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

¹ Institute of Clinical Medicine, National Yang-Ming University, Taipei, Taiwan
² Institute of Public Health, National Yang-Ming University, Taipei, Taiwan
³ AIDS Prevention and Research Center, National Yang-Ming University, Taipei, Taiwan
⁴ Department of Internal Medicine, Division of Infectious Disease, Taipei Veterans General Hospital, 201 Section 2 Shih-Pai Road, Taipei 11217, Taiwan
⁵ Department of Medical Research and Education, Taipei Veterans General Hospital, 201 Section 2 Shih-Pai Road, Taipei 11217, Taiwan

Correspondence
Chin-Tien Wang
chintien{at}ym.edu.tw

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.

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				C. Ludwig, A. Leiherer, and R. Wagner Importance of Protease Cleavage Sites within and Flanking Human Immunodeficiency Virus Type 1 Transframe Protein p6* for Spatiotemporal Regulation of Protease Activation J. Virol., May 1, 2008; 82(9): 4573 - 4584. [Abstract] [Full Text] [PDF]