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
- Research Support, N.I.H., Extramural
- Research Support, Non-U.S. Gov't
MeSH terms
- 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*
Substances
- Receptors, Virus
- Spike Glycoprotein, Coronavirus
- Dipeptidyl Peptidase 4
- Adenosine Deaminase