A p6(Pol)-protease fusion protein is present in mature particles of human immunodeficiency virus type 1

Nava Almog; Ruth Roller; Gila Arad; Lea Passi-Even; Mark A. Wainberg; Moshe Kotler

doi:10.1128/jvi.70.10.7228-7232.1996

A p6(Pol)-protease fusion protein is present in mature particles of human immunodeficiency virus type 1

Nava Almog, Ruth Roller, Gila Arad, Lea Passi-Even, Mark A. Wainberg, Moshe Kotler^*

^*Corresponding author for this work

Institute for Medical Research Israel-Canada (IMRIC)

Research output: Contribution to journal › Article › peer-review

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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 least three sites.

Original language	English
Pages (from-to)	7228-7232
Number of pages	5
Journal	Journal of Virology
Volume	70
Issue number	10
DOIs	https://doi.org/10.1128/jvi.70.10.7228-7232.1996
State	Published - Oct 1996

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10.1128/jvi.70.10.7228-7232.1996

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title = "A p6(Pol)-protease fusion protein is present in mature particles of human immunodeficiency virus type 1",

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 least three sites.",

author = "Nava Almog and Ruth Roller and Gila Arad and Lea Passi-Even and Wainberg, {Mark A.} and Moshe Kotler",

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T1 - A p6(Pol)-protease fusion protein is present in mature particles of human immunodeficiency virus type 1

AU - Almog, Nava

AU - Roller, Ruth

AU - Arad, Gila

AU - Passi-Even, Lea

AU - Wainberg, Mark A.

AU - Kotler, Moshe

PY - 1996/10

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N2 - 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 least three sites.

AB - 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 least three sites.

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A p6(Pol)-protease fusion protein is present in mature particles of human immunodeficiency virus type 1

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