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

被引：21

作者：

Almog, N

Roller, R

Arad, G

PassiEven, L

Wainberg, MA

Kotler, M

机构：

[1] HEBREW UNIV JERUSALEM, HADASSAH MED SCH, DEPT MOL GENET, IL-91010 JERUSALEM, ISRAEL

[2] MCGILL UNIV, JEWISH GEN HOSP, AIDS CTR, MONTREAL, PQ H3T 1E2, CANADA

来源：

JOURNAL OF VIROLOGY | 1996年 / 70卷 / 10期

关键词：

D O I：

10.1128/JVI.70.10.7228-7232.1996

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 fusionprotein undergoes autocleavage in vitro at at least three sites.

引用

收藏

页码：7228 / 7232

页数：5

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