Covalent bonded Gag multimers in human immunodeficiency virus type-1 particles

Microbiol Immunol. 2009 Nov;53(11):609-20. doi: 10.1111/j.1348-0421.2009.00164.x.

Abstract

The oligomerization of HIV-1 Gag and Gag-Pol proteins, which are assembled at the plasma membrane, leads to viral budding. The budding generally places the viral components under non-reducing conditions. Here the effects of non-reducing conditions on Gag structures and viral RNA protection were examined. Using different reducing conditions and SDS-PAGE, it was shown that oligomerized Gag possesses intermolecular covalent bonds under non-reducing conditions. In addition, it was demonstrated that the mature viral core contains a large amount of covalent bonded Gag multimers, as does the immature core. Viral genomic RNA becomes sensitive to ribonuclease in reducing conditions. These results suggest that, under non-reducing conditions, covalent bonded Gag multimers are formed within the viral particles and play a role in protection of the viral genome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Electrophoresis, Polyacrylamide Gel
  • HIV-1 / chemistry*
  • HIV-1 / genetics
  • HIV-1 / physiology
  • Humans
  • Oxidation-Reduction
  • Protein Conformation
  • Protein Multimerization
  • RNA, Viral / chemistry
  • Ribonuclease, Pancreatic / metabolism
  • Virion / chemistry
  • Virion / genetics
  • Virus Replication
  • gag Gene Products, Human Immunodeficiency Virus / chemistry*
  • gag Gene Products, Human Immunodeficiency Virus / genetics

Substances

  • RNA, Viral
  • gag Gene Products, Human Immunodeficiency Virus
  • Ribonuclease, Pancreatic