Cysteine nitrosylation inactivates the HIV-1 protease |
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Authors: | T Persichini M Colasanti GM Lauro P Ascenzi |
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Affiliation: | Department of Biology, University of Rome 'Roma Tre,&rsquo, Viale Marconi 446, I-00146, Rome, Italy. |
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Abstract: | Nitric oxide (NO) may modulate the catalytic activity of cysteine-containing enzymes. HIV-1 protease action is modulated by the redox equilibrium of Cys67 and Cys95 regulatory residues. In the present study, the inhibitory effect of NO, released by the NO-donor (+/-)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (NOR-3), on the aspartyl HIV-1 protease action is reported. HIV-1 protease inactivation via NO-mediated nitrosylation of Cys regulatory residue(s) may represent a possible mechanism for inhibition of HIV-1 replication. |
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