Myristoylation-enhanced binding of the HIV-1 Nef protein to T cell skeletal matrix

Virology. 1993 Nov;197(1):420-5. doi: 10.1006/viro.1993.1605.

Abstract

The negative factor, Nef, of HIV-1 was found to associate to an extent of 16-42% with the detergent insoluble cytoskeletal fraction of T lymphocytes. Furthermore, Escherichia coli expressed Nef protein was found to bind during in vitro reactions with the cytoskeletal matrix to an extent of 30-50%. Cytoskeletal association of Nef was significantly enhanced by myristoylation. The specificity of the myristoylation-enhanced binding was demonstrated by the lack of an effect of myristoylation on binding of the HIV-1 Gag protein to the cytoskeleton. Cytoskeletal binding was saturable, and inhibited by high concentrations of sodium chloride, or with SDS or urea. Binding of Nef to the cytoskeletal matrix may be important in mediating its effects on HIV-1 replication.

Publication types

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

MeSH terms

  • Cloning, Molecular
  • Cytoskeleton / metabolism*
  • Escherichia coli
  • Gene Products, gag / metabolism
  • Gene Products, nef / biosynthesis
  • Gene Products, nef / metabolism*
  • Genes, nef
  • HIV-1 / genetics
  • HIV-1 / metabolism*
  • Human T-lymphotropic virus 1 / genetics
  • Humans
  • Kinetics
  • Myristic Acid
  • Myristic Acids / metabolism*
  • Promoter Regions, Genetic
  • Protein Processing, Post-Translational*
  • Recombinant Proteins / metabolism
  • T-Lymphocytes / metabolism*
  • Transfection
  • Tumor Cells, Cultured
  • nef Gene Products, Human Immunodeficiency Virus

Substances

  • Gene Products, gag
  • Gene Products, nef
  • Myristic Acids
  • Recombinant Proteins
  • nef Gene Products, Human Immunodeficiency Virus
  • Myristic Acid