Method: The HIV-1 PR and mutants were constructed with five mutations Q7K, L33I, L63I, C67A, and C95A to prevent cysteine-thiol oxidation and diminish autoproteolysis.
Antiretroviral drug susceptibility among drug-naive adults with recent HIV infection in Rakai, Uganda.
Fluctuating partially native-like topologies in the acid denatured ensemble of autolysis resistant HIV-1 protease.
PMID: 19100236
2009
Archives of biochemistry and biophysics
Abstract: We report here NMR characterization of the acid-denatured state of a mutant of HIV-1 protease, designed to prevent autolysis (Q7K, L33I, L63I) and to prevent cysteine oxidation (C67A and C95A).
Solution kinetics measurements suggest HIV-1 protease has two binding sites for darunavir and amprenavir.
PMID: 18808097
2008
Journal of medicinal chemistry
Table: L33I
Pattern and impact of emerging resistance mutations in treatment experienced patients failing darunavir-containing regimen.
Abstract: Emergence of DRV-associated-resistance mutations was observed in 72% (18/25) of patients, at codons L89I/M/V (32%), V32I (28%), V11I (20%), I47V/A (20%), I54L/M (20%), L33F/I (16%) and I50V (16%).
Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir.
Method: The optimized HIV-1 PR clone with mutations Q7K, L33I, and L63I to diminish the autoproteolysis of the PR, as well as mutations C67A and C95A to prevent cysteine-thiol oxidation was used as the initial template for adding drug resistant mutations.
Result: The wild type HIV-1 PR in these studies contains mutations Q7K, L33I, and L63I to diminish autoproteolysis and C67A and C95A to prevent cysteine-thiol oxidation, and showed almost identical kinetic parameters, stability and dimer dissociation as the unmutated wild type
Virological response to darunavir/ritonavir-based regimens in antiretroviral-experienced patients (PREDIZISTA study).
Abstract: We determined the genotypic score I13V+V32I+L33F/I/V+E35D+ M361/L/V+I47V+F53L+I62V.
Genotypic resistance profile and clinical progression of treatment-experienced HIV type 1-infected patients with virological failure.
PMID: 18240962
2008
AIDS research and human retroviruses
Abstract: In multivariable models adjusting for prior AIDS, baseline CD4 counts, HIV-1 RNA, and calendar year, viral resistance variables associated with increased hazards of clinical progression were the presence of reverse transcriptase substitution T215F (p = 0.002) and the presence of three or more protease substitutions among L33F/I/V, V82A/F/L/T, I84V, and L90M (p = 0.003).
Unique thermodynamic response of tipranavir to human immunodeficiency virus type 1 protease drug resistance mutations.
Abstract: Characterization of tipranavir binding to wild-type protease, active site mutants I50V and V82F/I84V, the multidrug-resistant mutant L10I/L33I/M46I/I54V/L63I/V82A/I84V/L90M, and the tipranavir in vitro-selected mutant I13V/V32L/L33F/K45I/V82L/I84V was performed by isothermal titration calorimetry and crystallography.
Food and Drug Administration analysis of tipranavir clinical resistance in HIV-1-infected treatment-experienced patients.
Abstract: The most common protease mutations that developed in tipranavir-treated individuals who experienced virologic failure were L10I/V/S, I13V, L33V/I/F, M36V/I/L V82T, V82L, and I84V.
HIV mutation literature information.
PMID: 
2010
The FEBS journal
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