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

The Middle East respiratory syndrome coronavirus (MERS-CoV) spike glycoprotein receptor-binding domain (RBD) is the key viral component that facilitates entry into host cells by binding to the dipeptidyl peptidase 4 (DPP4) receptor (Raj et al., 2013, Nature). The RBD consists of a core subdomain and a receptor-binding motif (RBM), the latter of which directly contacts DPP4 (Lu et al., 2013, Nature). Epitope 1 within this interface represents a highly conserved and potent site for neutralization; antibodies targeting this specific region, such as m336, can effectively block viral attachment and subsequent membrane fusion (Ying et al., 2014, J Virol). This domain is a primary focus for the development of vaccines and monoclonal antibody therapies, including REGN3048 and REGN3051, aimed at preventing or treating MERS-CoV infections (Pascal et al., 2015, J Exp Med). Because the RBD-DPP4 interaction is essential for viral pathogenesis, it serves as a critical bottleneck for the virus and a high-value target for drug discovery. Structural studies have shown that Epitope 1 is particularly vulnerable to neutralization because it overlaps significantly with the receptor-binding footprint (Du et al., 2014, Expert Opin Ther Targets). Therapeutic interventions targeting this epitope must account for potential viral mutations that could lead to escape, although the interface is relatively conserved among MERS-CoV strains. Overall, the MERS-CoV S RBD at the DPP4 interface is a validated target for both prophylactic and therapeutic applications in the management of MERS.

Other names

MERS-CoV S RBDMERS-CoV spike protein receptor-binding domainMERS-CoV S1-RBDMERS-CoV RBDDPP4-binding domain of MERS-CoVMERS-CoV RBD Epitope 1

Competitive inhibition of the RBD-DPP4 interaction, thereby preventing viral attachment and entry into host cells (Ying et al., 2014, J Virol).