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.
Publication types
- Research Support, Non-U.S. Gov't
MeSH terms
- Antibodies, Neutralizing / immunology*
- Antibodies, Viral / immunology
- Binding Sites
- Cell Line
- Coronavirus / immunology*
- Coronavirus / physiology*
- Dipeptidyl Peptidase 4 / metabolism
- Epitopes, B-Lymphocyte / genetics
- Epitopes, B-Lymphocyte / immunology*
- Humans
- Membrane Glycoproteins / immunology*
- Membrane Glycoproteins / metabolism*
- Receptors, Virus / metabolism
- Spike Glycoprotein, Coronavirus
- Viral Envelope Proteins / immunology*
- Viral Envelope Proteins / metabolism*
- Virus Attachment*
Substances
- Antibodies, Neutralizing
- Antibodies, Viral
- Epitopes, B-Lymphocyte
- Membrane Glycoproteins
- Receptors, Virus
- Spike Glycoprotein, Coronavirus
- Viral Envelope Proteins
- spike glycoprotein, SARS-CoV
- spike protein, mouse hepatitis virus
- DPP4 protein, human
- Dipeptidyl Peptidase 4