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.

dx.doi.org/10.1128/JVI.02935-13, hdl.handle.net/1765/68010
Journal of Virology
This work was funded by the European Commission 7th Framework Programme; grant id fp7/223498 - European management platform for emerging and re-emerging infectious disease entities (EMPERIE), This work was funded by the European Commission 7th Framework Programme; grant id fp7/278976 - ANTIcipating the Global Onset of Novel Epidemics (ANTIGONE)
Department of Virology

Stalin Raj, V.S, Smits, S.L, Provacia, L.B.V, van den Brand, J.M.A, Wiersma, L.C.M, Ouwendijk, W.J.D, … Haagmans, B.L. (2014). Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the middle East respiratory syndrome coronavirus. Journal of Virology, 88(3), 1834–1838. doi:10.1128/JVI.02935-13