Article
Myristoylation is important at multiple stages in poliovirus assembly.
Journal of virology - 1 May 1991
Moscufo N, Simons J, Chow M
Abstract excerpt
The N-terminal glycine of the VP4 capsid subunit of poliovirus is covalently modified with myristic acid (C14 saturated fatty acid). To investigate the function of VP4 myristoylation in poliovirus replication, amino acid substitutions were placed within the myristoylation consensus sequence at the alanine residue (4003A) adjacent to the N-terminal glycine by using site-directed mutagenesis methods. Mutants which...
Topics
- Amino Acid Sequence
- Base Sequence
- DNA, Viral
- HeLa Cells
- Humans
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Myristic Acids
- Phenotype
- Plasmids
- Poliovirus
- Virus Replication
