literature

HIV mutation literature information.

Genotypic resistance profiles of HIV-2-treated patients in West Africa.

PMID: 24583671 2014 AIDS (London, England)

Abstract: The most prevalent protease inhibitor resistance mutations were V47A (60%) and I54M (30%).

Method: Among the protease inhibitor resistance mutations, the I50V, I54M, and I84V were associated with resistance to darunavir.

Method: In this study, HIV-2 resistance mutations were identified using the list generated by the 'Collaborative HIV and Anti-HIV Drug Resistance Network', leading to the following mutations in reverse transcriptase - K65R, D67G/N, N69S/T, K70N/R, L74V, V111I,

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

PMID: 25101529 2014 Topics in antiviral medicine

Discussion: The negative impact of the protease mutations I47V, I54M, T74P, and I84V and the positive impact of the protease mutation V82A on virologic response to darunavir/ritonavir were shown in 2 data sets independently.

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, L76V, V82A

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

PMID: 24738918 2014 ACS chemical biology

5Result: Additionally, ""second shell"" mutations L10I, L24I, L33F, and I54M alter residues that form direct interactions with residues in the active site cavity."

Result: In PRP51-D25N/DRV, the I54M mutation introduced new van der Waals interactions with DRV (Figures 3C and 5), while M46L had no contacts with the ligand.

Result: Mutations M46L and I54M alter residues in the flaps and are proposed to have small indirect effects on inhibitor binding and may alter the flap dynamics.

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.

The role of mutations at codons 32, 47, 54, and 90 in HIV-1 protease flap dynamics.

PMID: 32309558 2014 Discoveries (Craiova, Romania)

Abstract: Also, I54M and L90M may be responsible for asymmetric movement of the protease flaps

Conclusion: I54M and L90M may be responsible for asymmetric movement of the protease flaps.

Conclusion: Our results indicate a novel structural role for the I47V, V32I, I54M and L90M resistance mutations.

Dimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir.

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.

"Description of the L76V resistance protease mutation in HIV-1 B and ""non-B"" subtypes."

PMID: 23349869 2013 PloS one

Method: In our study, samples with at least one of the major PI RAM of the IAS-USA list as follows: D30N, V32I, M46I/L, I47A/V, G48V, I50L/V, I54L/M, Q58E, T74P, L76V,

Result: Among subtype B samples, the major PI RAM significantly correlating as pairs with L76V were: M46I, I54L/M, Q58E, V82F, I84V, and L90M.

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 non-polymorphic ARV-selected mutations were classified as drug resistance mutations (DRM): (i) the NRTI resistance mutations M41L, A62V, K65RN, D67NG, T69D, T69 insertions, T69 deletion, K70REGQ, L74VI, V75MT, F77L, Y115F, F116Y, Q151M, M184VI, L210W, T215YFSDCIV, and Table: I54L/M

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

Abstract: Mutations V82A and I54M showed compensating structural changes consistent with 6-7-fold lower inhibition.

Abstract: The high resolution X-ray crystal structures of inhibitor 1 in complexes with single substitution mutants PR(R8Q), PR(D30N), PR(I50V), PR(I54M), and PR(V82A) were analyzed in relation to kinetic data.

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 <

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