A Comparative Insight into Amprenavir Resistance of Mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 Protease Based on Thermodynamic Integration and MM-PBSA Methods.
Abstract: Q calibrators showed the PI resistance mutation I50V when directly amplified and sequenced from the 423-bp PCR product targeting protease gene.
Abstract: The I50V protease inhibitor (PI) resistance mutation was found in 87.4% of protease gene fragments sequenced from 199 nucleic acid isolates extracted using an NASBA virus load assay, performed between 1997 and 2001 in Brazil.
Abstract: The majority of the patients' samples had a mixture of I50I and I50V; however, this artifact was nor seen when a 989-bp PCR product was used.
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%).
Structural and kinetic analysis of pyrrolidine-based inhibitors of the drug-resistant Ile84Val mutant of HIV-1 protease.
Abstract: Although the Ile50Val mutation leads to a significant decrease in affinity for all compounds in this series, they retain or even show increased affinity towards the important Ile84Val mutation.
Abstract: Herein, we report the influence of the active-site mutations Ile50Val and Ile84Val on these inhibitors by structural and kinetic analysis.
Combating HIV resistance - focus on darunavir.
PMID: 19209258
2008
Therapeutics and clinical risk management
Abstract: Darunavir resistance-associated mutations have been defined as V11I, V32I, L33F, I47V, I50V, I54L/M, G73S, L76V, I84V, and L89V.
Natural polymorphisms in the human immunodeficiency virus type 2 protease can accelerate time to development of resistance to protease inhibitors.
PMID: 17116674
2007
Antimicrobial agents and chemotherapy
Abstract: After 25 weeks, other cultures had developed I50V and I84V mutations.
A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism.
Discussion: Changes at the p1/p6 cleavage site (L449F or P453L), which on their own do not confer resistance, were associated with reduced sensitivity in the background of the I50V in protease.
Genotypic resistance in plasma and peripheral blood lymphocytes in a group of naive HIV-1 patients.
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.
HIV-1 subtype B protease and reverse transcriptase amino acid covariation.
Figure: Includes the 22 mutations obtained from the mutation pairs with the highest positive association (Table 1) in bold, and 13 additional clinically relevant protease inhibitor resistance mutations (L10F, V32I, L33F, I47V, I50V/L, F53L, I54L/M, Q58E, L76V, V82T, and N88S).
Discussion: Protease covariation was dominated by the clustering of nelfinavir-associated mutations (D30N and N88D), two main groups of PI-resistance mutations
Key amprenavir resistance mutations counteract dramatic efficacy of darunavir in highly experienced patients.
Abstract: Patients harbouring viruses with amprenavir-specific resistance profiles, such as I50V or V32I + I47V, failed on a darunavir/ritonavir-containing regimen.
HIV mutation literature information.
PMID: 
2008
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