E138A in HIV-1 reverse transcriptase is more common in subtype C than B: Implications for rilpivirine use in resource-limited settings
Identifieur interne : 001C03 ( Ncbi/Checkpoint ); précédent : 001C02; suivant : 001C04E138A in HIV-1 reverse transcriptase is more common in subtype C than B: Implications for rilpivirine use in resource-limited settings
Auteurs : Nicolas Sluis-Cremer [États-Unis] ; Michael R. Jordan [États-Unis] ; Kelly Huber [États-Unis] ; Carole L. Wallis [Afrique du Sud] ; Silvia Bertagnolio [Suisse] ; John W. Mellors [États-Unis] ; Neil T. Parkin [États-Unis] ; P. Richard Harrigan [Canada]Source :
- Antiviral research [ 0166-3542 ] ; 2014.
Descripteurs français
- KwdFr :
- Agents antiVIH (pharmacologie), Humains, Infections à VIH (traitement médicamenteux), Infections à VIH (virologie), Mutation faux-sens, Nitriles (pharmacologie), Pyrimidines (pharmacologie), Rilpivirine, Résistance virale aux médicaments, Substitution d'acide aminé, Transcriptase inverse du VIH (génétique), Transcriptase inverse du VIH (métabolisme), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (enzymologie), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique).
- MESH :
- enzymologie : VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- génétique : Transcriptase inverse du VIH, VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- métabolisme : Transcriptase inverse du VIH.
- pharmacologie : Agents antiVIH, Nitriles, Pyrimidines.
- traitement médicamenteux : Infections à VIH.
- virologie : Infections à VIH.
- Humains, Mutation faux-sens, Rilpivirine, Résistance virale aux médicaments, Substitution d'acide aminé, VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
English descriptors
- KwdEn :
- Amino Acid Substitution, Anti-HIV Agents (pharmacology), Drug Resistance, Viral, HIV Infections (drug therapy), HIV Infections (virology), HIV Reverse Transcriptase (genetics), HIV Reverse Transcriptase (metabolism), HIV-1 (classification), HIV-1 (enzymology), HIV-1 (genetics), Humans, Mutation, Missense, Nitriles (pharmacology), Pyrimidines (pharmacology), Rilpivirine.
- MESH :
- chemical , genetics : HIV Reverse Transcriptase.
- chemical , metabolism : HIV Reverse Transcriptase.
- chemical , pharmacology : Anti-HIV Agents, Nitriles, Pyrimidines.
- classification : HIV-1.
- drug therapy : HIV Infections.
- enzymology : HIV-1.
- genetics : HIV-1.
- virology : HIV Infections.
- Amino Acid Substitution, Drug Resistance, Viral, Humans, Mutation, Missense, Rilpivirine.
Abstract
The nonnucleoside reverse transcriptase (RT) inhibitor rilpivirine (RPV) has been co-formulated with emtricitabine and tenofovir disoproxil fumarate for initial therapy of HIV-1-infected individuals. RPV, formulated as a long-acting nanosuspension, will also be assessed for its ability to prevent HIV-1 infection in resource limited settings. In this study, we determined whether any pre-existing genetic differences occurred among different HIV-1 subtypes at residues in RT associated with decreased virologic response to RPV. We found that the E138A substitution occurs more frequently in subtype C (range: 5.9–7.5%) than B (range: 0–2.3%) sequences from both treatment-naïve and -experienced individuals (p<0.01) in 4 independent genotype databases. In one of the databases (Stanford University), E138K and E138Q were also more common in RTI-experienced subtype C sequences (1.0% and 1.1%, respectively) than in subtype B sequences (0.3% and 0.6%, respectively). E138A/K/Q in subtype C decreased RPV susceptibility 2.9-, 5.8-, and 5.4-fold, respectively. Taken together, these data suggest that E138A could impact treatment or prevention strategies that include RPV in geographic areas where subtype C infection is prevalent.
Url:
DOI: 10.1016/j.antiviral.2014.04.001
PubMed: 24746459
PubMed Central: 4089891
Affiliations:
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Mellors</name><affiliation wicri:level="2"><nlm:aff id="A1">University of Pittsburgh School of Medicine, Department of Medicine, Division of Infectious Diseases, Pittsburgh, PA, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>University of Pittsburgh School of Medicine, Department of Medicine, Division of Infectious Diseases, Pittsburgh, PA</wicri:regionArea><placeName><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Parkin, Neil T" sort="Parkin, Neil T" uniqKey="Parkin N" first="Neil T." last="Parkin">Neil T. Parkin</name><affiliation wicri:level="2"><nlm:aff id="A6">Data First Consulting, Belmont, CA, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Data First Consulting, Belmont, CA</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Harrigan, P Richard" sort="Harrigan, P Richard" uniqKey="Harrigan P" first="P. Richard" last="Harrigan">P. Richard Harrigan</name><affiliation wicri:level="1"><nlm:aff id="A7">BC Centre for Excellence in HIV/AIDS, Vancouver, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>BC Centre for Excellence in HIV/AIDS, Vancouver</wicri:regionArea><wicri:noRegion>Vancouver</wicri:noRegion></affiliation></author></analytic><series><title level="j">Antiviral research</title><idno type="ISSN">0166-3542</idno><idno type="eISSN">1872-9096</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Anti-HIV Agents (pharmacology)</term><term>Drug Resistance, Viral</term><term>HIV Infections (drug therapy)</term><term>HIV Infections (virology)</term><term>HIV Reverse Transcriptase (genetics)</term><term>HIV Reverse Transcriptase (metabolism)</term><term>HIV-1 (classification)</term><term>HIV-1 (enzymology)</term><term>HIV-1 (genetics)</term><term>Humans</term><term>Mutation, Missense</term><term>Nitriles (pharmacology)</term><term>Pyrimidines (pharmacology)</term><term>Rilpivirine</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agents antiVIH (pharmacologie)</term><term>Humains</term><term>Infections à VIH (traitement médicamenteux)</term><term>Infections à VIH (virologie)</term><term>Mutation faux-sens</term><term>Nitriles (pharmacologie)</term><term>Pyrimidines (pharmacologie)</term><term>Rilpivirine</term><term>Résistance virale aux médicaments</term><term>Substitution d'acide aminé</term><term>Transcriptase inverse du VIH (génétique)</term><term>Transcriptase inverse du VIH (métabolisme)</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) ()</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (enzymologie)</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>HIV Reverse Transcriptase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>HIV Reverse Transcriptase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anti-HIV Agents</term><term>Nitriles</term><term>Pyrimidines</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="en"><term>HIV-1</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>HIV Infections</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>HIV-1</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>HIV-1</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Transcriptase inverse du VIH</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Transcriptase inverse du VIH</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Agents antiVIH</term><term>Nitriles</term><term>Pyrimidines</term></keywords><keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Infections à VIH</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à VIH</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>HIV Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Drug Resistance, Viral</term><term>Humans</term><term>Mutation, Missense</term><term>Rilpivirine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Mutation faux-sens</term><term>Rilpivirine</term><term>Résistance virale aux médicaments</term><term>Substitution d'acide aminé</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P2">The nonnucleoside reverse transcriptase (RT) inhibitor rilpivirine (RPV) has been co-formulated with emtricitabine and tenofovir disoproxil fumarate for initial therapy of HIV-1-infected individuals. RPV, formulated as a long-acting nanosuspension, will also be assessed for its ability to prevent HIV-1 infection in resource limited settings. In this study, we determined whether any pre-existing genetic differences occurred among different HIV-1 subtypes at residues in RT associated with decreased virologic response to RPV. We found that the E138A substitution occurs more frequently in subtype C (range: 5.9–7.5%) than B (range: 0–2.3%) sequences from both treatment-naïve and -experienced individuals (p<0.01) in 4 independent genotype databases. In one of the databases (Stanford University), E138K and E138Q were also more common in RTI-experienced subtype C sequences (1.0% and 1.1%, respectively) than in subtype B sequences (0.3% and 0.6%, respectively). E138A/K/Q in subtype C decreased RPV susceptibility 2.9-, 5.8-, and 5.4-fold, respectively. Taken together, these data suggest that E138A could impact treatment or prevention strategies that include RPV in geographic areas where subtype C infection is prevalent.</p></div></front></TEI><affiliations><list><country><li>Afrique du Sud</li><li>Canada</li><li>Suisse</li><li>États-Unis</li></country><region><li>Californie</li><li>Massachusetts</li><li>Pennsylvanie</li></region><settlement><li>Boston</li></settlement></list><tree><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Sluis Cremer, Nicolas" sort="Sluis Cremer, Nicolas" uniqKey="Sluis Cremer N" first="Nicolas" last="Sluis-Cremer">Nicolas Sluis-Cremer</name></region><name sortKey="Huber, Kelly" sort="Huber, Kelly" uniqKey="Huber K" first="Kelly" last="Huber">Kelly Huber</name><name sortKey="Jordan, Michael R" sort="Jordan, Michael R" uniqKey="Jordan M" first="Michael R." last="Jordan">Michael R. Jordan</name><name sortKey="Jordan, Michael R" sort="Jordan, Michael R" uniqKey="Jordan M" first="Michael R." last="Jordan">Michael R. Jordan</name><name sortKey="Mellors, John W" sort="Mellors, John W" uniqKey="Mellors J" first="John W." last="Mellors">John W. Mellors</name><name sortKey="Parkin, Neil T" sort="Parkin, Neil T" uniqKey="Parkin N" first="Neil T." last="Parkin">Neil T. Parkin</name></country><country name="Afrique du Sud"><noRegion><name sortKey="Wallis, Carole L" sort="Wallis, Carole L" uniqKey="Wallis C" first="Carole L." last="Wallis">Carole L. Wallis</name></noRegion></country><country name="Suisse"><noRegion><name sortKey="Bertagnolio, Silvia" sort="Bertagnolio, Silvia" uniqKey="Bertagnolio S" first="Silvia" last="Bertagnolio">Silvia Bertagnolio</name></noRegion></country><country name="Canada"><noRegion><name sortKey="Harrigan, P Richard" sort="Harrigan, P Richard" uniqKey="Harrigan P" first="P. Richard" last="Harrigan">P. 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