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

The Middle East respiratory syndrome coronavirus (MERS-CoV) spike glycoprotein receptor-binding domain (RBD) is a specialized region of the viral S protein that mediates attachment to host cells by binding to the human receptor dipeptidyl peptidase 4 (DPP4) (Wang et al., 2013, Nature). This interaction is the primary determinant of viral host range and tissue tropism, serving as the essential first step for viral entry and subsequent infection of the respiratory epithelium (UniProt P0C6S4). Because of its critical role in the viral life cycle and its accessibility on the viral surface, the RBD is the primary target for the development of neutralizing antibodies and vaccines. REGN3051 is a fully human monoclonal antibody that specifically targets an epitope within the RBD that overlaps with the DPP4 binding interface (Pascal et al., 2015, J Infect Dis). By binding to this site, REGN3051 sterically blocks the virus from docking onto host cells, effectively neutralizing the pathogen. This target is central to therapeutic strategies aimed at preventing or treating MERS-CoV, particularly in outbreak settings or zoonotic transmission events.

Other names

MERS-CoV S proteinMERS-CoV spike proteinMERS-CoV RBDSpike glycoprotein receptor-binding domainMERS-CoV S1 domain

Neutralization of viral infection by competitively inhibiting the interaction between the viral spike receptor-binding domain (RBD) and the host cell receptor dipeptidyl peptidase 4 (DPP4).