JVI: The receptor binding domain of the new MERS coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing a

[tetano]

Published ahead of print 19 June 2013, doi: 10.1128/JVI.01277-13 JVI.01277-13

The receptor binding domain of the new MERS coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing antibodies

Huihui Mou1,
V. Stalin Raj2,
Frank J.M. van Kuppeveld1,
Peter J.M. Rottier1,
Bart L. Haagmans2 and
Berend Jan Bosch1#

+ Author Affiliations

1Department of Infectious Diseases and Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL, Utrecht, the Netherlands
2Department of Viroscience, Erasmus Medical Center, Rotterdam, the Netherlands

ABSTRACT

The spike (S) protein of the recently emerged human 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 358-588) by evaluating the interaction of spike truncation variants with receptor expressing cells and soluble DPP4. Antibodies to this domain - much less so to the preceding N-terminal region - efficiently neutralize MERS-CoV infection.


http://jvi.asm.org/content/early/2013/06/13/JVI.01277-13.abstract