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

The SARS-CoV-2 spike protein receptor-binding domain (RBD) is a critical structural component located within the S1 subunit of the viral spike glycoprotein [UniProt P0DTC2]. Its primary biological function is to recognize and bind with high affinity to the human Angiotensin-Converting Enzyme 2 (ACE2) receptor, an interaction that serves as the essential first step for viral attachment and entry into host cells [Nature, 2020, 581(7807)]. Because the RBD-ACE2 interface is the principal gateway for infection, it is the dominant target for the host's neutralizing antibody response and the primary focus for the development of vaccines and monoclonal antibody therapies [PubMed, 32225176]. Therapeutic agents, such as monoclonal antibodies, are designed to bind specifically to epitopes within the RBD to sterically block its interaction with ACE2, thereby preventing the virus from infecting target cells [FDA, 2021]. However, the RBD is a highly plastic region subject to significant evolutionary pressure, leading to frequent mutations that can result in immune evasion and reduced susceptibility to existing treatments [Science, 2021, 371(6535)]. Consequently, monitoring the structural integrity and mutational profile of the RBD is vital for the ongoing development of effective COVID-19 countermeasures.

Other names

Spike RBDS-RBDReceptor-binding motifRBMSARS-CoV-2 S1-RBDSpike protein S1 subunit receptor-binding domain

Neutralization of viral entry by competitively inhibiting the binding of the viral spike protein to the host Angiotensin-Converting Enzyme 2 (ACE2) receptor.