Result: Both isolates presented the M46L mutation-conferring intermediate-level resistance to nelfinavir and potential low-level resistance to lopinavir and atazanavir-alone in the subtype C strain and along with multiple other resistance mutations, such as L24I, I47V, F53L, I54V, and V82A in the F1 strain.
Restriction fragment mass polymorphism (RFMP) analysis based on MALDI-TOF mass spectrometry for detecting antiretroviral resistance in HIV-1 infected patients.
PMID: 23480551
2013
Clinical microbiology and infection
Abstract: The concordance rates between the RFMP and direct sequencing assays for the examined codons were 97% (K65R), 97% (T69Ins/D), 97% (L74VI), 97% (K103N), 96% (V106AM), 97% (Q151M), 97% (Y181C), 97% (M184VI) and 94% (T215YF) in the reverse transcriptase coding region, and 100% (D30N), 100% (M46I), 100% (G48V), 100% (I50V), 100% (I54LS), 99% (V82A), 99% (I84V) and 100% (L90M) in th
Transmission patterns of HIV-subtypes A/AE versus B: inferring risk-behavior trends and treatment-efficacy limitations from viral genotypic data obtained prior to and during antiretroviral therapy.
Method: The I54V and V82A PR-mutant HIV clone has been described earlier.
Method: The transduced Jurkat E6-1 cells were inoculated at a MOI of 0.05 with WT HIV and CA-mutant HIV, and the PR-mutant HIV PRI54V+V82A served as a positive control for rescue of reduced infectivity of the mutant viruses.
Result: In parallel, we included the PR-mutant PRI54V+V82A HIV as a positive control to validate the rescue by overexpression of HSP90AB1.
Novel P2 tris-tetrahydrofuran group in antiviral compound 1 (GRL-0519) fills the S2 binding pocket of selected mutants of HIV-1 protease.
PMID: 23298236
2013
Journal of medicinal chemistry
Introduction: In order to study the molecular basis for the potency of inhibitor 1 against drug resistant viral strains, crystal structures of inhibitor 1 complexes with PR mutants bearing single substitutions of R8Q, D30N, I50V, I54M and V82A (PRR8Q, PRD30N, PRI50V, PRI54M and PRV82A) were analyzed.
Introduction: The mutation V82A in the active site cavity can eliminate interactions with inhibitor, and also exhibits a shift of its main chain atoms to adapt to inhibitor.
Method: Mutants (R8Q, D30N,
Antiviral resistance and correlates of virologic failure in the first cohort of HIV-infected children gaining access to structured antiretroviral therapy in Lima, Peru: a cross-sectional analysis.
Method: The OLA was conducted according to the NIH protocol for mutations at HIV-1B protease positions D30N, I50V, V82A, V82S, V82T, I84V, N88D, and L90M as well as reverse transcriptase positions K103N, Y181C, K65R, T215F, T215Y, M184V, and Q151M.
Significantly improved HIV inhibitor efficacy prediction employing proteochemometric models generated from antivirogram data.
5Result: Significant differences in the prevalence of PI RAMs detected with the L76V between subtype B and ""non-B"" samples were found at 4 positions with a higher prevalence of the V32I, M46I/L, V82A/F/L/T/S and L90M mutations in subtype B than in ""non-B"" samples: 10 vs 0%, P = 0.04; 92 vs 82%, P = 0.036; 52 vs 26%, P = 0.0011; and 42 vs 18%, P = 0.002, respectively."
5Result: Then, the most prevalent mutation found with L76V was the V82A/F/L/T/S (52%) in subtype B samples and I84V (36%) in ""non-B"" samples."
Result: This cluster was linked to L24I, I54V, and
Cooperative effects of drug-resistance mutations in the flap region of HIV-1 protease.
Introduction: Besides G48V or I54V, Flap+(I54V) has an additional active site mutation V82A, as does Flap+(I54A).
Introduction: Both G48V and V82A are associated with SQV resistance.
Introduction: Flap+(I54V) is a drug resistant protease variant containing a combination of active site and flap mutations (L10I/G48V/I54V/V82A) (Figure 1) that often occur together in treated patients.
Introduction: Hence, the combination of mutations in the variants studied here, Flap+(I54V) and Flap+(
ViMRT
HIV mutation literature information.
PMID: 
2014
Journal of the International AIDS Society
