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 HIV mutation literature information.


  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.
Method: The following sense with cognate antisense (not shown) oligonucleotides (Integrated DNA Technologies, Coralville, IA) was used in the mutagenesis: G118R, 5'-GTACATACAGACAATCGCAGCAATTTCACCAGTAC-3'; E138K, 5'-GGCGGGGATCAAGCAGAAATTTGGCATTCCCTA-3'; G140A, 5'-GGGGATCAAGCAGGAATTTGCCATTCCCTACAATC-3'; G140S, 5'-GGGGATCAAGCAGGAATTTAGCATTCCCTACAATC-3';


  New raltegravir resistance pathways induce broad cross-resistance to all currently used integrase inhibitors.
 PMID: 24710029       2014       The Journal of antimicrobial chemotherapy
Abstract: CONCLUSIONS: This study showed that G118R and F121Y mutations, rarely described in patients failing on raltegravir, induced broad cross-resistance to all currently used integrase inhibitors.
Abstract: In silico, results showed that G118R and F121Y enzymes were associated with reduced binding affinities to each of the inhibitors and with a decreased number of hydrogen bonds compared with the wild-type complexes.
Abstract: METHODS: The behaviour of integrases with mutations G118R and F121Y towards raltegravir, elvitegravir and dolutegravir was analysed by evaluating phenotypic susceptibility and by means of in silico techniques (investigating binding affinities and the stabilization of the inhibi


  Effect of HIV-1 integrase resistance mutations when introduced into SIVmac239 on susceptibility to integrase strand transfer inhibitors.
 PMID: 24920794       2014       Journal of virology
Abstract: DTG remained fully effective against all site-directed mutants except G118R and R263K.
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.


  Biochemical analysis of the role of G118R-linked dolutegravir drug resistance substitutions in HIV-1 integrase.
 PMID: 24080645       2013       Antimicrobial agents and chemotherapy
Abstract: Homology modeling provided insight into the mechanism of resistance conferred by G118R as well as the effects of H51Y or E138K on enzyme activity.
Abstract: Now, we have characterized the impact of the G118R substitution, alone or in combination with either H51Y or E138K, on 3' processing and integrase strand transfer activity.
Abstract: The addition of H51Y and E138K to G118R partially restored strand trans


  Viral fitness cost prevents HIV-1 from evading dolutegravir drug pressure.
 PMID: 23432922       2013       Retrovirology
Discussion: In vitro selection experiments with both DTG and another second-generation compound termed MK-2048 have identified several mutations within the integrase coding region, including G118R, S153Y, and R263K that confer low-level resistance to these drugs .


  HIV Drug Resistance and the Advent of Integrase Inhibitors.
 PMID: 23180144       2013       Current infectious disease reports
Abstract: Here, we provide new information about the most recent mutations identified and other mutations that confer resistance to several integrase inhibitors, such as new resistance mutations-for example, G118R, R263K, and S153Y-that have been identified through in vitro selection studies with second-generation integrase strand transfer inhibitors (INSTIs).


  The development of novel HIV integrase inhibitors and the problem of drug resistance.
 PMID: 22989757       2012       Current opinion in virology
Abstract: Several newly identified resistance mutations, such as G118R, R263K and S153Y, have been identified through tissue culture selection studies with second-generation integrase strand-transfer inhibitors (INSTIs).


  Resistance to HIV integrase inhibitors.
 PMID: 22789986       2012       Current opinion in HIV and AIDS
Abstract: RECENT FINDINGS: New resistance mutations, such as G118R, R263K and S153Y, have been recently identified through in-vitro selection studies with second-generation integrase strand-transfer inhibitors (INSTIs).


  Risk factors for raltegravir resistance development in clinical practice.
 PMID: 22763565       2012       The Journal of antimicrobial chemotherapy
Abstract: Among patients without main resistance mutations, two patients showed raltegravir phenotypic resistance, one naturally with F121Y at baseline and the other acquiring G118R at failure.


  The HIV-1 integrase G118R mutation confers raltegravir resistance to the CRF02_AG HIV-1 subtype.
 PMID: 21933786       2011       The Journal of antimicrobial chemotherapy
Abstract: For this patient, the phenotypic analysis showed that addition of only the G118R mutation conferred a high level of resistance to raltegravir (fold change = 25.5) and elvitegravir (fold change = 9.2).



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