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Targeting of Chrolamphenicol Acetyltransferase to Human Immunodeficiency Virus Particles via Vpr and Vpx
Author(s) -
Sato Akihiko,
Isaka Yoshitaka,
Kodama Makoto,
Yoshimoto Jun,
Kawauchi Shinobu,
Kuwata Takeo,
Adachi Akio,
Hayami Masanori,
Yoshie Osamu,
Fujiwara Tamio
Publication year - 1995
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1995.tb03293.x
Subject(s) - chloramphenicol acetyltransferase , biology , virology , acetyltransferase , fusion protein , human immunodeficiency virus (hiv) , rna , microbiology and biotechnology , gene , biochemistry , acetylation , gene expression , reporter gene , recombinant dna
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.