Abstract: Comparison of the mutants resistance to the known strand transfer inhibitors raltegravir and elvitegravir, and a new inhibitor XZ-259 (a dihydro-1H-isoindol derivative), showed that integrases of both subtypes with the Q148K mutation were insensitive to raltegravir and elvitegravir but were effectively inhibited by XZ-259.
Abstract: The mutation Q148K almost equally reduced the activity of integrases of both subtypes.
Abstract: To assess the impact of drug resistance mutations on the activity of IN of HIV-1 subtype A strain FSU-A, which is dominant in Russia, variants of the consensus IN of this subtype containing the primary resistance mutations G118R and Q148K and secondary compensatory subst
Integrase inhibitor (INI) genotypic resistance in treatment-naive and raltegravir-experienced patients infected with diverse HIV-1 clades.
PMID: 26311843
2015
The Journal of antimicrobial chemotherapy
Table: Q148K
Discussion: <
Discussion: As mutations at codon 140 play a key role in restoring the fitness of Q148 mutants, their occurrence can also influence the emergence of Q148H/R/K, thus explaining the reduced prevalence of Q148 mutants observed in non-B subtypes.
Discussion: Consistent with available data, there was a strong preferential association of N155H with E92Q, Y143H/R/C with T97A, and G140S/A with Q148H/R/K.
Discussion: Indeed, the N155H and Q148H/R/K pathways have been shown to sequentially emerge in separate genomes within a given individual over time.
Lack of integrase inhibitors associated resistance mutations among HIV-1C isolates.
PMID: 26626277
2015
Journal of translational medicine
Abstract: Neither major resistance-associated IN mutations (T66I/A/K, E92Q/G, T97A, Y143HCR, S147G, Q148H/R/K, and N155H) nor silent mutations known to change the genetic barrier were observed.
Conclusion: None of the previously reported major mutations (T66AIK, E92Q, Y143RCH, S147G, Q148HRK and N155H) associated with resistance to INIs were observed in HIV-1C Ethiopian isolates, indicating that
Resistance to HIV integrase strand transfer inhibitors among clinical specimens in the United States, 2009-2012.
Abstract: Major integrase mutations included T66AIK, E92QV, F121Y, Y143CHR, S147G, Q148HKR, and N155H; multiple accessory mutations were also assessed.
HIV-1-infected patients with advanced disease failing a raltegravir-containing salvage regimen in Sao Paulo, Brazil.
PMID: 24359837
2014
International journal of antimicrobial agents
Abstract: At failure, major RAL resistance mutations included Q148H/R/K (21/47; 45%), N155H (14/47; 30%), Y143R/H/C (3/47; 6%) and E92Q (1/47; 2%).
Abstract: Most samples with Q148H/R/K also showed G140S/A/C (21/47; 45%).
Bicyclic 1-hydroxy-2-oxo-1,2-dihydropyridine-3-carboxamide-containing HIV-1 integrase inhibitors having high antiviral potency against cells harboring raltegravir-resistant integrase mutants.
PMID: 24471816
2014
Journal of medicinal chemistry
Abstract: Importantly, some of these new inhibitors retain greater antiviral efficacy compared to that of RAL when tested against a panel of IN mutants that included Y143R, N155H, G140S/Q148H, G118R, and E138K/Q148K.
Conclusion: Several compounds have selectivity indices of greater than 20,000, and certain of these inhibitors have greater antiviral efficacies than RAL against a panel of IN mutants that included Y143R, N155H, G118R, and the double mutants G140S/Q148H and E1
Comparison of illumina and 454 deep sequencing in participants failing raltegravir-based antiretroviral therapy.
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: The specific amino acid changes that are known to confer RAL resistance in HIV-1 have also been shown to develop in RAL-treated HIV-2 patients: N155H, Q148K/R and, to a lesser extent, Y143C.
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
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.
HIV mutation literature information.
PMID: 
2015
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