Method: Patients with more than one darunavir resistance-associated mutation or with known major integrase resistance-associated mutations (N155H, Q148H/R/K, Y143C/R, and G140S) were excluded from the study.
HIV-2 integrase polymorphisms and longitudinal genotypic analysis of HIV-2 infected patients failing a raltegravir-containing regimen.
Introduction: Information on its efficiency against HIV-2 strains bearing integrase inhibitor resistance mutations is still limited, but phenotypic assays carried out with HIV-2 clinical isolates from patients treated with RAL showed that mutations T97A/Y143C, G140S/Q148R or G140T/Q148R/N155H conferred moderate resistance to DTG (7-18-fold increase of the EC50).
Introduction: On the other hand, the N155H-Y143C and N155H-Q148R replacements seem to define mutually exclusive pathways to RAL resistance in HIV-2.
Introduction: Overall, three major resistance pathways h
Effect of HIV-1 integrase resistance mutations when introduced into SIVmac239 on susceptibility to integrase strand transfer inhibitors.
Abstract: Each of the G118R, Y143R, Q148R, R263K, and G140S/Q148R mutations, when introduced into SIV, impaired infectiousness and replication fitness compared to wild-type virus.
Abstract: In contrast, Y143R, Q148R, and N155H all yielded low levels of resistance to RAL.
Abstract: The combination of G140S/Q148R conferred high-level resistance to both RAL and EVG (>300- and 286-fold, respectively).
Abstract: Using TZM-bl cells, we demonstrated that the Q148R and N155H mutational pathways conferred resistance to EVG (36-
2014 Update of the drug resistance mutations in HIV-1.
Discussion: N155H mutants tend to predominate early in the course of raltegravir failure, but are gradually replaced by viruses with higher resistance, often bearing mutations G140S+Q148H/R/K, with continuing raltegravir treatment.
Discussion: Minor mutations described in the Q148H/K/R pathway include L74M plus E138A, E138K, or G140S.
Discussion: Raltegravir failure is associated with integrase mutations in at least 3 distinct, but not exclusive, genetic pathways defined by 2 or more mutations including (1) a signature (major) mutation at Q148H/K/R, N155H, or
Week 144 resistance analysis of elvitegravir/cobicistat/emtricitabine/tenofovir DF versus atazanavir+ritonavir+emtricitabine/tenofovir DF in antiretroviral-naive patients.
Abstract: Emergent substitutions were E92Q, N155H, or Q148R (n = 2 each) and T66I or T97A (n = 1 each) in IN and M184V/I (n = 7) and K65R (n = 1) in RT.
HIV-1 group O integrase displays lower susceptibility to raltegravir and has a different mutational pathway for resistance than HIV-1 group M.
PMID: 25397483
2014
Journal of the International AIDS Society
Abstract: Mutations selected in HIV-O can be classified as follows: (1) mutations described for HIV-M such as T97A, Q148R, V151A/I (RAL), T66I, E92Q, E157Q (EVG) and M50I, R263K (DTG) and (2) signature mutations for HIV-O.
Abstract: Only the HIV-O/Div selected the Q148R mutation for RAL and R263K+M50I for DTG, as previously described for HIV-M.
Use of dolutegravir in two INI-experienced patients with multiclass resistance resulted in excellent virological and immunological responses.
PMID: 25397500
2014
Journal of the International AIDS Society
Abstract: Ultra-deep sequencing of integrase showed the selection of Q148R, E138K+Q148K, and N155H variants and phenotypic raltegravir resistance was demonstrated.
Table: Q148R
Impact of primary elvitegravir resistance-associated mutations in HIV-1 integrase on drug susceptibility and viral replication fitness.
PMID: 23529738
2013
Antimicrobial agents and chemotherapy
Abstract: Primary INSTI resistance-associated mutations (RAMs) at six IN positions have been identified in HIV-1-infected patients failing EVG-containing regimens in clinical studies: T66I/A/K, E92Q/G, T97A, S147G, Q148R/H/K, and N155H.
Abstract: Recombinant viruses containing the six most common mutations exhibited a range of reduced EVG susceptibility: 92-fold for Q148R, 30-fold for N155H, 26-fold for E92Q, 10-fold for T66I, 4-fold for S147G, and 2-fold for
Binding mode prediction of biologically active compounds from plant Salvia Miltiorrhiza as integrase inhibitor.
Introduction: The secondary mutation at position G140 (G140S) combined with primary mutation Q148K/R/H significantly enhanced drug resistance.
Introduction: The two primary resistance pathways involved mutations of the amino acids at Q148 (Q148K/R/H) or N155 (N155/H) whereas a third primary mutation pathway at Y143 (Y143C/R) was less commonly found .
In vitro phenotypes to elvitegravir and dolutegravir in primary macrophages and lymphocytes of clonal recombinant viral variants selected in patients failing raltegravir.
PMID: 23798668
2013
The Journal of antimicrobial chemotherapy
Abstract: Only Q148H/R variants had a reduced level of susceptibility (FC 5.48-18.64).
HIV mutation literature information.
PMID: 
2014
PloS one
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