๐ 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
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. ยฉ 2013, American Society for Microbiology.
author
๐ค Mou, Huihui
๐ค Raj, V. Stalin
๐ค Van Kuppeveld, Frank J.M.
๐ค Rottier, Peter J.M.
๐ค Haagmans, Bart L.
๐ค Bosch, Berend Jan
year
โฐ 2013
journal
๐ Journal of Virology
issn
๐ 0022538X 10985514
volume
87
number
16
page
9379-9383
citedbycount
107
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