰胺键与N端甘氨酸残基酰化豆蔻酸。我们之前的研究表明，豆蔻酸在脊髓灰质炎病毒组装和感染早期事件中起作用。为了更好地理解其在组装过程中的作用，我们在VP4的豆蔻酰化信号序列中引入了甘氨酸1到丙氨酸的氨基酸替换。这种替换在体内阻止了VP0的豆蔻酰化，并消除了携带该突变的基因组转录本的感染性。这些突变的RNA仍然能够在转染细胞中复制，但组装过程效率低下，未检测到成熟病毒颗粒。
