literature

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, L33F, K43T, F53L, Q58E, A71IL, G73STCA, T74P, N83D, and L89V) are assumed to have ancillary roles such as compensation for lower efficiency of proteolysis caused by major mutations; major resistance mutations (V32I, M46IL, I47VA, G48VM,

PMID: 34897227 2022 Journal of acquired immune deficiency syndromes (1999)

Table: V82A/F

Revealing the drug resistance mechanism of saquinavir due to G48V and V82F mutations in subtype CRF01_AE HIV-1 protease: molecular dynamics simulation and binding free energy calculations.

PMID: 34919029 2021 Journal of biomolecular structure & dynamics

Abstract: In this work, the resistance mechanism against SQV due to active site mutations G48V and V82F in CRF01_AE (AE) protease was explored.

Abstract: The V82F mutant structure also maintains similar intramolecular hydrogen bond interactions as observed in AE-WT.Communicated by Ramaswamy H.

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: 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.

Using Molecular Transmission Networks to Reveal the Epidemic of Pretreatment HIV-1 Drug Resistance in Guangxi, China.

PMID: 34567064 2021 Frontiers in genetics

Result: The largest PDR-related cluster within network contained DRM propagation of E138A, V82VF, V179D, V179VD, and V106I, while the remaining two PDR-related clusters are only involved in V106I propagation.

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).

HIV-1 acquired drug resistance to integrase inhibitors in a cohort of antiretroviral therapy multi-experienced Mexican patients failing to raltegravir: a cross-sectional study.

PMID: 32041622 2020 AIDS research and therapy

Table: V82F

Synthesis and biological evaluation of a series of 2-(((5-akly/aryl-1H-pyrazol-3-yl)methyl)thio)-5-alkyl-6-(cyclohexylmethyl)-pyrimi din-4(3H)-ones as potential HIV-1 inhibitors.

PMID: 32140396 2020 Acta pharmaceutica Sinica. B

Method: C8166 cells were infected with HIV-1A17, HIV-174V or HIV-1RF/V82F/184V, and PHA-stimulated PBMCs were incubated with HIV-1WAN or HIV-1TC-1 in RPMI-1640 at different serial dilutions of the compounds with a MOI of 0.1.

Method: In addition, wild-type strains HIV-1IIIB and HIV-1Ba-L, and HIV-1 resistant strains HIV-1A17, HIV-174V and HIV-1RF/V82F/184V were obtained from the NIH AIDS Research and Reference Reagent Program (Bethesda, Maryland, ME, USA).

Result: Based on the results of the first round of screening, we performed further antiviral activity evaluation of I-11 and I-12 as representative compounds and assessed the activity against different HIV-1 strains including wild-type strains (HIV-1IIIB and HIV-1Ba-L), resistant strains (HIV-1A17, HIV-174V and HIV-1RF/V82F/184V) and clini

High predictive efficacy of integrase strand transfer inhibitors in perinatally HIV-1-infected African children in therapeutic failure of first- and second-line antiretroviral drug regimens recommended by the WHO.

PMID: 30891603 2019 The Journal of antimicrobial chemotherapy

Result: DRMs to PIs corresponded mainly to natural polymorphism in the P gene while only the major DRMs V82A/F (n = 3; 20%) and L33F (n = 1, 6.7%) could be found.

Exploring the drug resistance mechanism of active site, non-active site mutations and their cooperative effects in CRF01_AE HIV-1 protease: molecular dynamics simulations and free energy calculations.

PMID: 30051758 2019 Journal of biomolecular structure & dynamics

Abstract: In this work, we have investigated the mechanism of resistance against indinavir (IDV) due to therapy selected active site mutation V82F, non-active site mutations PF82V and their cooperative effects PV82F in subtype AE-protease using molecular dynamics simulations and binding free energy calculations.

Abstract: Large positional deviation of IDV was observed in V82F complex.

Abstract: The simulations suggested all the three complexes lead to decrease in binding affinity of IDV, whereas the PF82V complex resulted in an enhanced binding affinity compared to V82F and PV82F complexes.

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