ArticlePloS one2010
The HIV-1 integrase mutations Y143C/R are an alternative pathway for resistance to Raltegravir and impact the enzyme functions.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Coevolved Multidrug-Resistant HIV-1 Protease and Reverse Transcriptase Influences Integrase Drug Susceptibility and Replication Fitness.Pathogens (Basel, Switzerland) · 2021Article
- Two-long terminal repeat (LTR) DNA circles are a substrate for HIV-1 integrase.The Journal of biological chemistry · 2019Article
- Impact of the HIV-1 genetic background and HIV-1 population size on the evolution of raltegravir resistance.Retrovirology · 2018Article
- Lack of impact of pre-existing T97A HIV-1 integrase mutation on integrase strand transfer inhibitor resistance and treatment outcome.PloS one · 2017Article
- Characterization of the Drug Resistance Profiles of Integrase Strand Transfer Inhibitors in Simian Immunodeficiency Virus SIVmac239.Journal of virology · 2015Article
- Multiple genetic pathways involving amino acid position 143 of HIV-1 integrase are preferentially associated with specific secondary amino acid substitutions and confer resistance to raltegravir and cross-resistance to elvitegravir.Antimicrobial agents and chemotherapy · 2013Article
- Impact of primary elvitegravir resistance-associated mutations in HIV-1 integrase on drug susceptibility and viral replication fitness.Antimicrobial agents and chemotherapy · 2013Article
- Quantitative prediction of integrase inhibitor resistance from genotype through consensus linear regression modeling.Virology journal · 2013Article
- Broad phenotypic cross-resistance to elvitegravir in HIV-infected patients failing on raltegravir-containing regimens.Antimicrobial agents and chemotherapy · 2012Article
- Article
- Unprocessed viral DNA could be the primary target of the HIV-1 integrase inhibitor raltegravir.PloS one · 2012Article
- Raltegravir in HIV-1 infection: Safety and Efficacy in Treatment-naïve Patients.Clinical medicine reviews in therapeutics · 2011Article
- G140S/Q148R and N155H mutations render HIV-2 Integrase resistant to raltegravir whereas Y143C does not.Retrovirology · 2011Article
- Structure-analysis of the HIV-1 integrase Y143C/R raltegravir resistance mutation in association with the secondary mutation T97A.Antimicrobial agents and chemotherapy · 2011Article
- Elvitegravir overcomes resistance to raltegravir induced by integrase mutation Y143.AIDS (London, England) · 2011Article
- Role of raltegravir in the management of HIV-1 infection.HIV/AIDS (Auckland, N.Z.) · 2011Article
- Patterns of resistance development with integrase inhibitors in HIV.Infection and drug resistance · 2011Article
- Extended use of raltegravir in the treatment of HIV-1 infection: optimizing therapy.Infection and drug resistance · 2010Article
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8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resistance to HIV-1 integrase (IN) inhibitor raltegravir (RAL), is encoded by mutations in the IN region of the pol gene. The emergence of the N155H mutation was replaced by a pattern including the Y143R/C/H mutations in three patients with anti-HIV treatment failure. Cloning analysis of the IN gene showed an independent selection of the mutations at loci 155 and 143. Characterization of the phenotypic evolution showed that the switch from N155H to Y143C/R was linked to an increase in resistance to RAL. Wild-type (WT) IN and IN with mutations Y143C or Y143R were assayed in vitro in 3'end-processing, strand transfer and concerted integration assays. Activities of mutants were moderately impaired for 3'end-processing and severely affected for strand transfer. Concerted integration assay demonstrated a decrease in mutant activities using an uncleaved substrate. With 3'end-processing assay, IC(50) were 0.4 microM, 0.9 microM (FC = 2.25) and 1.2 microM (FC = 3) for WT, IN Y143C and IN Y143R, respectively. An FC of 2 was observed only for IN Y143R in the strand transfer assay. In concerted integration, integrases were less sensitive to RAL than in ST or 3'P but mutants were more resistant to RAL than WT.
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