Mechanism of allosteric inhibition of HIV-1 reverse transcriptase revealed by single-molecule and ensemble fluorescence
Identifieur interne : 002293 ( Main/Merge ); précédent : 002292; suivant : 002294Mechanism of allosteric inhibition of HIV-1 reverse transcriptase revealed by single-molecule and ensemble fluorescence
Auteurs : Grant D. Schauer [États-Unis] ; Kelly D. Huber [États-Unis] ; Sanford H. Leuba [États-Unis] ; Nicolas Sluis-Cremer [États-Unis]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 2014.
Descripteurs français
- KwdFr :
- Amorces ADN, Benzoxazines (pharmacologie), Désoxyribonucléotides (métabolisme), Inhibiteurs de la transcriptase inverse (pharmacologie), Matrices (génétique), Mutation, Polarisation de fluorescence, Régulation allostérique, Sous-unités de protéines (), Transcriptase inverse du VIH (), Transcriptase inverse du VIH (antagonistes et inhibiteurs), Transcriptase inverse du VIH (génétique), Transcriptase inverse du VIH (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Transcriptase inverse du VIH.
- génétique : Transcriptase inverse du VIH.
- métabolisme : Désoxyribonucléotides, Transcriptase inverse du VIH.
- pharmacologie : Benzoxazines, Inhibiteurs de la transcriptase inverse.
- Amorces ADN, Matrices (génétique), Mutation, Polarisation de fluorescence, Régulation allostérique, Sous-unités de protéines, Transcriptase inverse du VIH.
English descriptors
- KwdEn :
- Allosteric Regulation, Benzoxazines (pharmacology), DNA Primers, Deoxyribonucleotides (metabolism), Fluorescence Polarization, HIV Reverse Transcriptase (antagonists & inhibitors), HIV Reverse Transcriptase (chemistry), HIV Reverse Transcriptase (genetics), HIV Reverse Transcriptase (metabolism), Mutation, Protein Subunits (chemistry), Reverse Transcriptase Inhibitors (pharmacology), Templates, Genetic.
- MESH :
- chemical , antagonists & inhibitors : HIV Reverse Transcriptase.
- chemical , chemistry : HIV Reverse Transcriptase, Protein Subunits.
- chemical , genetics : HIV Reverse Transcriptase.
- chemical , metabolism : Deoxyribonucleotides, HIV Reverse Transcriptase.
- chemical , pharmacology : Benzoxazines, Reverse Transcriptase Inhibitors.
- Allosteric Regulation, DNA Primers, Fluorescence Polarization, Mutation, Templates, Genetic.
Abstract
Non-nucleoside reverse transcriptase (RT) inhibitors (NNRTIs) are routinely used to treat HIV-1 infection, yet their mechanism of action remains unclear despite intensive investigation. In this study, we developed complementary single-molecule fluorescence and ensemble fluorescence anisotropy approaches to discover how NNRTIs modulate the intra-molecular conformational changes and inter-molecular dynamics of RT-template/primer (T/P) and RT–T/P–dNTP complexes. We found that NNRTI binding to RT induces opening of the fingers and thumb subdomains, which increases the dynamic sliding motion of the enzyme on the T/P and reduces dNTP binding affinity. Further, efavirenz promotes formation of the E138-K101 salt bridge between the p51 and p66 subunits of RT, which contributes to opening of the thumb/fingers subdomains. Engineering a more polar salt bridge between p51 and p66 resulted in even greater increases in the thumb/fingers opening, RT sliding, dNTP binding disruption and
Url:
DOI: 10.1093/nar/gku819
PubMed: 25232099
PubMed Central: 4191400
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type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Sluis Cremer, Nicolas" sort="Sluis Cremer, Nicolas" uniqKey="Sluis Cremer N" first="Nicolas" last="Sluis-Cremer">Nicolas Sluis-Cremer</name><affiliation wicri:level="2"><nlm:aff id="AFF3">Department of Medicine, Division of Infectious Diseases, University of Pittsburgh School of Medicine, Scaife Hall, 3550 Terrace Street, Pittsburgh, PA 15261, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Division of Infectious Diseases, University of Pittsburgh School of Medicine, Scaife Hall, 3550 Terrace Street, Pittsburgh, PA 15261</wicri:regionArea><placeName><region type="state">Pennsylvanie</region></placeName></affiliation></author></analytic><series><title level="j">Nucleic Acids Research</title><idno type="ISSN">0305-1048</idno><idno type="eISSN">1362-4962</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Regulation</term><term>Benzoxazines (pharmacology)</term><term>DNA Primers</term><term>Deoxyribonucleotides (metabolism)</term><term>Fluorescence Polarization</term><term>HIV Reverse Transcriptase (antagonists & inhibitors)</term><term>HIV Reverse Transcriptase (chemistry)</term><term>HIV Reverse Transcriptase (genetics)</term><term>HIV Reverse Transcriptase (metabolism)</term><term>Mutation</term><term>Protein Subunits (chemistry)</term><term>Reverse Transcriptase Inhibitors (pharmacology)</term><term>Templates, Genetic</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN</term><term>Benzoxazines (pharmacologie)</term><term>Désoxyribonucléotides (métabolisme)</term><term>Inhibiteurs de la transcriptase inverse (pharmacologie)</term><term>Matrices (génétique)</term><term>Mutation</term><term>Polarisation de fluorescence</term><term>Régulation allostérique</term><term>Sous-unités de protéines ()</term><term>Transcriptase inverse du VIH ()</term><term>Transcriptase inverse du VIH (antagonistes et inhibiteurs)</term><term>Transcriptase inverse du VIH (génétique)</term><term>Transcriptase inverse du VIH (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>HIV Reverse Transcriptase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>HIV Reverse Transcriptase</term><term>Protein Subunits</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>Deoxyribonucleotides</term><term>HIV Reverse Transcriptase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Benzoxazines</term><term>Reverse Transcriptase Inhibitors</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Transcriptase inverse du VIH</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Transcriptase inverse du VIH</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Désoxyribonucléotides</term><term>Transcriptase inverse du VIH</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Benzoxazines</term><term>Inhibiteurs de la transcriptase inverse</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Allosteric Regulation</term><term>DNA Primers</term><term>Fluorescence Polarization</term><term>Mutation</term><term>Templates, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Matrices (génétique)</term><term>Mutation</term><term>Polarisation de fluorescence</term><term>Régulation allostérique</term><term>Sous-unités de protéines</term><term>Transcriptase inverse du VIH</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Non-nucleoside reverse transcriptase (RT) inhibitors (NNRTIs) are routinely used to treat HIV-1 infection, yet their mechanism of action remains unclear despite intensive investigation. In this study, we developed complementary single-molecule fluorescence and ensemble fluorescence anisotropy approaches to discover how NNRTIs modulate the intra-molecular conformational changes and inter-molecular dynamics of RT-template/primer (T/P) and RT–T/P–dNTP complexes. We found that NNRTI binding to RT induces opening of the fingers and thumb subdomains, which increases the dynamic sliding motion of the enzyme on the T/P and reduces dNTP binding affinity. Further, efavirenz promotes formation of the E138-K101 salt bridge between the p51 and p66 subunits of RT, which contributes to opening of the thumb/fingers subdomains. Engineering a more polar salt bridge between p51 and p66 resulted in even greater increases in the thumb/fingers opening, RT sliding, dNTP binding disruption and <italic>in vitro</italic> and <italic>in vivo</italic> RT inhibition than were observed with wild-type RT. We also observed that K103N, a clinically relevant NNRTI resistance mutation, does not prevent binding between efavirenz and RT-T/P but instead allows formation of a stable and productive RT–T/P–dNTP complex, possibly through disruption of the E138-K101 salt bridge. Collectively, these data describe unique structure–activity–resistance relationships that could be exploited for drug development.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Di Marzo Veronese, F" uniqKey="Di Marzo Veronese F">F. di Marzo Veronese</name></author><author><name sortKey="Copeland, T D" uniqKey="Copeland T">T.D. Copeland</name></author><author><name sortKey="Devico, A L" uniqKey="Devico A">A.L. DeVico</name></author><author><name sortKey="Rahman, R" uniqKey="Rahman R">R. Rahman</name></author><author><name sortKey="Oroszlan, S" uniqKey="Oroszlan S">S. Oroszlan</name></author><author><name sortKey="Gallo, R C" uniqKey="Gallo R">R.C. 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Ehteshami</name></author><author><name sortKey="Gotte, M" uniqKey="Gotte M">M. Götte</name></author><author><name sortKey="Cosa, G" uniqKey="Cosa G">G. Cosa</name></author></analytic></biblStruct></listBibl></div1></back></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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