Effect of human immunodeficiency virus type 1 transframe protein p6* mutations on viral protease-mediated Gag processing

Hsu Chen Chiu, Fu Der Wang, Yi Ming Arthur Chen, Chin Tien Wang

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The proteolytic processing of human immunodeficiency virus (HIV) particles mediated by the viral pol-encoded protease (PR) is essential for viral infectivity. The pol coding sequence partially overlaps with the gag coding sequence and is translated as a Gag-Pol polyprotein precursor. Within Gag-Pol, the C-terminal p6gag domain is replaced by a transframe peptide referred to as p6*, which separates the Gag nucleocapsid domain from PR. Several previous in vitro studies have ascribed a PR-suppression regulatory function to p6*. Here, it was demonstrated that an HIV-1 Gag-Pol lacking p6* is efficiently incorporated into virions when coexpressed with HIV-1 Gag precursor. However, the released virions are not processed appropriately and show a greatly reduced viral infectivity. This suggests that the p6* is indispensable during the process of PR-mediated virus particle maturation.

Original languageEnglish
Pages (from-to)2041-2046
Number of pages6
JournalJournal of General Virology
Volume87
Issue number7
DOIs
Publication statusPublished - Jul 1 2006
Externally publishedYes

Fingerprint

Virion
HIV-1
Peptide Hydrolases
Mutation
Proteins
pol Gene Products
gag Gene Products
Nucleocapsid
HIV
Peptides

ASJC Scopus subject areas

  • Virology

Cite this

Effect of human immunodeficiency virus type 1 transframe protein p6* mutations on viral protease-mediated Gag processing. / Chiu, Hsu Chen; Wang, Fu Der; Chen, Yi Ming Arthur; Wang, Chin Tien.

In: Journal of General Virology, Vol. 87, No. 7, 01.07.2006, p. 2041-2046.

Research output: Contribution to journalArticle

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