HIV mutation literature information.


  Detection of Gag C-terminal mutations among HIV-1 non-B subtypes in a subset of Cameroonian patients.
 PMID: 35082353       2022       Scientific reports
Introduction: Following the Stanford algorithm (mutation list), minor resistance mutations (L10F, V11I, K20TV, L23I, Result: In Class I, two mutations were positively correlated (phi > 0, p < 0.001) as pairs with protease major resistance mutations: L449F correlated with the major resistance mutations V32I (phi = 0.38, p = 0.008), I54V (phi = 0.27, p = 0.015) and L90M (phi = 0.32, p = 0.015); Y484P correlated with the major mutations I54V (phi = 0.33, p = 0.003) and V82A (phi = 0.26, p = 0.016).
Table: V32I


  HIV-1 drug resistance profiling using amino acid sequence space cartography.
 PMID: 35157024       2022       Bioinformatics (Oxford, England)
Abstract: V32I, L10F, and L33F in HIV protease) for the resistance development.


  Brief Report: Bictegravir/Emtricitabine/Tenofovir Alafenamide Efficacy in Participants With Preexisting Primary Integrase Inhibitor Resistance Through 48 Weeks of Phase 3 Clinical Trials.
 PMID: 34897227       2022       Journal of acquired immune deficiency syndromes (1999)
Table: V32I


  Analyses of HIV proteases variants at the threshold of viability reveals relationships between processing efficiency and fitness.
 PMID: 35299788       2021       Virus evolution
Abstract: We utilized a previous deep mutational scan of HIV-1 protease (PR) to identify variants with 15-45 per cent defects in replication and analysed the biochemical function of eight variants (L10M, L10S, V32C, V32I, A71V, A71S, Q92I, Q92N).
Result: 5A), while V32I,
Discussion: However, the magnitude of changes in activity were stronger for decreases (down to nearly undetectable levels for V32I cutting of MA-CA) compared to increases in activity (maximum of 2-fold relative to WT).


  Multiple Molecular Dynamics Simulations and Free-Energy Predictions Uncover the Susceptibility of Variants of HIV-1 Protease against Inhibitors Darunavir and KNI-1657.
 PMID: 34851643       2021       Langmuir
Abstract: Focused on the complexes of wild type (WT) PR and two mutant PRs (V32I/L33F/I54M/V82I and V32I/L33F/I54M/I84 V) with inhibitors Darunavir (DRV) and KNI-1657 (KNI), respectively, we have conducted research on the conformational dynamics and the resistance mechanism caused by residue mutations through multiple molecular dynamics (MD) simulations combined with an energy (MM-PBSA and solvated interaction energy (SIE)) prediction.


  Investigating potency of TMC-126 against wild-type and mutant variants of HIV-1 protease: a molecular dynamics and free energy study.
 PMID: 34787532       2021       SAR and QSAR in environmental research
Abstract: The potency of the inhibitor decreases in the order: wild type PR1 > M46L > MDR20 > I50V > PR2 > V32I > A28S.


  Prevalence and factors associated with HIV-1 drug resistance mutations in treatment-experienced patients in Nairobi, Kenya: A cross-sectional study.
 PMID: 34622871       2021       Medicine
Result: Lopinavir was the only PI class that demonstrated significant HIVDRM with mutations at V32I (2 patients), I47 V/A (2 patients), and V82A/F/T/S (3 patients).


  Acquired HIV-1 Protease Conformational Flexibility Associated with Lopinavir Failure May Shape the Outcome of Darunavir Therapy after Antiretroviral Therapy Switch.
 PMID: 33805099       2021       Biomolecules
Introduction: Research shows that the emergence of V32I, L33F, I47A, I50V, L76V, and 184V under drug pressure during LPV therapy may confer cross-resistance to DRV.
Introduction: The major HIV-1 PI resistance mutations that affect the efficacy of boosted LPV regimen are V32I, L33F, M46I/L, I47V/A, I50V, I54V/T/A/L/M, L76V, V82A/F/T/S, I84V.


  Virological response and resistance profile in highly treatment-experienced HIV-1-infected patients switching to dolutegravir plus boosted darunavir in clinical practice.
 PMID: 33480094       2021       HIV medicine
Abstract: Among 13 non-responding patients for whom a genotypic resistance test result at failure was available, only two (15.4%) accumulated further resistance in integrase (Y143C/H/R; S147G and N155H) and protease (V32I, L33F, I54L).


  HIV-1 reverse transcriptase and protease mutations for drug-resistance detection among treatment-experienced and naive HIV-infected individuals.
 PMID: 32119691       2020       PloS one
Table: V32I



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