Abstract
The human immunodeficiency virus type-1 (HIV-1) transframe protein p6* is located between the structural and enzymatic domains of the Gag-Pol polyprotein, flanked by the nucleocapsid (NC) and the protease (PR) domain at its amino and carboxyl termini, respectively. Here, we report that recombinant highly purified HIV-1 p6* specifically inhibits mature HIV-1 PR activity. Kinetic analyses and cross-linking experiments revealed a competitive mechanism for PR inhibition by p6*. We further demonstrate that the four carboxyl-terminal residues of p6* are essential but not sufficient for p6*-mediated inhibition of PR activity. Based on these results, we suggest a role of the transframe protein p6* in regulating HIV-1 PR activity during viral replication.
| Original language | English |
|---|---|
| Pages (from-to) | 21539-43 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 274 |
| Issue number | 31 |
| Publication status | Published - 30 Jul 1999 |
Keywords
- Amino Acid Sequence
- Binding, Competitive
- Cross-Linking Reagents
- Fusion Proteins, gag-pol
- Gene Products, gag
- HIV Protease
- HIV Protease Inhibitors
- Humans
- Kinetics
- Models, Chemical
- Mutagenesis, Site-Directed
- Recombinant Proteins
- gag Gene Products, Human Immunodeficiency Virus
- Journal Article
- Research Support, Non-U.S. Gov't
