Adaptive Evolution of MERS-CoV to Species Variation in DPP4
Identifieur interne : 000A75 ( Main/Exploration ); précédent : 000A74; suivant : 000A76Adaptive Evolution of MERS-CoV to Species Variation in DPP4
Auteurs : Michael Letko [États-Unis] ; Kerri Miazgowicz [États-Unis] ; Rebekah Mcminn [États-Unis] ; Stephanie N. Seifert [États-Unis] ; Isabel Sola [Espagne] ; Luis Enjuanes [Espagne] ; Aaron Carmody [États-Unis] ; Neeltje Van Doremalen [États-Unis] ; Vincent Munster [États-Unis]Source :
- Cell Reports [ 2211-1247 ] ; 2018.
Descripteurs français
- KwdFr :
- Adaptation physiologique, Alignement de séquences, Animaux, Cellules Vero, Chiroptera, Coronavirus du syndrome respiratoire du Moyen-Orient (génétique), Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme), Cricetulus, Dipeptidyl peptidase 4 (), Dipeptidyl peptidase 4 (génétique), Dipeptidyl peptidase 4 (métabolisme), Expression des gènes, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Interactions hôte-pathogène (génétique), Liaison aux protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Mutation, Pénétration virale, Récepteurs viraux (), Récepteurs viraux (génétique), Récepteurs viraux (métabolisme), Similitude de séquences d'acides aminés, Sites de fixation, Spécificité d'hôte, Structure en brin bêta, Structure en hélice alpha, Séquence d'acides aminés.
- MESH :
- génétique : Coronavirus du syndrome respiratoire du Moyen-Orient, Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Interactions hôte-pathogène, Récepteurs viraux.
- métabolisme : Coronavirus du syndrome respiratoire du Moyen-Orient, Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Récepteurs viraux.
- Adaptation physiologique, Alignement de séquences, Animaux, Cellules Vero, Chiroptera, Cricetulus, Dipeptidyl peptidase 4, Expression des gènes, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Mutation, Pénétration virale, Récepteurs viraux, Similitude de séquences d'acides aminés, Sites de fixation, Spécificité d'hôte, Structure en brin bêta, Structure en hélice alpha, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Adaptation, Physiological, Amino Acid Sequence, Animals, Binding Sites, Biological Coevolution, Chiroptera, Chlorocebus aethiops, Cricetulus, Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (metabolism), Gene Expression, Host Specificity, Host-Pathogen Interactions (genetics), Humans, Middle East Respiratory Syndrome Coronavirus (genetics), Middle East Respiratory Syndrome Coronavirus (metabolism), Models, Molecular, Mutation, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Receptors, Virus (chemistry), Receptors, Virus (genetics), Receptors, Virus (metabolism), Sequence Alignment, Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Vero Cells, Virus Internalization.
- MESH :
- chemical , chemistry : Dipeptidyl Peptidase 4, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemical , genetics : Dipeptidyl Peptidase 4, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Dipeptidyl Peptidase 4, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- genetics : Host-Pathogen Interactions, Middle East Respiratory Syndrome Coronavirus.
- metabolism : Middle East Respiratory Syndrome Coronavirus.
- Adaptation, Physiological, Amino Acid Sequence, Animals, Binding Sites, Biological Coevolution, Chiroptera, Chlorocebus aethiops, Cricetulus, Gene Expression, Host Specificity, Humans, Models, Molecular, Mutation, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Sequence Alignment, Sequence Homology, Amino Acid, Vero Cells, Virus Internalization.
Abstract
Middle East Respiratory Syndrome Coronavirus (MERS-CoV) likely originated in bats and passed to humans through dromedary camels; however, the genetic mechanisms underlying cross-species adaptation remain poorly understood. Variation in the host receptor, dipeptidyl peptidase 4 (DPP4), can block the interaction with the MERS-CoV spike protein and form a species barrier to infection. To better understand the species adaptability of MERS-CoV, we identified a suboptimal species-derived variant of DPP4 to study viral adaption. Passaging virus on cells expressing this DPP4 variant led to accumulation of mutations in the viral spike which increased replication. Parallel passages revealed distinct paths of viral adaptation to the same DPP4 variant. Structural analysis and functional assays showed that these mutations enhanced viral entry with suboptimal DPP4 by altering the surface charge of spike. These findings demonstrate that MERS-CoV spike can utilize multiple paths to rapidly adapt to novel species variation in DPP4.
Url:
DOI: 10.1016/j.celrep.2018.07.045
PubMed: 30110630
PubMed Central: 7104223
Affiliations:
- Espagne, États-Unis
- Colorado, Communauté de Madrid, Géorgie (États-Unis), Montana
- Madrid
- Université autonome de Madrid
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Le document en format XML
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Hamilton, MT 59840, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="aff3">Department of Infectious Diseases, College of Veterinary Medicine, The University of Georgia, Athens, GA 30602, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Infectious Diseases, College of Veterinary Medicine, The University of Georgia, Athens, GA 30602</wicri:regionArea><placeName><region type="state">Géorgie (États-Unis)</region></placeName></affiliation></author><author><name sortKey="Mcminn, Rebekah" sort="Mcminn, Rebekah" uniqKey="Mcminn R" first="Rebekah" last="Mcminn">Rebekah Mcminn</name><affiliation wicri:level="2"><nlm:aff id="aff1">Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="aff4">Department of Microbiology, Immunology, & Pathology, Colorado State University, Fort Collins, CO 80523, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology, Immunology, & Pathology, Colorado State University, Fort Collins, CO 80523</wicri:regionArea><placeName><region type="state">Colorado</region></placeName></affiliation></author><author><name sortKey="Seifert, Stephanie N" sort="Seifert, Stephanie N" uniqKey="Seifert S" first="Stephanie N." last="Seifert">Stephanie N. Seifert</name><affiliation wicri:level="2"><nlm:aff id="aff1">Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></author><author><name sortKey="Sola, Isabel" sort="Sola, Isabel" uniqKey="Sola I" first="Isabel" last="Sola">Isabel Sola</name><affiliation wicri:level="4"><nlm:aff id="aff5">Department of Molecular and Cell Biology, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Cantoblanco, Madrid, Spain</nlm:aff><country xml:lang="fr">Espagne</country><wicri:regionArea>Department of Molecular and Cell Biology, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Cantoblanco, Madrid</wicri:regionArea><placeName><settlement type="city">Madrid</settlement><region nuts="2" type="region">Communauté de Madrid</region></placeName><orgName type="university">Université autonome de Madrid</orgName></affiliation></author><author><name sortKey="Enjuanes, Luis" sort="Enjuanes, Luis" uniqKey="Enjuanes L" first="Luis" last="Enjuanes">Luis Enjuanes</name><affiliation wicri:level="4"><nlm:aff id="aff5">Department of Molecular and Cell Biology, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Cantoblanco, Madrid, Spain</nlm:aff><country xml:lang="fr">Espagne</country><wicri:regionArea>Department of Molecular and Cell Biology, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Cantoblanco, Madrid</wicri:regionArea><placeName><settlement type="city">Madrid</settlement><region nuts="2" type="region">Communauté de Madrid</region></placeName><orgName type="university">Université autonome de Madrid</orgName></affiliation></author><author><name sortKey="Carmody, Aaron" sort="Carmody, Aaron" uniqKey="Carmody A" first="Aaron" last="Carmody">Aaron Carmody</name><affiliation wicri:level="2"><nlm:aff id="aff2">Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></author><author><name sortKey="Van Doremalen, Neeltje" sort="Van Doremalen, Neeltje" uniqKey="Van Doremalen N" first="Neeltje" last="Van Doremalen">Neeltje Van Doremalen</name><affiliation wicri:level="2"><nlm:aff id="aff1">Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></author><author><name sortKey="Munster, Vincent" sort="Munster, Vincent" uniqKey="Munster V" first="Vincent" last="Munster">Vincent Munster</name><affiliation wicri:level="2"><nlm:aff id="aff1">Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Virology, Division of 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du Moyen-Orient (génétique)</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme)</term><term>Cricetulus</term><term>Dipeptidyl peptidase 4 ()</term><term>Dipeptidyl peptidase 4 (génétique)</term><term>Dipeptidyl peptidase 4 (métabolisme)</term><term>Expression des gènes</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Glycoprotéine de spicule des coronavirus (génétique)</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Interactions hôte-pathogène (génétique)</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutation</term><term>Pénétration virale</term><term>Récepteurs viraux ()</term><term>Récepteurs viraux (génétique)</term><term>Récepteurs viraux (métabolisme)</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Spécificité d'hôte</term><term>Structure en brin bêta</term><term>Structure en hélice alpha</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Receptors, Virus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Receptors, Virus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Receptors, Virus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Host-Pathogen Interactions</term><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term><term>Dipeptidyl peptidase 4</term><term>Glycoprotéine de spicule des coronavirus</term><term>Interactions hôte-pathogène</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term><term>Dipeptidyl peptidase 4</term><term>Glycoprotéine de spicule des coronavirus</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adaptation, Physiological</term><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Biological Coevolution</term><term>Chiroptera</term><term>Chlorocebus aethiops</term><term>Cricetulus</term><term>Gene Expression</term><term>Host Specificity</term><term>Humans</term><term>Models, Molecular</term><term>Mutation</term><term>Protein Binding</term><term>Protein Conformation, alpha-Helical</term><term>Protein Conformation, beta-Strand</term><term>Protein Interaction Domains and Motifs</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adaptation physiologique</term><term>Alignement de séquences</term><term>Animaux</term><term>Cellules Vero</term><term>Chiroptera</term><term>Cricetulus</term><term>Dipeptidyl peptidase 4</term><term>Expression des gènes</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutation</term><term>Pénétration virale</term><term>Récepteurs viraux</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Spécificité d'hôte</term><term>Structure en brin bêta</term><term>Structure en hélice alpha</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Summary</title><p>Middle East Respiratory Syndrome Coronavirus (MERS-CoV) likely originated in bats and passed to humans through dromedary camels; however, the genetic mechanisms underlying cross-species adaptation remain poorly understood. Variation in the host receptor, dipeptidyl peptidase 4 (DPP4), can block the interaction with the MERS-CoV spike protein and form a species barrier to infection. To better understand the species adaptability of MERS-CoV, we identified a suboptimal species-derived variant of DPP4 to study viral adaption. Passaging virus on cells expressing this DPP4 variant led to accumulation of mutations in the viral spike which increased replication. Parallel passages revealed distinct paths of viral adaptation to the same DPP4 variant. Structural analysis and functional assays showed that these mutations enhanced viral entry with suboptimal DPP4 by altering the surface charge of spike. These findings demonstrate that MERS-CoV spike can utilize multiple paths to rapidly adapt to novel species variation in DPP4.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Adney, D R" uniqKey="Adney D">D.R. 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Zaki</name></author><author><name sortKey="Van Boheemen, S" uniqKey="Van Boheemen S">S. van Boheemen</name></author><author><name sortKey="Bestebroer, T M" uniqKey="Bestebroer T">T.M. Bestebroer</name></author><author><name sortKey="Osterhaus, A D" uniqKey="Osterhaus A">A.D. Osterhaus</name></author><author><name sortKey="Fouchier, R A" uniqKey="Fouchier R">R.A. Fouchier</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Espagne</li><li>États-Unis</li></country><region><li>Colorado</li><li>Communauté de Madrid</li><li>Géorgie (États-Unis)</li><li>Montana</li></region><settlement><li>Madrid</li></settlement><orgName><li>Université autonome de Madrid</li></orgName></list><tree><country name="États-Unis"><region name="Montana"><name sortKey="Letko, Michael" sort="Letko, Michael" uniqKey="Letko M" first="Michael" last="Letko">Michael Letko</name></region><name sortKey="Carmody, Aaron" sort="Carmody, Aaron" uniqKey="Carmody A" first="Aaron" last="Carmody">Aaron Carmody</name><name sortKey="Mcminn, Rebekah" sort="Mcminn, Rebekah" uniqKey="Mcminn R" first="Rebekah" last="Mcminn">Rebekah Mcminn</name><name sortKey="Mcminn, Rebekah" sort="Mcminn, Rebekah" uniqKey="Mcminn R" first="Rebekah" last="Mcminn">Rebekah Mcminn</name><name sortKey="Miazgowicz, Kerri" sort="Miazgowicz, Kerri" uniqKey="Miazgowicz K" first="Kerri" last="Miazgowicz">Kerri Miazgowicz</name><name sortKey="Miazgowicz, Kerri" sort="Miazgowicz, Kerri" uniqKey="Miazgowicz K" first="Kerri" last="Miazgowicz">Kerri Miazgowicz</name><name sortKey="Munster, Vincent" sort="Munster, Vincent" uniqKey="Munster V" first="Vincent" last="Munster">Vincent Munster</name><name sortKey="Seifert, Stephanie N" sort="Seifert, Stephanie N" uniqKey="Seifert S" first="Stephanie N." last="Seifert">Stephanie N. Seifert</name><name sortKey="Van Doremalen, Neeltje" sort="Van Doremalen, Neeltje" uniqKey="Van Doremalen N" first="Neeltje" last="Van Doremalen">Neeltje Van Doremalen</name></country><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Sola, Isabel" sort="Sola, Isabel" uniqKey="Sola I" first="Isabel" last="Sola">Isabel Sola</name></region><name sortKey="Enjuanes, Luis" sort="Enjuanes, Luis" uniqKey="Enjuanes L" first="Luis" last="Enjuanes">Luis Enjuanes</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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