Result: Data regarding accessory mutations to Q151M were available in 155 (86%) patients: A62V was present in 49 (32%), V75I in 62 (40%), F77L in 47 (30%) and F116Y in 99 (64%), and 75% of patients showed at least one accessory mutation.
The HIV-1 Reverse Transcriptase A62V Mutation Influences Replication Fidelity and Viral Fitness in the Context of Multi-Drug-Resistant Mutations.
Abstract: In particular, A62V was observed in various multi-dideoxynucleoside resistant (MDR) mutation complexes, including the Q151M complex (i.e., A62V, V75I, F77L, F116Y, and Q151M), and the T69SSS insertion complex, which has a serine-serine insertion between amino acid positions 69 and 70 (i.e., M41L, A62V, T69SSS, K70R, and T215Y).
Introduction: In particular, A62V is normally seen in different mutational arrangements, located mostly on the flexible beta3-beta4 loop region of the fingers sub-domain of
Risk factors and outcomes for the Q151M and T69 insertion HIV-1 resistance mutations in historic UK data.
Distinct Pattern of Thymidine Analogue Mutations with K65R in Patients Failing Tenofovir-Based Antiretroviral Therapy.
PMID: 29084434
2018
AIDS research and human retroviruses
Introduction: However, in the 31 patients with no K65R present at S2, 6 had intermediate or high-level resistance to AZT: 4 were caused by TAM-2 DRMs, 1 by T215Y, and 1 by Q151M-complex mutations Q151M, A62V, V75I, F77L, F116Y.
Chemical system biology based molecular interactions to identify inhibitors against Q151M mutant of HIV-1 reverse transcriptase.
Introduction: Notably, HIV-1 RT Q151M is a critical mutation that confers multi-NRTI resistance, accompanied by A62V, V75I, F77L, and F116Y mutations (Q151M-complex).
Result: A recent structural study of HIV-1 RTQ151M-complex suggested that the F116Y mutation improves polymerization fitness, which might be caused by N-site stabilization through hydrogen bond formation between the side-chain hydroxyl of Tyr116 and the main-chain O of Lys73.
Result: Furthermore, the anti-HIV-1 activity of ETV drastically improved in the presence of Q151M and additional mutations Y115F and
HIV-1 with HBV-associated Q151M substitution in RT becomes highly susceptible to entecavir: structural insights into HBV-RT inhibition by entecavir.
Method: Antiviral assays (p24 assay) using wild-type HIV-1 (HIV-1WT) and replicable HIV-1 variants (HIV-1Q151M, HIV-1Q151M/Y115F/F116Y, and HIV-1Q151M/I63V/L74V) were also conducted as previously described.
Result: Critically, EFdA activity against HIV-1Q151M and HIV-1Q151M/Y115F/F116Y increased (IC50: 30 pM for both variants) when compared to that against HIV-1WT (IC50: 0.4 nM).
Result: HIV-1Q151M, HIV-1Q151M/Y115F/F116Y, and HIV-1Q151M/I63V/L74V propagated slower than did HIV-1WT, but HIV-1Q151M/Y115F/F116Y reached similar or slightly greater supernatant p24 le
Week 48 resistance analysis of Elvitegravir/Cobicistat/Emtricitabine/Tenofovir DF versus Atazanavir + Ritonavir + Emtricitabine/Tenofovir DF in HIV-1 infected women (WAVES study GS-US-236-0128).
Method: Primary NRTI-R substitutions assessed were M41L, A62V, K65R, D67N, T69 insertions, K70E/R, L74I/V, V75I, F77L, Y115F, F116Y, Q151M, M184V/I, L210W, T215F/Y, and K219E/N/Q/R in RT.
Structural Insights into HIV Reverse Transcriptase Mutations Q151M and Q151M Complex That Confer Multinucleoside Drug Resistance.
PMID: 28396546
2017
Antimicrobial agents and chemotherapy
Abstract: The compensatory set of mutations in Q151Mc, particularly F116Y, restricts the side chain flexibility of M151 and helps restore the DNA polymerization efficiency of the enzyme.
Chemical system biology based molecular interactions to identify inhibitors against Q151M mutant of HIV-1 reverse transcriptase.
PMID: 28396546
2017
Antimicrobial agents and chemotherapy
Abstract: Q151M and four associated mutations, A62V, V75I, F77L, and F116Y, were detected in patients failing therapies with dideoxynucleosides (didanosine [ddI], zalcitabine [ddC]) and/or zidovudine (AZT).
HIV mutation literature information.
PMID: 
2019
PloS one
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