Introduction: The following mutations have been added to existing classes or drugs: K65E/N has been added to the bars for the nucleoside and nucleotide analogue reverse transcriptase inhibitors (nRTIs) abacavir, didanosine, emtricitabine, lamivudine, stavudine, and tenofovir; L100I has been added to the bar for the nonnucleoside analogue reverse transcriptase inhibitor (NNRTI) rilpivirine; and F121Y has been added to the bars for the integrase strand transfer inhibitors (InSTIs) dolutegravir, elvitegravir, and raltegravir.
Discussion: In site-directed mutants and clinical isolates, the mutation F121Y has a profound effect on susce
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
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.
"Prolonged and substantial discordance in prevalence of raltegravir-resistant HIV-1 in plasma versus PBMC samples revealed by 454 ""deep"" sequencing."
Method: Secondary raltegravir-associated DRMs were defined to be E92V, Q95K, T97A, F121Y, E138A/K, G140A/C/S, S147G, V151A/I/L, M154I/L, E157Q, and G163K/R, and linkages examined were T97A and Y143C/R, E138A/K and Q148H/K/R, G140S and Q148H/K/R, and G163K/R and
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.
G118R and F121Y mutations identified in patients failing raltegravir treatment confer dolutegravir resistance.
1Abstract: Both Stanford Database and Geno2Pheno list 1Abstract: We report for the first time the ""in vivo"" selection F121Y and evolution to Y143R in a 31years old male clade B HIV-1 infected patient failing a raltegravir-containing salvage regimen."
Abstract: F121Y might be an alternative pathway to Y143R.
Abstract: Changing of RAL-containing regimen upon the identification of F121Y might avoid the evolution of raltegravir resistance.
Abstract: The emergence of F121Y was observed at week 32 and 40, alongside with L74I, T97A, Q137H and V151I.
In vitro resistance selections using elvitegravir, raltegravir, and two metabolites of elvitegravir M1 and M4.
Abstract: Additional resistance selection experiments using elvitegravir led to the development of previously reported integrase inhibitor resistance mutations (T66I, F121Y, and S153Y) as well as a novel R263K integrase mutation.
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%).
The HIV-1 integrase mutations Y143C/R are an alternative pathway for resistance to Raltegravir and impact the enzyme functions.
Method: We followed-up the 50 mutations of resistance present at 32 positions: associated with in vitro or in vivo resistance to HIV-1 integrase inhibitors: H51Y, T66I/A/K, V72I, L74I/A/M, E92Q, T97A, T112I, F121Y, T125K, A128T, E138 K/A/D, G140R/C/H, Y143C/H/R, Q146K/P, S147G, Q148K/R/H, V151I, PMID: 19014951
2009
Journal of molecular biology
Discussion: Second site mutations of F121Y and T125K subsequently appear in HIV-1 IN containing the V72I mutation.
HIV mutation literature information.
PMID: 
2014
Topics in antiviral medicine
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