Genetic variation of the HIV-1 integrase region in newly diagnosed anti-retroviral drug-naive patients with HIV/AIDS in Korea.
PMID: 20946407
2011
Clinical microbiology and infection
Abstract: Major mutation sites in the integrase (E92Q, F121Y, G140A/S, Y143C/R, Q148H/R/K and N155H) were not detected, and only a few minor mutation sites (L74M, V151I, E157Q, V165I, I203M, S230N and D232N) were identified in 21 strains (28%).
Cross-resistance profile determination of two second-generation HIV-1 integrase inhibitors using a panel of recombinant viruses derived from raltegravir-treated clinical isolates.
PMID: 20956600
2011
Antimicrobial agents and chemotherapy
Abstract: Although samples with the Y143R/C mutation had reduced susceptibility to RAL, they remained susceptible to MK-2048 and compound G.
G140S/Q148R and N155H mutations render HIV-2 Integrase resistant to raltegravir whereas Y143C does not.
PMID: 21576445
2011
Antimicrobial agents and chemotherapy
Abstract: Reigadas et al., PLoS One 5:e10311, 2010), we investigated the genetic pathway and the dynamics of emergence of the Y143C/R mutations in three patients failing RAL-containing regimens.
Abstract: The HIV-1 integrase (IN) mutations Y143C/R are known as raltegravir (RAL) primary resistance mutations.
Rapid Development of High-Level Resistance to Dolutegravir With Emergence of T97A Mutation in 2 Treatment-Experienced Individuals With Baseline Partial Sensitivity to Dolutegravir.
PMID: 21576445
2011
Antimicrobial agents and chemotherapy
Abstract:
Abstract: Assays without RAL suggested that the T97A mutation could rescue the catalytic activity which was impaired by the presence of the Y143C/R mutation.
Abstract: FCs of 18 and 100 were observed with the strand transfer assay for IN Y143C/T97A and Y143R/T97A mutations, with IC(50) of 0.625 muM and 2.5 muM, respectively.
Abstract: In the strand transfer assay, the IN Y143C or R mutation combined with the secondary mutation T97A severely impaired susceptibility to RAL compared to results with the IN Y143C or R mutation alone.
Switching between raltegravir resistance pathways analyzed by deep sequencing.
Introduction: Three codons can mutate to generate primary resistance mutations, which encode Y143R/C/H, Q148H
Discussion: Our findings taken together support the idea that Y143H, and possibly Y143C and Q148R, are authentic replication-competent polymorphisms that are present in viral populations in the absence of RAL.
Discussion: The Y143C and Q148R substitutions were marginally significant by some measures but did not survive correction for multiple comparisons.
Discussion: also investigated RAL resistance using 454 sequencing and reported detection of Y143H, Y143C, and Q148R prior to initiation of therapy.
Long-lasting persistence of integrase resistance mutations in HIV-2-infected patients after raltegravir withdrawal.
Abstract: RESULTS: At the time of RAL withdrawal, virus exhibited different integrase resistance pathways: G140S/Q148R, E92Q/N155H, T97A/N155H and T97A/Y143C.
Abstract: Regarding patient 4, the mutant T97A/Y143C was still detected at M1 and M3 following RAL withdrawal.
Phenotypic susceptibility of HIV-2 to raltegravir: integrase mutations Q148R and N155H confer raltegravir resistance.
Abstract: Amino acid changes Q148R and N155H individually conferred resistance to raltegravir (14-fold and seven-fold, respectively), whereas the Y143C replacement had no statistically significant effect on raltegravir sensitivity.
Introduction: Specific amino acid changes that are known to confer raltegravir resistance in HIV-1 have been observed in integrase sequences from raltegravir-treated HIV-2 patients; these commonly include
Introduction: recently reported that Q148R and N155H individually improve the ability of purified HIV-2 integrase to catalyze strand transfer in the presence of raltegravir, whereas the Y143C change alone had no impact on raltegravir sensitivity.
Localization of ASV integrase-DNA contacts by site-directed crosslinking and their structural analysis.
Abstract: The development of resistance to raltegravir mainly involved three resistance mutations in integrase gene: Q148H/K/R, N155H, and Y143C/H/R.
Discussion: A recent crystal structure study enabled to describe the interactions between HIV-1 integrase residue Tyr 143 and the methyloxadiazole group of raltegravir, which could explain the role of the Y143C/H/R mutations in the development of resistance to raltegravir.
Discussion: Moreover, the characterization of the phenotypic evolution showed that a switch from N155H to Y143C/R was linked to an increase in resistance to raltegravir.
Discussion: Most of these shifts in raltegravir-resistance profiles
The HIV-1 integrase genotype strongly predicts raltegravir susceptibility but not viral fitness of primary virus isolates.
Abstract: OBJECTIVE: : Resistance to raltegravir is associated with three genetic pathways defined by the mutations Y143R/C, Q148H/R/K or N155H in integrase, which also infer a viral fitness cost.
HIV mutation literature information.
PMID: 
2011
Clinical microbiology and infection
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