MersV1, PubMed, Curation, bibRecord, 001B33

Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.

Identifieur interne : 001B33 ( PubMed/Curation ); précédent : 001B32; suivant : 001B34

Adenosine 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. Haagmans

Source :

Journal of virology [ 1098-5514 ] ; 2014.

RBID : pubmed:24257613

Descripteurs français

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

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Le document en format XML

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<term>Glycoprotéine de spicule des coronavirus (métabolisme)</term>
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<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Sequence Alignment</term>
<term>Virus Internalization</term>
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<front><div type="abstract" xml:lang="en">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. </div>
</front>
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<DateCompleted><Year>2014</Year>
<Month>04</Month>
<Day>16</Day>
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<ArticleTitle>Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.</ArticleTitle>
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<Abstract><AbstractText>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. </AbstractText>
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<ForeName>V Stalin</ForeName>
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<ForeName>Lisette B</ForeName>
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<ForeName>Judith M A</ForeName>
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Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.

Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.

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