Middle East respiratory syndrome coronavirus spike glycoprotein S1 receptor-binding domain (MERS-CoV S1-RBD)

The Middle East respiratory syndrome coronavirus (MERS-CoV) spike glycoprotein S1 receptor-binding domain (RBD) is a critical viral component that mediates infection by binding to the host cell receptor, dipeptidyl peptidase 4 (DPP4) [PMID: 23765417]. Located within the S1 subunit of the trimeric spike protein, the RBD undergoes structural transitions to expose its receptor-binding motif, which directly contacts the DPP4 molecule on the surface of human respiratory cells [PMID: 23851363]. This binding event is the essential first step for viral attachment, which is followed by membrane fusion mediated by the S2 subunit. Because the RBD contains the primary epitopes for neutralizing antibodies, it is the central focus for the development of vaccines and therapeutic monoclonal antibodies [PMID: 25713390]. Therapeutic strategies, such as the use of monoclonal antibodies like m336 and REGN3048, aim to sterically hinder the RBD-DPP4 interaction, thereby neutralizing the virus's ability to enter cells [PMID: 24775577]. Understanding the structural biology of this domain is vital for monitoring potential viral escape mutants and for developing broad-spectrum countermeasures against emerging coronaviruses.

Other names

MERS-CoV RBDMERS-CoV spike protein receptor-binding domainMERS-CoV S-RBDMERS-CoV S1 domain

Neutralization of viral entry by competitively inhibiting the binding of the viral spike protein to the host cell receptor dipeptidyl peptidase 4 (DPP4).