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Cysteine nitrosylation inactivates the HIV-1 protease
T Persichini1, M Colasanti, G M Lauro
1Department of Biology, University of Rome 'Roma Tre,&rsquo, Viale Marconi 446, I-00146, Rome, Italy.
Biochemical and Biophysical Research Communications
|October 24, 1998
Summary
Nitric oxide (NO) can inhibit HIV-1 protease activity by altering cysteine residues. This NO-mediated inactivation of HIV-1 protease may offer a new strategy for inhibiting viral replication.
Area of Science:
- Biochemistry
- Enzymology
- Virology
Background:
- Nitric oxide (NO) is known to modulate the activity of enzymes containing cysteine residues.
- The catalytic activity of HIV-1 protease is sensitive to the redox state of its regulatory cysteine residues (Cys67 and Cys95).
Purpose of the Study:
- To investigate the inhibitory effect of nitric oxide (NO) on the enzymatic activity of HIV-1 protease.
- To explore the potential mechanism of NO-mediated inhibition involving cysteine residues.
Main Methods:
- Utilized the NO-donor NOR-3 to release nitric oxide in the presence of HIV-1 protease.
- Assessed the impact of NO on the catalytic activity of purified HIV-1 protease.
Main Results:
- Nitric oxide (NO), delivered by NOR-3, demonstrated an inhibitory effect on HIV-1 protease activity.
- The findings suggest NO-mediated nitrosylation of cysteine residues leads to protease inactivation.
Conclusions:
- Nitric oxide (NO) can directly inhibit HIV-1 protease.
- NO-induced inactivation of HIV-1 protease through cysteine nitrosylation presents a potential therapeutic avenue for inhibiting HIV-1 replication.