Comparison of genotypic and virtual phenotypic drug resistance interpretations with laboratory-based phenotypes among CRF01_AE and subtype B HIV-infected individuals.
Result: Three subjects harboured major protease mutations (V32I, M46I, I47V, L90M), selected in prior failures.
Table: V32I
Structural studies of antiviral inhibitor with HIV-1 protease bearing drug resistant substitutions of V32I, I47V and V82I.
PMID: 25562662
2015
Journal of molecular graphics & modelling
Abstract: Although the second binding of TMC114 with flap does increase binding energy for the mutants (V32I-2T and M46L-2T), the considerable entropy loss results in the lower binding Gibbs free energies.
Abstract: For the single binding (1T) the less binding affinity can be attributed to the entropic loss for both V32I-1T and M46L-1T.
Abstract: However, for some mutants such as V32I and M46L the TMC114 can bind not only to the active cavity but also to the groove of the flexible flaps.
Abstract: MM-PBSA calculations explain the binding free energies unfavorable for the M46L and V32I mutants as compared to the WT.
Abstract: The conformational dynamics of HIV-1-pr
Structural studies of antiviral inhibitor with HIV-1 protease bearing drug resistant substitutions of V32I, I47V and V82I.
PMID: 26317593
2015
Journal of chemical information and modeling
Abstract: Drug resistance of mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 protease (PR) was found in clinical treatment of HIV patients with the drug amprenavir (APV).
Conformational variation of an extreme drug resistant mutant of HIV protease.
PMID: 26397743
2015
Journal of molecular graphics & modelling
Introduction: Recently; for example; the effects of single mutations V32I and M46L were studied by molecular dynamics in.
Method: Plasmid DNA encoding PR (subtype B of group M) with 20 mutations Q7K; L10F; I13V; I15V; D30N; V32I; L33F; E35D; M36I; S37N; I47V; I54L; Q58E; I62V; L63P; A71V; I84V; PMID: 29124158
2015
Biochemistry and biophysics reports
Introduction: L33F was initially identified as an accessory mutation to I54L/M, V32I+I47V, and I84V/I but is now recognized as a nonpolymorphic major drug resistance mutation.
Structural studies on molecular mechanisms of Nelfinavir resistance caused by non-active site mutation V77I in HIV-1 protease.
Introduction: The other mutations which were co-occurring with DBM and TPM included major mutations like- M46IL, I54MV, I84V, L90M, N88S, V32I, I47V, V82AS, D30N, G48V; and accompanied by minor mutations like- L10I, I13V, L63P, A71V, L89M, I93L, E35DN, I15V, D60E, L24I etc.
HIV-1 Drug Resistance Mutations: Potential Applications for Point-of-Care Genotypic Resistance Testing.
Result: The remaining 8% of viruses with predicted intermediate or high-level LPV resistance had a combination of two or more PI DRMs with lower mutation scores, including V32I, M46I, I54M/L/V, I47V, V82S/T/M and L90M.
Table: V32I
HIV Drug Resistance Surveillance in Honduras after a Decade of Widespread Antiretroviral Therapy.
Abstract: Notably, DRV failed to bind to mutant PR containing four amino acid substitutions (V32I, L33F, I54M, and I84V) that confer resistance to DRV on HIV-1.