Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.
Identifieur interne : 001D55 ( Main/Exploration ); précédent : 001D54; suivant : 001D56Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.
Auteurs : V Stalin Raj [Pays-Bas] ; Saskia L. Smits ; Lisette B. Provacia ; Judith M A. Van Den Brand ; Lidewij Wiersma ; Werner J D. Ouwendijk ; Theo M. Bestebroer ; Monique I. Spronken ; Geert Van Amerongen ; Peter J M. Rottier ; Ron A M. Fouchier ; Berend Jan Bosch ; Albert D M E. Osterhaus ; Bart L. HaagmansSource :
- Journal of virology [ 1098-5514 ] ; 2014.
Descripteurs français
- KwdFr :
- Adenosine deaminase (génétique), Adenosine deaminase (métabolisme), Alignement de séquences, Animaux, Coronaviridae (génétique), Coronaviridae (physiologie), Dipeptidyl peptidase 4 (), Dipeptidyl peptidase 4 (génétique), Dipeptidyl peptidase 4 (métabolisme), Données de séquences moléculaires, Furets, Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Infections à Coronaviridae (enzymologie), Infections à Coronaviridae (virologie), Liaison aux protéines, Modèles animaux de maladie humaine, Pénétration virale, Récepteurs viraux (), Récepteurs viraux (génétique), Récepteurs viraux (métabolisme), Séquence d'acides aminés.
- MESH :
- enzymologie : Infections à Coronaviridae.
- génétique : Adenosine deaminase, Coronaviridae, Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Récepteurs viraux.
- métabolisme : Adenosine deaminase, Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Récepteurs viraux.
- physiologie : Coronaviridae.
- virologie : Infections à Coronaviridae.
- Alignement de séquences, Animaux, Dipeptidyl peptidase 4, Données de séquences moléculaires, Furets, Humains, Liaison aux protéines, Modèles animaux de maladie humaine, Pénétration virale, Récepteurs viraux, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Adenosine Deaminase (genetics), Adenosine Deaminase (metabolism), Amino Acid Sequence, Animals, Coronaviridae (genetics), Coronaviridae (physiology), Coronaviridae Infections (enzymology), Coronaviridae Infections (virology), Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (metabolism), Disease Models, Animal, Ferrets, Humans, Molecular Sequence Data, Protein Binding, Receptors, Virus (chemistry), Receptors, Virus (genetics), Receptors, Virus (metabolism), Sequence Alignment, Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Virus Internalization.
- MESH :
- chemical , chemistry : Dipeptidyl Peptidase 4, Receptors, Virus.
- chemical , genetics : Adenosine Deaminase, Dipeptidyl Peptidase 4, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Adenosine Deaminase, Dipeptidyl Peptidase 4, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- enzymology : Coronaviridae Infections.
- genetics : Coronaviridae.
- physiology : Coronaviridae.
- virology : Coronaviridae Infections.
- Amino Acid Sequence, Animals, Disease Models, Animal, Ferrets, Humans, Molecular Sequence Data, Protein Binding, Sequence Alignment, Virus Internalization.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) replicates in cells of different species using dipeptidyl peptidase 4 (DPP4) as a functional receptor. Here we show the resistance of ferrets to MERS-CoV infection and inability of ferret DDP4 to bind MERS-CoV. Site-directed mutagenesis of amino acids variable in ferret DPP4 thus revealed the functional human DPP4 virus binding site. Adenosine deaminase (ADA), a DPP4 binding protein, competed for virus binding, acting as a natural antagonist for MERS-CoV infection.
DOI: 10.1128/JVI.02935-13
PubMed: 24257613
Affiliations:
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Smits</name></author><author><name sortKey="Provacia, Lisette B" sort="Provacia, Lisette B" uniqKey="Provacia L" first="Lisette B" last="Provacia">Lisette B. Provacia</name></author><author><name sortKey="Van Den Brand, Judith M A" sort="Van Den Brand, Judith M A" uniqKey="Van Den Brand J" first="Judith M A" last="Van Den Brand">Judith M A. Van Den Brand</name></author><author><name sortKey="Wiersma, Lidewij" sort="Wiersma, Lidewij" uniqKey="Wiersma L" first="Lidewij" last="Wiersma">Lidewij Wiersma</name></author><author><name sortKey="Ouwendijk, Werner J D" sort="Ouwendijk, Werner J D" uniqKey="Ouwendijk W" first="Werner J D" last="Ouwendijk">Werner J D. Ouwendijk</name></author><author><name sortKey="Bestebroer, Theo M" sort="Bestebroer, Theo M" uniqKey="Bestebroer T" first="Theo M" last="Bestebroer">Theo M. Bestebroer</name></author><author><name sortKey="Spronken, Monique I" sort="Spronken, Monique I" uniqKey="Spronken M" first="Monique I" last="Spronken">Monique I. 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Here we show the resistance of ferrets to MERS-CoV infection and inability of ferret DDP4 to bind MERS-CoV. Site-directed mutagenesis of amino acids variable in ferret DPP4 thus revealed the functional human DPP4 virus binding site. Adenosine deaminase (ADA), a DPP4 binding protein, competed for virus binding, acting as a natural antagonist for MERS-CoV infection. </div></front></TEI><affiliations><list><country><li>Pays-Bas</li></country><region><li>Hollande-Méridionale</li></region><settlement><li>Rotterdam</li></settlement></list><tree><noCountry><name sortKey="Bestebroer, Theo M" sort="Bestebroer, Theo M" uniqKey="Bestebroer T" first="Theo M" last="Bestebroer">Theo M. Bestebroer</name><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name><name sortKey="Fouchier, Ron A M" sort="Fouchier, Ron A M" uniqKey="Fouchier R" first="Ron A M" last="Fouchier">Ron A M. Fouchier</name><name sortKey="Haagmans, Bart L" sort="Haagmans, Bart L" uniqKey="Haagmans B" first="Bart L" last="Haagmans">Bart L. Haagmans</name><name sortKey="Osterhaus, Albert D M E" sort="Osterhaus, Albert D M E" uniqKey="Osterhaus A" first="Albert D M E" last="Osterhaus">Albert D M E. Osterhaus</name><name sortKey="Ouwendijk, Werner J D" sort="Ouwendijk, Werner J D" uniqKey="Ouwendijk W" first="Werner J D" last="Ouwendijk">Werner J D. Ouwendijk</name><name sortKey="Provacia, Lisette B" sort="Provacia, Lisette B" uniqKey="Provacia L" first="Lisette B" last="Provacia">Lisette B. Provacia</name><name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J M" last="Rottier">Peter J M. Rottier</name><name sortKey="Smits, Saskia L" sort="Smits, Saskia L" uniqKey="Smits S" first="Saskia L" last="Smits">Saskia L. Smits</name><name sortKey="Spronken, Monique I" sort="Spronken, Monique I" uniqKey="Spronken M" first="Monique I" last="Spronken">Monique I. Spronken</name><name sortKey="Van Amerongen, Geert" sort="Van Amerongen, Geert" uniqKey="Van Amerongen G" first="Geert" last="Van Amerongen">Geert Van Amerongen</name><name sortKey="Van Den Brand, Judith M A" sort="Van Den Brand, Judith M A" uniqKey="Van Den Brand J" first="Judith M A" last="Van Den Brand">Judith M A. Van Den Brand</name><name sortKey="Wiersma, Lidewij" sort="Wiersma, Lidewij" uniqKey="Wiersma L" first="Lidewij" last="Wiersma">Lidewij Wiersma</name></noCountry><country name="Pays-Bas"><region name="Hollande-Méridionale"><name sortKey="Raj, V Stalin" sort="Raj, V Stalin" uniqKey="Raj V" first="V Stalin" last="Raj">V Stalin Raj</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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