SARS-CoV-2 spike protein receptor-binding domain (RBD) (SARS-CoV-2 S RBD)

The SARS-CoV-2 spike protein receptor-binding domain (RBD) is a specialized region within the S1 subunit of the viral spike glycoprotein (UniProt: P0DTC2). Its primary biological function is to facilitate the high-affinity binding of the virus to the human Angiotensin-Converting Enzyme 2 (ACE2) receptor, which serves as the gateway for viral entry into host cells (Nature, 2020). As the critical interface for infection, the RBD is the primary target for neutralizing antibodies generated by both natural infection and vaccination (Nature, 2020). Therapeutic interventions, such as monoclonal antibodies like Sotrovimab or Bebtelovimab, are designed to bind specifically to the RBD to prevent it from docking with ACE2, thereby neutralizing the virus's ability to infect cells (FDA, 2022). However, the RBD is highly prone to mutations, leading to the emergence of variants of concern that can exhibit increased transmissibility or immune evasion (Nature Reviews Microbiology, 2021). Consequently, the RBD remains a focal point for ongoing drug development and genomic surveillance in the management of COVID-19 (CDC, 2023).

Other names

Spike RBDS-RBDSARS-CoV-2 S1 subunit RBDReceptor-binding domain of the spike protein

Neutralization of viral entry by competitively or sterically blocking the interaction between the viral RBD and the host ACE2 receptor (Nature, 2020; FDA, 2022).