Myristylation of picornavirus capsid protein VP4 and its structural significance

Nature. 1987 Jun 11-17;327(6122):482-6. doi: 10.1038/327482a0.

Abstract

We have obtained evidence that poliovirus and other picornavirus particles are specifically modified by having myristic acid covalently bound to a capsid protein. The electron density map of poliovirus confirms the position of the myristate molecule and defines its location in the virus particle. Analogies with other myristylated proteins suggest that the myristate moiety in picornaviruses may be involved in capsid assembly or in the entry of virus into cells.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Capsid / genetics
  • Capsid / metabolism*
  • Models, Molecular
  • Molecular Conformation
  • Myristic Acid
  • Myristic Acids / metabolism*
  • Picornaviridae / genetics
  • Picornaviridae / metabolism*
  • Poliovirus / genetics
  • Poliovirus / metabolism
  • Poliovirus / ultrastructure
  • Protein Conformation
  • Protein Processing, Post-Translational*

Substances

  • Myristic Acids
  • Myristic Acid