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 HIV mutation literature information.


  Lack of integrase inhibitors associated resistance mutations among HIV-1C isolates.
 PMID: 26626277       2015       Journal of translational medicine
Discussion: This includes T66IAK, E92Q, F121Y, G140SA, Y143HCR, Q146P, S147G, Q148KHR, and N155HS; (2) minor INI-resistance mutations were defined as non-polymorphic or minimally polymorphic mutations that reduce INI susceptibility H51Y, L74 M, T97A, E138AK, S153Y,


  Cross-resistance to elvitegravir and dolutegravir in 502 patients failing on raltegravir: a French national study of raltegravir-experienced HIV-1-infected patients.
 PMID: 25558077       2015       The Journal of antimicrobial chemotherapy
Abstract: The most frequent mutations observed were N155H/S (19.1%), Q148G/H/K/R (15.4%) and Y143C/G/H/R/S (6.7%).


  Preclinical profile of BI 224436, a novel HIV-1 non-catalytic-site integrase inhibitor.
 PMID: 24663024       2014       Antimicrobial agents and chemotherapy
Abstract: BI 224436 also retains full antiviral activity against recombinant viruses encoding INSTI resistance substitutions N155S, Q148H, and E92Q.


  "Prolonged and substantial discordance in prevalence of raltegravir-resistant HIV-1 in plasma versus PBMC samples revealed by 454 ""deep"" sequencing."
 PMID: 23049972       2012       PloS one
Method: Out of the eight patients with DRMs, five of them developed at least one of the three major raltegravir resistance pathways (Y143R/C/H, Q148H/R/K and/or N155H/S), had longitudinal paired plasma and PBMC samples available, and had samples that could be successfully amplified and sequenced.
Method: Primary raltegravir-associated DRMs were defined to be E92Q, Y143R/C/H, Q148H/R/K, and N155H/S (HXB2 int amino acid coordinates), according to the International AIDS Society guidelines.


  Single mutations in HIV integrase confer high-level resistance to raltegravir in primary human macrophages.
 PMID: 21628534       2011       Antimicrobial agents and chemotherapy
Abstract: We show here that during macrophage infection, the presence of a single primary raltegravir resistance mutation (Q148H, Q148R, N155H, or N155S) is sufficient to provide resistance to raltegravir comparable to that seen in viruses expressing both primary and secondary mutations in costimulated CD4(+) T cells.


  The HIV-1 integrase mutations Y143C/R are an alternative pathway for resistance to Raltegravir and impact the enzyme functions.
 PMID: 20436677       2010       PloS one
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: 20377427       2010       AIDS research and human retroviruses
Abstract: Amino acid sequence analysis revealed there were no primary mutations (Y143R/C/H, Q148H/R/K, and N155H/S) associated with reduced susceptibility to the integrase inhibitors raltegravir and elvitegravir.


  Effects of HIV type-1 immune selection on susceptability to integrase inhibitor resistance.
 PMID: 19918099       2009       Antiviral therapy
Introduction: Additionally, the major resistance mutations Q148H/RK and N155S have been shown to reduce replicative capacity.
Result: Of the 38 major and minor integrase inhibitor resistance associated codons, 44, 61, 66, 92, 121, 140, 143, 147, 148, 155, 226 and 263 were the only positions absolutely conserved across all 342 sequences and these included six primary resistance-associated mutations for raltegravir and elvitegravir (T66I, E92Q, G140S, Y143C/H/R Q148H/R/K and N155S/H).


  Virological and immunological response in HIV-1-infected patients with multiple treatment failures receiving raltegravir and optimized background therapy, ANRS CO3 Aquitaine Cohort.
 PMID: 19336453       2009       The Journal of antimicrobial chemotherapy
Abstract: Raltegravir-related mutations emerged in 9 of 11 failing patients (82%): Q148H/R (n = 5), N155S/H (n = 3) and S230N (n = 1).


  A quantum mechanic/molecular mechanic study of the wild-type and N155S mutant HIV-1 integrase complexed with diketo acid.
 PMID: 17981909       2008       Biophysical journal
Abstract: In this study, we use molecular dynamics simulations, within the hybrid quantum mechanics/molecular mechanics (QM/MM) approach, to determine the protein-ligand interaction energy for wild-type and N155S mutant HIV-1 IN, both complexed with a DKA.
Abstract: Our calculations show that the binding energy is higher in wild-type than in the N155S mutant, in accordance with the experimental results.



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