Targeting of chrolamphenicol acetyltransferase to human immunodeficiency virus particles via Vpr and Vpx

Microbiol Immunol. 1995;39(12):1015-9. doi: 10.1111/j.1348-0421.1995.tb03293.x.

Abstract

Vpr and Vpx are the auxiliary proteins of human immunodeficiency viruses (HIVs) selectively incorporated into mature viral particles. We showed that the bacterial chloramphenicol acetyltransferase (CAT) fused to the N-terminus of HIV-1 Vpr, HIV-2 Vpr, or HIV-2 Vpx was incorporated into mature virions in a type-selective manner. By using chimeric proteins between HIV-1 Vpr and HIV-2 Vpx, we found that the N-terminal side of these proteins was mainly important for type-selective virion incorporation. The C-terminal arginine-rich region of HIV-1 Vpr was also found to transport CAT fusion proteins into virions but without any type selectivity. Furthermore, the corresponding regions of HIV-2 Vpr and HIV-2 Vpx had no such activity. This region of HIV-1 Vpr may interact nonspecifically with viral genomic RNA. Collectively, Vpr and Vpx may provide a means to introduce foreign proteins and other molecules into HIV virions for therapeutic purposes.

MeSH terms

  • Amino Acid Sequence
  • Chloramphenicol O-Acetyltransferase / genetics*
  • Cloning, Molecular
  • Gene Products, vpr / genetics
  • Gene Targeting / methods*
  • HIV-1 / genetics*
  • HIV-2 / genetics*
  • Molecular Sequence Data
  • Recombinant Fusion Proteins / genetics
  • Viral Regulatory and Accessory Proteins / genetics
  • vpr Gene Products, Human Immunodeficiency Virus

Substances

  • Gene Products, vpr
  • Recombinant Fusion Proteins
  • VPX protein, Human immunodeficiency virus 2
  • Viral Regulatory and Accessory Proteins
  • vpr Gene Products, Human Immunodeficiency Virus
  • Chloramphenicol O-Acetyltransferase