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 HIV mutation literature information.


  Raltegravir and elvitegravir-resistance mutation E92Q affects HLA-B*40:02-restricted HIV-1-specific CTL recognition.
 PMID: 24657622       2014       Microbes and infection
Abstract: EL11-specific CTLs recognized E92Q peptide-pulsed and E92Q mutant virus-infected cells less effectively than EL11 peptide-pulsed and wild-type virus-infected cells, respectively.
Abstract: Ex vivo ELISpot analysis showed no induction of E92Q-specific T cells in chronically HIV-1-infected individuals.
Abstract: We here investigated the effect of a raltegravir and elvitegravir-resistance mutation (E92Q) on HLA-B*40:02-restricted Int92-102 (EL11: ETGQETAYFLL)-specific CTLs.


  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.


  HIV-2 integrase polymorphisms and longitudinal genotypic analysis of HIV-2 infected patients failing a raltegravir-containing regimen.
 PMID: 24681625       2014       PloS one
Abstract: The 10 raltegravir-experienced patients exhibited resistance mutations via three main genetic pathways: N155H, Q148R, and eventually E92Q - T97A.
Introduction: Overall, three major resistance pathways have been identified and shown to elicit high-level raltegravir and elvitegravir resistance in HIV-2: i) N155H/E92Q, ii) Q148R/G140S, and iii) Y143C/E92Q or Y143C/T97A.
Result: Collectively, our data revealed three distinct patterns of mutations eliciting resistance to raltegravir in HIV-2: Q148R in one patient,  PMID: 25101529       2014       Topics in antiviral medicine
Discussion: E92Q alone reduces susceptibility to elvitegravir more than 20-fold and causes limited (<5-fold) cross resistance to raltegravir.
Discussion: Cross-resistance studies with raltegravir- and elvitegravir-resistant viruses indicate that Q148H and G140S in combination with mutations L74I/M, E92Q, T97A, E138A/K, G140A, or N155H are associated with 5-fold to 20-fold reduced dolutegravir susceptibility and reduced virologic suppression in patients.
Discussion: Mutations described in the N155H pathway include this major mutation plus either L74M, E92Q, <


  Week 144 resistance analysis of elvitegravir/cobicistat/emtricitabine/tenofovir DF versus atazanavir+ritonavir+emtricitabine/tenofovir DF in antiretroviral-naive patients.
 PMID: 25350960       2014       HIV clinical trials
Abstract: Emergent substitutions were E92Q, N155H, or Q148R (n = 2 each) and T66I or T97A (n = 1 each) in IN and M184V/I (n = 7) and K65R (n = 1) in RT.


  Raltegravir and elvitegravir-resistance mutation E92Q affects HLA-B*40:02-restricted HIV-1-specific CTL recognition.
 PMID: 25373632       2014       Interdisciplinary sciences, computational life sciences
Abstract: Although Elvitegravir (EVG) is a newly developed antiretrovirals drug to treat the acquired immunodeficiency syndrome (AIDS), drug resistance has already been found in clinic, such as E92Q/N155H and Q148H/G140S.
Abstract: As full length crystal structure for HIV-1 integrase is still unsolved, we herein use the crystal structure of the full length prototype foamy virus (PFV) in complex with virus DNA and inhibitor Elvitegravir as a template to construct the wild type and E92Q/N155H mutant system of HIV-1 integrase.
Abstract: Molecular dynamic simulations was used to revel the binding mode and the drug resistance of the EVG


  HIV-1 group O integrase displays lower susceptibility to raltegravir and has a different mutational pathway for resistance than HIV-1 group M.
 PMID: 25397483       2014       Journal of the International AIDS Society
Abstract: Mutations selected in HIV-O can be classified as follows: (1) mutations described for HIV-M such as T97A, Q148R, V151A/I (RAL), T66I, E92Q, E157Q (EVG) and M50I, R263K (DTG) and (2) signature mutations for HIV-O.


  HIV-2 antiviral potency and selection of drug resistance mutations by the integrase strand transfer inhibitor elvitegravir and NRTIs emtricitabine and tenofovir in vitro.
 PMID: 23187937       2013       Journal of acquired immune deficiency syndromes (1999)
Abstract: HIV-2 site-directed mutant (SDM) viruses with E92G and E92Q integrase mutations showed 3.7- and 16-fold reduced susceptibilities to EVG, respectively.
Abstract: In resistance selections, EVG selected E92G/Q and S147N in integrase, FTC selected M184V/I in RT, and TFV selected K65R and Y115F in RT.


  Impact of primary elvitegravir resistance-associated mutations in HIV-1 integrase on drug susceptibility and viral replication fitness.
 PMID: 23529738       2013       Antimicrobial agents and chemotherapy
Abstract: Primary INSTI resistance-associated mutations (RAMs) at six IN positions have been identified in HIV-1-infected patients failing EVG-containing regimens in clinical studies: T66I/A/K, E92Q/G, T97A, S147G, Q148R/H/K, and N155H.
Abstract: Recombinant viruses containing the six most common mutations exhibited a range of reduced EVG susceptibility: 92-fold for Q148R, 30-fold for N155H, 26-fold for E92Q, 10-fold for T66I, 4-fold for S147G, and 2-fold for


  Consensus HIV-1 FSU-A integrase gene variants electroporated into mice induce polyfunctional antigen-specific CD4+ and CD8+ T cells.
 PMID: 23667513       2013       PloS one
Figure: Amino acid sequences of the consensus HIV-1 clade A integrase (IN_a), its inactive variant containing mutation in the active site D64V (IN_in), and inactive variant with mutations conferring resistance to elvitegravir H51Y, E92Q, S147G, E157Q, K160Q (IN_in_e3), all with Met-Gly dipeptide on the N-terminus (A); Schematic representation of the structure of the synthetic genes.
Discussion: For HIV-1 clade A, the main mutations of elvitegravir resistance are H51Y, E92Q, S147G, along with E157Q and a secondary nonpolymorphic mutation, K160Q, highly infrequent in



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