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. 1996 Oct;70(10):7228–7232. doi: 10.1128/jvi.70.10.7228-7232.1996

A p6Pol-protease fusion protein is present in mature particles of human immunodeficiency virus type 1.

N Almog 1, R Roller 1, G Arad 1, L Passi-Even 1, M A Wainberg 1, M Kotler 1
PMCID: PMC190778  PMID: 8794372

Abstract

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.

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Selected References

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