Targeting of Chrolamphenicol Acetyltransferase to Human Immunodeficiency Virus Particles via Vpr and Vpx

Access this Article

Search this Article

Author(s)

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.

Journal

  • MICROBIOLOGY and IMMUNOLOGY

    MICROBIOLOGY and IMMUNOLOGY 39(12), 1015-1019, 1995-12-20

    Center For Academic Publications Japan

References:  29

Codes

  • NII Article ID (NAID)
    10005870543
  • NII NACSIS-CAT ID (NCID)
    AA00738350
  • Text Lang
    ENG
  • Article Type
    NOT
  • ISSN
    03855600
  • Data Source
    CJP  J-STAGE 
Page Top