literature

HIV mutation literature information.

Natural polymorphisms and unusual mutations in HIV-1 protease with potential antiretroviral resistance: a bioinformatic analysis.

PMID: 24629078 2014 BMC bioinformatics

Result: We modelled the proteins with unusual mutations (L5F, D29V, L63G, L63R, P79L and T91V), natural polymorphisms (L63H andL63S), and drug-resistant mutant PRs with single mutations or patterns of mutations (D30N, V32I, M36I, M46I, I47V, G48V, I50V, I50L, I54M, Q58E, T74P,

Table: V32I

Structures of darunavir-resistant HIV-1 protease mutant reveal atypical binding of darunavir to wide open flaps.

PMID: 24738918 2014 ACS chemical biology

Method: The PRP51 construct contains 14 mutations (L10I, I15V, K20R, L24I, V32I, L33F, M36I, M46L, I54M, L63P, K70Q, V82I, I84V, and L89M) plus three other mutations Q7K to minimize autoproteolysis and C67A and C95A to prevent cysteine-induced aggregation.

Result: Four mutations associated with drug resistance, V32I,

PMID: 25092296 2014 Proc Natl Acad Sci U S A

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.

A uniquely prevalent nonnucleoside reverse transcriptase inhibitor resistance mutation in Russian subtype A HIV-1 viruses.

PMID: 25259833 2014 AIDS (London, England)

Result: Of the 243 patients who received one or more protease inhibitors, 32 (13%) had a study-defined protease inhibitor-resistance mutation most commonly L10F, K20T, V32I, L33F, M46I/L, I47V/A, I50L, F53L, I54V/L, Q58E, L76V, V82A/C, I84V, L89V, and L90M.

Cobicistat-boosted darunavir in HIV-1-infected adults: week 48 results of a Phase IIIb, open-label single-arm trial.

PMID: 25926858 2014 AIDS research and therapy

Method: Patients were required to have plasma VL >=1000 HIV-1 RNA copies/ml (Amplicor HIV-1 Monitor Test, version 1.5, Roche Diagnostics, Basel, Switzerland) at screening, eGFRCG >=80 ml/min, genotypic sensitivity to the two investigator-selected N[t]RTIs (GenoSure MG assay, Monogram Biosciences, South San Francisco, CA, USA), and none of the following darunavir RAMs: V11I, V32I, L33F, I47V, I50V, I54M, I54L, T74P, L76V, I84V or L89V.

2014 Update of the drug resistance mutations in HIV-1.

PMID: 25101529 2014 Topics in antiviral medicine

Discussion: However, there is emerging evidence that specific mutations, most notably I47A (and possibly I47V) and V32I, are associated with high-level resistance.

Revealing origin of decrease in potency of darunavir and amprenavir against HIV-2 relative to HIV-1 protease by molecular dynamics simulations.

PMID: 25362963 2014 Scientific reports

Result: As shown from Figure 7B, the residues involving the increase of the van der Waals interaction in PR2 are V32I, V82I, D29', D30' and I84' compared to PR1.

Result: As shown in Figure 7A, the van der Waals interactions of the mutated residues V32I, I47V, V32'I and I47'V in PR2 with DRV are decreased by 0.49, 0.86, 0.69 and 0.26 kcal mol-1 compared to PR1, respectively.

Result: By comparing Figure 9E and G to Figure 9A and C, it is found that the distance of the carbon atoms between the alkyls of V32I and V82I in PR2 and the hydrophobic groups (the aniline and Phenyl) of APV are obviously shortened,

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.

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,

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