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.
| Original language | Undefined/Unknown |
|---|---|
| Pages (from-to) | 9379-9383 |
| Number of pages | 5 |
| Journal | Journal of Virology |
| Volume | 87 |
| Issue number | 16 |
| DOIs | |
| Publication status | Published - 2013 |
Research programs
- EMC MM-04-27-01