literature

HIV mutation literature information.

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.

PMID: 23469241 2013 PloS one

Table: V32I

Extreme multidrug resistant HIV-1 protease with 20 mutations is resistant to novel protease inhibitors with P1'-pyrrolidinone or P2-tris-tetrahydrofuran.

PMID: 23590295 2013 Journal of medicinal chemistry

Introduction: Recently, we characterized a clinical

Result: Comparison with the PR/amprenavir structure reveals that mutations D30N, V32I, I47V and I84V in PR20 alter the size, shape and charge of the S2/S2' pocket in the PR20/amprenavir complex as described previously for the PR20/darunavir and PR20/saquinavir (3UFN) complexes.

Result: The wild type enzymes from HIV-1 and HIV-2 share 39-48% sequence identity; however, several of the mutations in PR20 exist in the wild type PR2 sequence including V32I and I47V in the S2/S2' subsites.

Trends in Genotypic HIV-1 Antiretroviral Resistance between 2006 and 2012 in South African Patients Receiving First- and Second-Line Antiretroviral Treatment Regimens.

PMID: 23840622 2013 PloS one

Method: The following protease mutations were considered LPV/r-resistance mutations: L10F, L24I, V32I, L33F, M46IL, I47A, I50V, I54MLV, L76V, V82ATSFMC, I84V, L89V, L90M.

Table: V32I

Persistence of HIV-1 transmitted drug resistance mutations.

PMID: 23904291 2013 The Journal of infectious diseases

Table: V32I

Simultaneous detection of major drug resistance mutations in the protease and reverse transcriptase genes for HIV-1 subtype C by use of a multiplex allele-specific assay.

PMID: 23985909 2013 Journal of clinical microbiology

Abstract: All the wild-type and mutant alleles were unequivocally distinguished with plasmid templates, and the limits of detection were 1.56% for K219Q and K219E, 3.13% for L76V, 6.25% for K65R, K70R, L74V, L100I, K103N, K103R, Q151M, Y181C, and I47V, and 12.5% for M41L, K101P, K101E, V106A, V106M, Y115F, M184V,

PMID: 21545648 2012 Fundamental & clinical pharmacology

Abstract: Darunavir GIQ is defined as the ratio between darunavir trough plasma concentration and the count of darunavir resistance-associated mutations (V11I, V32I, L33F, I47V, I50V, I54L/M, T74P, L76V, I84V, L89V) corrected or not corrected by the count of mutations with positive impact (V82A and E35D).

Interpretation of genotypic resistance to predict darunavir/ritonavir failure in antiretroviral experienced patients.

PMID: 22067663 2012 Journal of acquired immune deficiency syndromes (1999)

Abstract: Four mutations (V32I, I50V, L76V, I84V) were predictive of failure, the hazard ratio progressively increased by detecting 1 (hazard ratio: 2.0, 95% confidence interval: 1.3 to 3.0), 2 (3.6, 2.0 to 6.6), or 3 of them (9.7, 2.8 to 33.5).

Genotypic resistance profiles associated with virological failure to darunavir-containing regimens: a cross-sectional analysis.

PMID: 22237471 2012 Infection

Abstract: At DRV failure, the major increase was still observed for V32I; I54L, V11I, T74P and I50V also increased.

Abstract: DISCUSSION: The higher statistical difference at baseline between failing versus non-failing patients was observed for the V32I and I84V mutations.

Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors.

PMID: 22238126 2012 Protein science

Abstract: Furthermore, we analyzed the PR1 mutant (PR(1M) ) with substitutions V32I, I47V, and V82I that mimic the inhibitor binding site of PR2.

Energetic basis for drug resistance of HIV-1 protease mutants against amprenavir.

PMID: 22350569 2012 Journal of computer-aided molecular design

Abstract: Drug resistance arises from an increase in the energetic contribution from the van der Waals interactions between APV and PR (V32I, I50V, and I84V mutant) or a rise in the energetic contribution from the electrostatic interactions between the inhibitor and its target (I54M and I54V mutant).

Abstract: For the V32I mutant, also an increased free energy for the polar solvation contributes to the drug resistance.

Abstract: However, the affinities of the drug resistant protease variants V32I, I50V, I54V, I54M, I84V and

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