A p6Pol-protease fusion protein is present in mature particles of human immunodeficiency virus type 1.
Human immunodeficiency virus type 1 (HIV-1) protease (PR) and p6(Pol) are translated as part of the Gag-Pol polyprotein after a ribosomal frameshift. PR is essential to virus replication and is responsible for cleaving Gag and Gag-Pol precursors, but the role of p6(Pol) in HIV-1 infection is poorly understood. Here, we report that (i) PR is present in mature HIV-1 virions primarily as a p6(Pol)-PR fusion protein; (ii) HIV-1 PR cleaves viral precursor proteins expressed in bacterial cells at the Phe-Leu bond (positions 1639 to 1642) located at the junction of the NC and p6(Pol) proteins, releasing the p6(Pol)-PR fusion protein; and (iii) purified p6(Pol)-PR fusion protein undergoes autocleavage in vitro at at least three sites.
Almog
N
N
Department of Molecular Genetics, The Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Roller
R
R
Arad
G
G
Passi-Even
L
L
Wainberg
M A
MA
Kotler
M
M
D000595:Amino Acid Sequence; D015685:Fusion Proteins, gag-pol; D015497:HIV-1 / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D014760:Viral Fusion Proteins; D014771:Virion
D015685:Fusion Proteins, gag-pol; D014760:Viral Fusion Proteins