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

The SARS coronavirus spike protein receptor-binding domain (RBD) is a critical functional unit located within the S1 subunit of the spike (S) glycoprotein on the surface of the SARS-CoV virion (UniProt P59594). Its primary biological role is to mediate high-affinity binding to the human Angiotensin-converting enzyme 2 (ACE2) receptor, which serves as the gateway for viral entry into host respiratory epithelial cells (Li et al., 2003, Nature). Because the RBD is the most exposed and immunodominant portion of the virus, it is the primary target for neutralizing antibodies and the development of subunit vaccines (Du et al., 2009, Virology). Therapeutic agents, such as the monoclonal antibodies m396 and S230, work by binding to specific epitopes within the RBD to sterically block its association with ACE2 (ter Meulen et al., 2006, PLoS Medicine). Mutations within the RBD can significantly alter the virus's transmissibility and its ability to jump between species, making it a key focus for genomic surveillance and pandemic preparedness. Understanding the structural biology of the RBD-ACE2 interface has been fundamental in designing interventions to combat Severe Acute Respiratory Syndrome (SARS).

Other names

SARS-CoV-1 spike protein receptor-binding domainSARS-CoV S1-RBDSpike glycoprotein receptor-binding domainSARS-CoV S1 receptor-binding domain

Neutralization of viral entry by competitively inhibiting the interaction between the viral receptor-binding domain and the host Angiotensin-converting enzyme 2 (ACE2) receptor (Li et al., 2005, Nature).