Elucidating molecular interactions of L-nucleotides with HIV-1 reverse transcriptase and mechanism of M184V-caused drug resistance.
Identifieur interne : 000153 ( Main/Exploration ); précédent : 000152; suivant : 000154Elucidating molecular interactions of L-nucleotides with HIV-1 reverse transcriptase and mechanism of M184V-caused drug resistance.
Auteurs : Magdeleine Hung [États-Unis] ; E John Tokarsky [États-Unis] ; Leanna Lagpacan [États-Unis] ; Lijun Zhang [États-Unis] ; Zucai Suo [États-Unis] ; Eric B. Lansdon [États-Unis]Source :
- Communications biology [ 2399-3642 ] ; 2019.
Descripteurs français
- KwdFr :
- Allèles (MeSH), Bases de données génétiques (MeSH), Humains (MeSH), Infections à VIH (traitement médicamenteux), Infections à VIH (virologie), Inhibiteurs de la transcriptase inverse (composition chimique), Inhibiteurs de la transcriptase inverse (pharmacologie), Mutation (MeSH), Nucléotides (composition chimique), Nucléotides (pharmacologie), Résistance virale aux médicaments (MeSH), Substitution d'acide aminé (MeSH), Tests de sensibilité microbienne (MeSH), Transcriptase inverse du VIH (antagonistes et inhibiteurs), Transcriptase inverse du VIH (composition chimique), Transcriptase inverse du VIH (génétique), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (effets des médicaments et des substances chimiques), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (enzymologie), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique).
- MESH :
- antagonistes et inhibiteurs : Transcriptase inverse du VIH.
- composition chimique : Inhibiteurs de la transcriptase inverse, Nucléotides, Transcriptase inverse du VIH.
- effets des médicaments et des substances chimiques : VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- 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).
- pharmacologie : Inhibiteurs de la transcriptase inverse, Nucléotides.
- traitement médicamenteux : Infections à VIH.
- virologie : Infections à VIH.
- Allèles, Bases de données génétiques, Humains, Mutation, Résistance virale aux médicaments, Substitution d'acide aminé, Tests de sensibilité microbienne.
English descriptors
- KwdEn :
- Alleles (MeSH), Amino Acid Substitution (MeSH), Databases, Genetic (MeSH), Drug Resistance, Viral (MeSH), HIV Infections (drug therapy), HIV Infections (virology), HIV Reverse Transcriptase (antagonists & inhibitors), HIV Reverse Transcriptase (chemistry), HIV Reverse Transcriptase (genetics), HIV-1 (drug effects), HIV-1 (enzymology), HIV-1 (genetics), Humans (MeSH), Microbial Sensitivity Tests (MeSH), Mutation (MeSH), Nucleotides (chemistry), Nucleotides (pharmacology), Reverse Transcriptase Inhibitors (chemistry), Reverse Transcriptase Inhibitors (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : HIV Reverse Transcriptase.
- chemical , chemistry : HIV Reverse Transcriptase, Nucleotides, Reverse Transcriptase Inhibitors.
- drug effects : HIV-1.
- drug therapy : HIV Infections.
- enzymology : HIV-1.
- chemical , genetics : HIV Reverse Transcriptase, HIV-1.
- chemical , pharmacology : Nucleotides, Reverse Transcriptase Inhibitors.
- virology : HIV Infections.
- Alleles, Amino Acid Substitution, Databases, Genetic, Drug Resistance, Viral, Humans, Microbial Sensitivity Tests, Mutation.
Abstract
Emtricitabine (FTC) and lamivudine (3TC), containing an oxathiolane ring with unnatural (-)-stereochemistry, are widely used nucleoside reverse transcriptase inhibitors (NRTIs) in anti-HIV therapy. Treatment with FTC or 3TC primarily selects for the HIV-1 RT M184V/I resistance mutations. Here we provide a comprehensive kinetic and structural basis for inhibiting HIV-1 RT by (-)-FTC-TP and (-)-3TC-TP and drug resistance by M184V. (-)-FTC-TP and (-)-3TC-TP have higher binding affinities (1/Kd) for wild-type RT but slower incorporation rates than dCTP. HIV-1 RT ternary crystal structures with (-)-FTC-TP and (-)-3TC-TP corroborate kinetic results demonstrating that their oxathiolane sulfur orients toward the DNA primer 3'-terminus and their triphosphate exists in two different binding conformations. M184V RT displays greater (>200-fold) Kd for the L-nucleotides and moderately higher (>9-fold) Kd for the D-isomers compared to dCTP. The M184V RT structure illustrates how the mutation repositions the oxathiolane of (-)-FTC-TP and shifts its triphosphate into a non-productive conformation.
DOI: 10.1038/s42003-019-0706-x
PubMed: 31872074
PubMed Central: PMC6910994
Affiliations:
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Transcriptase (genetics)</term><term>HIV-1 (drug effects)</term><term>HIV-1 (enzymology)</term><term>HIV-1 (genetics)</term><term>Humans (MeSH)</term><term>Microbial Sensitivity Tests (MeSH)</term><term>Mutation (MeSH)</term><term>Nucleotides (chemistry)</term><term>Nucleotides (pharmacology)</term><term>Reverse Transcriptase Inhibitors (chemistry)</term><term>Reverse Transcriptase Inhibitors (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Allèles (MeSH)</term><term>Bases de données génétiques (MeSH)</term><term>Humains (MeSH)</term><term>Infections à VIH (traitement médicamenteux)</term><term>Infections à VIH (virologie)</term><term>Inhibiteurs de la transcriptase inverse (composition chimique)</term><term>Inhibiteurs de la transcriptase inverse (pharmacologie)</term><term>Mutation (MeSH)</term><term>Nucléotides (composition chimique)</term><term>Nucléotides (pharmacologie)</term><term>Résistance virale aux médicaments (MeSH)</term><term>Substitution d'acide aminé (MeSH)</term><term>Tests de sensibilité microbienne (MeSH)</term><term>Transcriptase inverse du VIH (antagonistes et inhibiteurs)</term><term>Transcriptase inverse du VIH (composition chimique)</term><term>Transcriptase inverse du VIH (génétique)</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (effets des médicaments et des substances chimiques)</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="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>Nucleotides</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="composition chimique" xml:lang="fr"><term>Inhibiteurs de la transcriptase inverse</term><term>Nucléotides</term><term>Transcriptase inverse du VIH</term></keywords><keywords scheme="MESH" qualifier="drug effects" 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="effets des médicaments et des substances chimiques" xml:lang="fr"><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</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" type="chemical" qualifier="genetics" xml:lang="en"><term>HIV Reverse Transcriptase</term><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="pharmacologie" xml:lang="fr"><term>Inhibiteurs de la transcriptase inverse</term><term>Nucléotides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Nucleotides</term><term>Reverse Transcriptase Inhibitors</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>Alleles</term><term>Amino Acid Substitution</term><term>Databases, Genetic</term><term>Drug Resistance, Viral</term><term>Humans</term><term>Microbial Sensitivity Tests</term><term>Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Allèles</term><term>Bases de données génétiques</term><term>Humains</term><term>Mutation</term><term>Résistance virale aux médicaments</term><term>Substitution d'acide aminé</term><term>Tests de sensibilité microbienne</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Emtricitabine (FTC) and lamivudine (3TC), containing an oxathiolane ring with unnatural (-)-stereochemistry, are widely used nucleoside reverse transcriptase inhibitors (NRTIs) in anti-HIV therapy. Treatment with FTC or 3TC primarily selects for the HIV-1 RT M184V/I resistance mutations. Here we provide a comprehensive kinetic and structural basis for inhibiting HIV-1 RT by (-)-FTC-TP and (-)-3TC-TP and drug resistance by M184V. (-)-FTC-TP and (-)-3TC-TP have higher binding affinities (1/<i>K</i><sub>d</sub>) for wild-type RT but slower incorporation rates than dCTP. HIV-1 RT ternary crystal structures with (-)-FTC-TP and (-)-3TC-TP corroborate kinetic results demonstrating that their oxathiolane sulfur orients toward the DNA primer 3'-terminus and their triphosphate exists in two different binding conformations. M184V RT displays greater (>200-fold) <i>K</i><sub>d</sub> for the <i>L</i>-nucleotides and moderately higher (>9-fold) <i>K</i><sub><i>d</i></sub> for the <i>D</i>-isomers compared to dCTP. The M184V RT structure illustrates how the mutation repositions the oxathiolane of (-)-FTC-TP and shifts its triphosphate into a non-productive conformation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31872074</PMID><DateCompleted><Year>2020</Year><Month>07</Month><Day>06</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>06</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">2399-3642</ISSN><JournalIssue CitedMedium="Internet"><Volume>2</Volume><PubDate><Year>2019</Year></PubDate></JournalIssue><Title>Communications biology</Title><ISOAbbreviation>Commun Biol</ISOAbbreviation></Journal><ArticleTitle>Elucidating molecular interactions of <i>L</i>-nucleotides with HIV-1 reverse transcriptase and mechanism of M184V-caused drug resistance.</ArticleTitle><Pagination><MedlinePgn>469</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s42003-019-0706-x</ELocationID><Abstract><AbstractText>Emtricitabine (FTC) and lamivudine (3TC), containing an oxathiolane ring with unnatural (-)-stereochemistry, are widely used nucleoside reverse transcriptase inhibitors (NRTIs) in anti-HIV therapy. Treatment with FTC or 3TC primarily selects for the HIV-1 RT M184V/I resistance mutations. Here we provide a comprehensive kinetic and structural basis for inhibiting HIV-1 RT by (-)-FTC-TP and (-)-3TC-TP and drug resistance by M184V. (-)-FTC-TP and (-)-3TC-TP have higher binding affinities (1/<i>K</i><sub>d</sub>) for wild-type RT but slower incorporation rates than dCTP. HIV-1 RT ternary crystal structures with (-)-FTC-TP and (-)-3TC-TP corroborate kinetic results demonstrating that their oxathiolane sulfur orients toward the DNA primer 3'-terminus and their triphosphate exists in two different binding conformations. M184V RT displays greater (>200-fold) <i>K</i><sub>d</sub> for the <i>L</i>-nucleotides and moderately higher (>9-fold) <i>K</i><sub><i>d</i></sub> for the <i>D</i>-isomers compared to dCTP. The M184V RT structure illustrates how the mutation repositions the oxathiolane of (-)-FTC-TP and shifts its triphosphate into a non-productive conformation.</AbstractText><CopyrightInformation>© The Author(s) 2019.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y" EqualContrib="Y"><LastName>Hung</LastName><ForeName>Magdeleine</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>1Gilead Sciences, Inc., 333 Lakeside Dr., Foster City, CA 94404 USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Tokarsky</LastName><ForeName>E John</ForeName><Initials>EJ</Initials><AffiliationInfo><Affiliation>2The Ohio State Biophysics Program, The Ohio State University, Columbus, OH 43210 USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lagpacan</LastName><ForeName>Leanna</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>1Gilead Sciences, Inc., 333 Lakeside Dr., Foster City, CA 94404 USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Lijun</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>1Gilead Sciences, Inc., 333 Lakeside Dr., Foster City, CA 94404 USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Suo</LastName><ForeName>Zucai</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>2The Ohio State Biophysics Program, The Ohio State University, Columbus, OH 43210 USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>3Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306 USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lansdon</LastName><ForeName>Eric B</ForeName><Initials>EB</Initials><Identifier Source="ORCID">0000-0001-9461-1475</Identifier><AffiliationInfo><Affiliation>1Gilead Sciences, Inc., 333 Lakeside Dr., Foster City, CA 94404 USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>S10 OD021832</GrantID><Acronym>OD</Acronym><Agency>NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>12</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Commun Biol</MedlineTA><NlmUniqueID>101719179</NlmUniqueID><ISSNLinking>2399-3642</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009711">Nucleotides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018894">Reverse Transcriptase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.-</RegistryNumber><NameOfSubstance UI="C514824">reverse transcriptase, Human immunodeficiency virus 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.49</RegistryNumber><NameOfSubstance UI="D054303">HIV Reverse Transcriptase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000483" MajorTopicYN="N">Alleles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D030541" MajorTopicYN="N">Databases, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D024882" MajorTopicYN="Y">Drug Resistance, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015658" MajorTopicYN="N">HIV Infections</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054303" MajorTopicYN="N">HIV Reverse Transcriptase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015497" MajorTopicYN="N">HIV-1</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008826" MajorTopicYN="N">Microbial Sensitivity Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009711" MajorTopicYN="N">Nucleotides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018894" MajorTopicYN="N">Reverse Transcriptase Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Enzyme mechanisms</Keyword><Keyword MajorTopicYN="Y">HIV infections</Keyword><Keyword MajorTopicYN="Y">Pharmaceutics</Keyword><Keyword MajorTopicYN="Y">X-ray crystallography</Keyword></KeywordList><CoiStatement>Competing interestsM.H., L.L., L.Z. and E.B.L. are or were employed by Gilead Sciences at the time of data generation. 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