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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Deaminase / genetics
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Adenosine Deaminase / metabolism*
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Amino Acid Sequence
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Animals
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Coronaviridae / genetics
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Coronaviridae / physiology*
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Coronaviridae Infections / enzymology*
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Coronaviridae Infections / virology
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Dipeptidyl Peptidase 4 / chemistry
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Dipeptidyl Peptidase 4 / genetics
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Dipeptidyl Peptidase 4 / metabolism*
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Disease Models, Animal
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Ferrets
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Humans
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Molecular Sequence Data
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Protein Binding
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Receptors, Virus / chemistry
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Receptors, Virus / genetics
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Receptors, Virus / metabolism*
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Sequence Alignment
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Spike Glycoprotein, Coronavirus / genetics
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Spike Glycoprotein, Coronavirus / metabolism
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Virus Internalization*
Substances
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Receptors, Virus
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Spike Glycoprotein, Coronavirus
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Dipeptidyl Peptidase 4
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Adenosine Deaminase