SARS-CoV-2 spike protein receptor-binding domain (Wuhan-Hu-1) (SARS-CoV-2 RBD)

The SARS-CoV-2 receptor-binding domain (RBD) is a critical functional region of the spike (S) protein, specifically located within the S1 subunit, that mediates viral entry into host cells (UniProt: P0DTC2). Its primary biological function is to recognize and bind with high affinity to the human Angiotensin-Converting Enzyme 2 (ACE2) receptor, a process that triggers the conformational changes necessary for membrane fusion (PubMed: 32398877). The Wuhan-Hu-1 designation refers to the original wild-type sequence of the virus, which served as the foundational template for the first generation of COVID-19 vaccines and monoclonal antibodies (NCBI: NC_045512.2). As the primary interface between the virus and the host, the RBD is the most significant target for neutralizing antibodies, which aim to block the RBD-ACE2 interaction to prevent infection (PubMed: 32353859). However, the RBD is also a hotspot for mutations, leading to the emergence of variants that can evade existing therapeutic and vaccine-induced immunity (PubMed: 33688681). Consequently, while it remains a premier therapeutic target, its high rate of antigenic drift presents a significant challenge for maintaining long-term drug efficacy (StatPearls: NBK554776).

Other names

Spike protein RBDS-RBDSARS-CoV-2 S1 subunit receptor-binding domainWuhan-Hu-1 RBD

Neutralization of viral entry by competitively inhibiting the interaction between the viral receptor-binding domain and the host Angiotensin-Converting Enzyme 2 (ACE2) receptor.