ArticleAntimicrobial agents and chemotherapy2013
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.
Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
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Who cites it
22 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.
- Current ARTs, Virologic Failure, and Implications for AIDS Management: A Systematic Review.Viruses · 2023Pooled it
- HIV-1 Genetic Diversity and Drug Resistance Mutation Profiles in Donetsk, Luhansk and Zaporizhzhia Regions.Viruses · 2026Article
- Prevalence of major INSTI and HIV-1 drug resistance mutations in pre- and antiretroviral-treated patients in Indonesia.Narra J · 2024Article
- Integrase strand transfer inhibitor (INSTI)-resistance mutations for the surveillance of transmitted HIV-1 drug resistance.The Journal of antimicrobial chemotherapy · 2020Article
- Multifaceted HIV integrase functionalities and therapeutic strategies for their inhibition.The Journal of biological chemistry · 2019Review
- Durability of INI-containing regimens after switching from PI-containing regimens: a single-centre cohort of drug-experienced HIV-infected subjects.Drug design, development and therapy · 2019Article
- The S230R Integrase Substitution Associated With Virus Load Rebound During Dolutegravir Monotherapy Confers Low-Level Resistance to Integrase Strand-Transfer Inhibitors.The Journal of infectious diseases · 2018Article
- Analyses of HIV-1 integrase sequences prior to South African national HIV-treatment program and available of integrase inhibitors in Cape Town, South Africa.Scientific reports · 2018Article
- Human Immunodeficiency Virus Type 1 Drug Resistance Mutations Update.The Journal of infectious diseases · 2017Article
- HIV drug resistance against strand transfer integrase inhibitors.Retrovirology · 2017Review
- Lack of impact of pre-existing T97A HIV-1 integrase mutation on integrase strand transfer inhibitor resistance and treatment outcome.PloS one · 2017Article
- HIV-1 drug resistance and resistance testing.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2016Review
- Antiviral Activity of Bictegravir (GS-9883), a Novel Potent HIV-1 Integrase Strand Transfer Inhibitor with an Improved Resistance Profile.Antimicrobial agents and chemotherapy · 2016Article
- Effect on HIV-1 viral replication capacity of DTG-resistance mutations in NRTI/NNRTI resistant viruses.Retrovirology · 2016Article
- Different Pathways Leading to Integrase Inhibitors Resistance.Frontiers in microbiology · 2016Review
- Simian-tropic HIV as a model to study drug resistance against integrase inhibitors.Antimicrobial agents and chemotherapy · 2015Article
- In vitro activity of dolutegravir against wild-type and integrase inhibitor-resistant HIV-2.Retrovirology · 2015Article
- Antiviral characteristics of GSK1265744, an HIV integrase inhibitor dosed orally or by long-acting injection.Antimicrobial agents and chemotherapy · 2015Article
- Practical guidance for nonoccupational postexposure prophylaxis to prevent HIV infection: an editorial review.AIDS (London, England) · 2014Review
- Review
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4 authors.
Funding
Abstract
Y143C,R substitutions in HIV-1 integrase define one of three primary raltegravir (RAL) resistance pathways. Here we describe clinical isolates with alternative substitutions at position 143 (Y143A, Y143G, Y143H, and Y143S [Y143A,G,H,S]) that emerge less frequently, and we compare the genotypic and phenotypic profiles of these viruses to Y143C,R viruses to reconcile the preferential selection of Y143C,R variants during RAL treatment. Integrase amino acid sequences and RAL susceptibility were characterized in 117 patient isolates submitted for drug resistance testing and contained Y143 amino acid changes. The influence of specific Y143 substitutions on RAL susceptibility and their preferential association with particular secondary substitutions were further defined by evaluating the composition of patient virus populations along with a large panel of site-directed mutants. Our observations demonstrate that the RAL resistance profiles of Y143A,G,H,S viruses and their association with specific secondary substitutions are similar to the well-established Y143C profile but distinct from the Y143R profile. Y143R viruses differ from Y143A,C,G,H,S viruses in that Y143R confers a greater reduction in RAL susceptibility as a single substitution, consistent with a lower resistance barrier. Among Y143A,C,G,H,S viruses, the higher prevalence of Y143C viruses is the result of a lower genetic barrier than that of the Y143A,G,S viruses and a lower resistance barrier than that of the Y143H viruses. In addition, Y143A,C,G,H,S viruses require multiple secondary substitutions to develop large reductions in RAL susceptibility. Patient-derived viruses containing Y143 substitutions exhibit cross-resistance to elvitegravir.
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