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

Research paper by Hsu-Chen HC Chiu, Fu-Der FD Wang, Yi-Ming Arthur YM Chen, Chin-Tien CT Wang

Indexed on: 09 Jun '06Published on: 09 Jun '06Published in: The Journal of general virology


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 p6(gag) 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.