Capsid protein VP4 of poliovirus is N-myristoylated.
AUTOR(ES)
Paul, A V
RESUMO
Poliovirus was labeled in vivo with [3H]myristic acid. Analysis of the capsid polypeptides revealed that the [3H]myristic acid residues copurified with VP4, the smallest and internal capsid protein of the virion. Evidence is presented showing unambiguously that the N-terminal glycine residue of VP4 is N-myristoylated. A previous analysis of the tryptic peptides of VP4 [Dorner, A. J., Dorner, L. F., Larsen, G. R., Wimmer, E. & Anderson, C. W. (1982) J. Virol. 42, 1017-1028] had shown that the N-terminal blocking group exists on all VP4 molecules as well as on VP0 and P1, two precursor polypeptides to VP4 in poliovirus. The possible function of the myristic acid residue in VP4 and in its precursor in poliovirus proliferation is discussed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=299409Documentos Relacionados
- Role of myristoylation of poliovirus capsid protein VP4 as determined by site-directed mutagenesis of its N-terminal sequence.
- Expression of the OSU rotavirus outer capsid protein VP4 by an adenovirus recombinant.
- Membrane interaction of small N-myristoylated peptides: implications for membrane anchoring and protein-protein association.
- Poliovirus Mutants at Histidine 195 of VP2 Do Not Cleave VP0 into VP2 and VP4
- The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant.