Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.
Raj, V Stalin; Smits, Saskia L; Provacia, Lisette B; van den Brand, Judith M A; Wiersma, Lidewij; Ouwendijk, Werner J D; Bestebroer, Theo M; Spronken, Monique I; van Amerongen, Geert; Rottier, Peter J M; Fouchier, Ron A M; Bosch, Berend Jan; Osterhaus, Albert D M E; Haagmans, Bart L
(2014) Journal of Virology, volume 88, issue 3, pp. 1834 - 8
(Article)
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
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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.
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Keywords: Molecular Sequence Data, Protein Binding, Receptors, Virus, Adenosine Deaminase: metabolism, Amino Acid Sequence, Animals, Coronaviridae, Coronaviridae Infections, Coronaviridae Infections: enzymology, Coronaviridae Infections: virology, Coronaviridae: genetics, Coronaviridae: physiology, Dipeptidyl Peptidase 4, Dipeptidyl Peptidase 4: chemistry, Adenosine Deaminase, Virus Internalization, Spike Glycoprotein, Coronavirus: metabolism, Spike Glycoprotein, Coronavirus: genetics, Spike Glycoprotein, Coronavirus, Sequence Alignment, Receptors, Virus: metabolism, Adenosine Deaminase: genetics, Receptors, Virus: genetics, Receptors, Virus: chemistry, Dipeptidyl Peptidase 4: genetics, Dipeptidyl Peptidase 4: metabolism, Disease Models, Animal, Ferrets, Humans
ISSN: 0022-538X
Publisher: American Society for Microbiology
(Peer reviewed)
