The spike (S) protein of the recently emerged human Middle East respiratory syndromecoronavirus (MERS-CoV) mediates infection by binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the S protein to a 231-amino-acid fragment (residues 358 to 588) by evaluating the interaction of spike truncation variants with receptor-expressing cells and soluble DPP4. Antibodies to this domain-mch less so those to the preceding N-terminal region-efficiently neutralize MERS-CoV infection.

dx.doi.org/10.1128/JVI.01277-13, hdl.handle.net/1765/64810
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

Mou, H, Raj, V.S, van Kuppeveld, F.J.M, Rottier, P.J.M, Haagmans, B.L, & Bosch, B.J. (2013). The receptor binding domain of the new middle east respiratory syndrome coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing antibodies. Journal of Virology, 87(16), 9379–9383. doi:10.1128/JVI.01277-13