Severe acute respiratory syndrome coronavirus 1 spike protein receptor-binding domain (SARS-CoV-1 RBD) (SARS-CoV-1 RBD)

The SARS-CoV-1 spike protein receptor-binding domain (RBD) is a critical functional unit within the S1 subunit of the viral spike glycoprotein (UniProt: P59594). Its primary biological role is to mediate high-affinity binding to the host cell surface receptor, Angiotensin-converting enzyme 2 (ACE2), which serves as the gateway for viral entry into human respiratory epithelial cells (PubMed: 14560002). During the infection process, the RBD transitions between "up" and "down" conformations to either hide from the immune system or expose its binding interface to ACE2 (PubMed: 16051146). As the principal target for the host's neutralizing antibody response, the RBD is the focus of most therapeutic interventions, including monoclonal antibodies and subunit vaccines (PubMed: 15033583). Drugs and antibodies targeting this domain, such as m396 or CR3022, function by sterically blocking the RBD-ACE2 interaction, thereby preventing the virus from initiating the fusion process (PubMed: 17349144, 32245444). Consequently, the RBD is a vital component in the study of viral pathogenesis and the development of countermeasures against SARS-related coronaviruses.

Other names

SARS-CoV RBDSpike RBDS1-RBDSARS-CoV-1 S-RBDSpike glycoprotein receptor-binding domain

Neutralization of viral infectivity by competitively inhibiting the binding of the viral spike protein to the host Angiotensin-converting enzyme 2 (ACE2) receptor.