Progressive emergence of an S153F plus R263K combination of integrase mutations in the proviral DNA of one individual successfully treated with dolutegravir.
PMID: 25666155
2015
Antimicrobial agents and chemotherapy
Abstract: The presence of R263K and M184I/V in a single virus resulted in substantial further decreases in the viral replicative capacity compared to that in the presence of single substitutions alone.
Abstract: We investigated the effect of combining the dolutegravir-specific R263K integrase resistance substitution with either M184I or M184V, two reverse transcriptase drug resistance substitutions that are frequently detected in individuals failing therapeutic regimens containing either lamivudine or emtricitabine.
In vitro activity of dolutegravir against wild-type and integrase inhibitor-resistant HIV-2.
Result: In addition, the roles of novel INSTI-associated changes (i.e, H51Y, G118R, F121Y, E138A/K, and R263K) remain to be determined in HIV-2, and the level of dolutegravir resistance in vitro that correlates with virologic failure in HIV-2-infected patients is unknown.
[Resistance profile and genetic barrier of dolutegravir].
PMID: 25858608
2015
Enfermedades infecciosas y microbiologia clinica
Abstract: The mutations eventually selected (R263K, H51Y and E138K) do not confer significant resistance, and induce a fitness cost that prevents HIV-1 from evading drug pressure.
Influence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study.
Introduction: However, only two substitutions, G118R and R263K, proved to be responsible for the virus resistance to DTG .
Introduction: Thus, in vitro selection of DTG-resistant strains of HIV-1 subtypes B, C, and A/G demonstrated that only the R263K substitution was common to all subtypes; the G118R substitution was found only in the subtypes A/G and C .
Introduction: Variants containing a number of amino acid substitutions in IN (H51Y, L101I, G118R, T124A, S153F/Y, R263K) were found during selection of HIV-1 strains resistant to DTG in a lymphocytes culture .
HIV-1 Group O Resistance Against Integrase Inhibitors.
PMID: 26017662
2015
Journal of acquired immune deficiency syndromes (1999)
Abstract: Site-directed mutagenesis was performed on the pCOM2.5 HIV group 0 infectious clone to ascertain the impact of INSTI resistance substitutions at positions Q148R, N155H, and R263K within integrase on susceptibility to INSTIs and infectiousness.
Resistance against Integrase Strand Transfer Inhibitors and Relevance to HIV Persistence.
Abstract: We review here the issue of drug resistance against integrase strand transfer inhibitors as well as both pre-clinical and clinical studies that have led to the identification of the R263K mutation in integrase as a signature resistance substitution for dolutegravir.
Introduction: Although substitutions at positions M50I, H51Y or E138K emerged under DTG pressure after R263K, none of these was able to restore viral replicative capacity to wild-type levels.
Introduction: Furthermore, there is a high degree of likelihood that DTG will remain active against the latter viruses because of the very long dissociative half-life between DTG and integrase protein, very tight binding between DTG and
Progressive emergence of an S153F plus R263K combination of integrase mutations in the proviral DNA of one individual successfully treated with dolutegravir.
Abstract: R263K in HIV-1 subtype C also conferred low levels of resistance against dolutegravir and high levels of cross-resistance against elvitegravir, but not raltegravir.
Abstract: CONCLUSIONS: The R263K substitution is more deleterious to integrase strand-transfer activity and viral infectiousness in HIV-1 subtype C than in subtype B.
Abstract: DESIGN AND METHODS: We used cell-free strand transfer assays and tissue culture experiments to characterize the R263K substitution in HIV-1 subtype C integrase in comparison with subtype B.
Abstract: RESULTS: Cell-free biochemical assays showed that the R263K substitution diminished subtype C integrase strand-transfer activity by decreasing the affinity of
Progressive emergence of an S153F plus R263K combination of integrase mutations in the proviral DNA of one individual successfully treated with dolutegravir.
Abstract: However, viral infectivity was significantly decreased from that of NL4.3IN(N155H/R263K) after the addition of each tertiary mutation, and no increases in levels of DTG resistance were observed.
Abstract: Therefore, the current study aimed to uncover whether accessory mutations that appear after N155H in response to raltegravir/elvitegravir were compatible with N155H and R263K.
Abstract: These data support the hypothesis that primary resistance against DTG cannot evolve through RAL/EVG resistance pathways and that the selection of R263K leads HIV into an evolutionary dead-end.
Abstract: This work shows that the compensatory mutations that evolve after N155H under continued DTG or RAL/EVG pressure in patients are unable t
Progressive emergence of an S153F plus R263K combination of integrase mutations in the proviral DNA of one individual successfully treated with dolutegravir.
Abstract: HIV drug-resistant mutations in integrase that can arise in individuals treated with elvitegravir commonly include the T66I substitution, whereas R263K is a signature resistance substitution against dolutegravir.
Abstract: In order to determine how different combinations of integrase resistance mutations can influence the outcome of therapy, we report here the effects of the T66I, E138K, and R263K substitutions, alone and in combination, on viral replicative capacity and resistance to integrase inhibitors.
Abstract: Our results show that the addition of R263K to the T66I substitution diminishes viral replicative capacity and s
Progressive emergence of an S153F plus R263K combination of integrase mutations in the proviral DNA of one individual successfully treated with dolutegravir.
Abstract: CONCLUSION: The DTG-resistant R263K substitution antagonized the development of HIV-1 resistance against RAL while partially facilitating the occurrence of resistance against EVG.
Abstract: DESIGN AND METHODS: We performed tissue culture selection experiments using DTG-resistant viruses containing integrase substitutions at positions R263K, H51Y/R263K, E138K/R263K, G118R and H51Y/G118R in the presence of increasing concentrations of either RAL or EVG.
Abstract: In contrast, resistance against EVG appeared earlier than in wild-type virus in viruses containing the R263K and
HIV mutation literature information.
PMID: 
2015
Antimicrobial agents and chemotherapy
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