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
Publication date
2013
Authors
Mou, H.
Stalin Raj, V.
van Kuppeveld, Frank J M
Rottier, P.J.M.
Haagmans, B.L.
Bosch, Berend-Jan
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Document Type
Article
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Abstract
The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (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—much less so those to the preceding N-terminal region—efficiently neutralize MERS-CoV infection.
Keywords
Antibodies, Neutralizing, Antibodies, Viral, Binding Sites, Cell Line, Coronavirus, Dipeptidyl Peptidase 4, Epitopes, B-Lymphocyte, Humans, Membrane Glycoproteins, Receptors, Virus, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins, Virus Attachment, Coronacrisis-Taverne
Citation
Mou, H, Stalin Raj, V, 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, vol. 87, no. 16, pp. 9379-9383. https://doi.org/10.1128/JVI.01277-13