Mapping the Specific Amino Acid Residues That Make Hamster DPP4 Functional as a Receptor for Middle East Respiratory Syndrome Coronavirus.
Identifieur interne : 001191 ( PubMed/Corpus ); précédent : 001190; suivant : 001192Mapping the Specific Amino Acid Residues That Make Hamster DPP4 Functional as a Receptor for Middle East Respiratory Syndrome Coronavirus.
Auteurs : Neeltje Van Doremalen ; Kerri L. Miazgowicz ; Vincent J. MunsterSource :
- Journal of virology [ 1098-5514 ] ; 2016.
English descriptors
- KwdEn :
- Amino Acids (chemistry), Amino Acids (metabolism), Animals, Coronavirus Infections (virology), Cricetinae, Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (metabolism), Disease Models, Animal, Humans, Middle East Respiratory Syndrome Coronavirus (genetics), Middle East Respiratory Syndrome Coronavirus (metabolism), Middle East Respiratory Syndrome Coronavirus (physiology), Models, Molecular, Protein Binding, Receptors, Virus (chemistry), Receptors, Virus (metabolism), Virus Internalization, Virus Replication.
- MESH :
- chemical , chemistry : Amino Acids, Dipeptidyl Peptidase 4, Receptors, Virus.
- chemical , metabolism : Amino Acids, Dipeptidyl Peptidase 4, Receptors, Virus.
- genetics : Middle East Respiratory Syndrome Coronavirus.
- metabolism : Middle East Respiratory Syndrome Coronavirus.
- physiology : Middle East Respiratory Syndrome Coronavirus.
- virology : Coronavirus Infections.
- Animals, Cricetinae, Disease Models, Animal, Humans, Models, Molecular, Protein Binding, Virus Internalization, Virus Replication.
Abstract
The novel emerging coronavirus Middle East respiratory syndrome coronavirus (MERS-CoV) binds to its receptor, dipeptidyl peptidase 4 (DPP4), via 14 interacting amino acids. We previously showed that if the five interacting amino acids which differ between hamster and human DPP4 are changed to the residues found in human DPP4, hamster DPP4 does act as a receptor. Here, we show that the functionality of hamster DPP4 as a receptor is severely decreased if less than 4 out of 5 amino acids are changed.
DOI: 10.1128/JVI.03267-15
PubMed: 27030263
Links to Exploration step
pubmed:27030263Le document en format XML
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Miazgowicz</name><affiliation><nlm:affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Munster, Vincent J" sort="Munster, Vincent J" uniqKey="Munster V" first="Vincent J" last="Munster">Vincent J. Munster</name><affiliation><nlm:affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA vincent.munster@nih.gov.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:27030263</idno><idno type="pmid">27030263</idno><idno type="doi">10.1128/JVI.03267-15</idno><idno type="wicri:Area/PubMed/Corpus">001191</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001191</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Mapping the Specific Amino Acid Residues That Make Hamster DPP4 Functional as a Receptor for Middle East Respiratory Syndrome Coronavirus.</title><author><name sortKey="Van Doremalen, Neeltje" sort="Van Doremalen, Neeltje" uniqKey="Van Doremalen N" first="Neeltje" last="Van Doremalen">Neeltje Van Doremalen</name><affiliation><nlm:affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Miazgowicz, Kerri L" sort="Miazgowicz, Kerri L" uniqKey="Miazgowicz K" first="Kerri L" last="Miazgowicz">Kerri L. Miazgowicz</name><affiliation><nlm:affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Munster, Vincent J" sort="Munster, Vincent J" uniqKey="Munster V" first="Vincent J" last="Munster">Vincent J. Munster</name><affiliation><nlm:affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA vincent.munster@nih.gov.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (chemistry)</term><term>Amino Acids (metabolism)</term><term>Animals</term><term>Coronavirus Infections (virology)</term><term>Cricetinae</term><term>Dipeptidyl Peptidase 4 (chemistry)</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Disease Models, Animal</term><term>Humans</term><term>Middle East Respiratory Syndrome Coronavirus (genetics)</term><term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term><term>Middle East Respiratory Syndrome Coronavirus (physiology)</term><term>Models, Molecular</term><term>Protein Binding</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (metabolism)</term><term>Virus Internalization</term><term>Virus Replication</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Dipeptidyl Peptidase 4</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acids</term><term>Dipeptidyl Peptidase 4</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cricetinae</term><term>Disease Models, Animal</term><term>Humans</term><term>Models, Molecular</term><term>Protein Binding</term><term>Virus Internalization</term><term>Virus Replication</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The novel emerging coronavirus Middle East respiratory syndrome coronavirus (MERS-CoV) binds to its receptor, dipeptidyl peptidase 4 (DPP4), via 14 interacting amino acids. We previously showed that if the five interacting amino acids which differ between hamster and human DPP4 are changed to the residues found in human DPP4, hamster DPP4 does act as a receptor. Here, we show that the functionality of hamster DPP4 as a receptor is severely decreased if less than 4 out of 5 amino acids are changed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27030263</PMID><DateCompleted><Year>2017</Year><Month>04</Month><Day>28</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-Print"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>90</Volume><Issue>11</Issue><PubDate><Year>2016</Year><Month>06</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Mapping the Specific Amino Acid Residues That Make Hamster DPP4 Functional as a Receptor for Middle East Respiratory Syndrome Coronavirus.</ArticleTitle><Pagination><MedlinePgn>5499-5502</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.03267-15</ELocationID><Abstract><AbstractText Label="UNLABELLED">The novel emerging coronavirus Middle East respiratory syndrome coronavirus (MERS-CoV) binds to its receptor, dipeptidyl peptidase 4 (DPP4), via 14 interacting amino acids. We previously showed that if the five interacting amino acids which differ between hamster and human DPP4 are changed to the residues found in human DPP4, hamster DPP4 does act as a receptor. Here, we show that the functionality of hamster DPP4 as a receptor is severely decreased if less than 4 out of 5 amino acids are changed.</AbstractText><AbstractText Label="IMPORTANCE">The novel emerging coronavirus MERS-CoV has infected >1,600 people worldwide, and the case fatality rate is ∼36%. In this study, we show that by changing 4 amino acids in hamster DPP4, this protein functions as a receptor for MERS-CoV. This work is vital in the development of new small-animal models, which will broaden our understanding of MERS-CoV and be instrumental in the development of countermeasures.</AbstractText><CopyrightInformation>Copyright © 2016, American Society for Microbiology. All Rights Reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>van Doremalen</LastName><ForeName>Neeltje</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Miazgowicz</LastName><ForeName>Kerri L</ForeName><Initials>KL</Initials><AffiliationInfo><Affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Munster</LastName><ForeName>Vincent J</ForeName><Initials>VJ</Initials><AffiliationInfo><Affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA vincent.munster@nih.gov.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052060">Research Support, N.I.H., Intramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>05</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.14.5</RegistryNumber><NameOfSubstance UI="C042807">DPP4 protein, 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