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

Autor: Mou, H., Stalin Raj, V., van Kuppeveld, F.J.M., Rottier, P.J.M., Haagmans, B.L., Bosch, B.J., Strategic Infection Biology, Dep Infectieziekten Immunologie, Faculteit Diergeneeskunde, I&I SIB1
Přispěvatelé: Strategic Infection Biology, Dep Infectieziekten Immunologie, Faculteit Diergeneeskunde, I&I SIB1, Virology, Medical Oncology
Rok vydání: 2013
Předmět:
Zdroj: Journal of Virology, 87(16), 9379. American Society for Microbiology
Journal of Virology; Vol 87
Journal of Virology, 87(16), 9379-9383. American Society for Microbiology
ISSN: 1098-5514
0022-538X
DOI: 10.1128/JVI.01277-13
Popis: 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.
Databáze: OpenAIRE