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Capsid protein VP4 of poliovirus is N-myristoylated
A V Paul1, A Schultz, S E Pincus
1Department of Microbiology, School of Medicine, State University of New York at Stony Brook 11794.
Abstract:
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.
Insights
Poliovirus capsid protein VP4 is N-myristoylated, with myristic acid attaching to its N-terminal glycine. This lipid modification of poliovirus VP4 and its precursors may play a role in viral proliferation.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Poliovirus is an RNA virus that causes poliomyelitis.
- Viral capsid proteins play crucial roles in viral structure and replication.
- Post-translational modifications can significantly impact protein function.
Purpose of the Study:
- To investigate the nature of the N-terminal modification of poliovirus VP4.
- To determine if the modification involves lipid acylation.
- To explore the potential role of this modification in poliovirus proliferation.
Main Methods:
- In vivo labeling of poliovirus with [3H]myristic acid.
- Analysis of radiolabeled capsid polypeptides by copurification.
- Characterization of the N-terminal modification of VP4.
Main Results:
- [3H]myristic acid residues were found to copurify with poliovirus VP4.
- Evidence confirmed N-myristoylation of the N-terminal glycine residue of VP4.
- The N-terminal blocking group, identified as myristic acid, is present on VP4 and its precursors (VP0, P1).
Conclusions:
- Poliovirus VP4 undergoes N-myristoylation at its N-terminal glycine.
- This lipid modification is also present on VP4 precursor polypeptides.
- The functional significance of VP4 N-myristoylation in poliovirus proliferation warrants further investigation.