Severe acute respiratory syndrome coronavirus 2 spike protein receptor-binding domain (RBD) (RBD)

The SARS-CoV-2 spike protein receptor-binding domain (RBD) is a key functional region of the S1 subunit of the viral spike (S) glycoprotein [1, 5]. Its primary biological role is to facilitate viral attachment to host cells by binding with high affinity to the human angiotensin-converting enzyme 2 (ACE2) receptor [4, 10]. This interaction is the critical first step in the viral life cycle, leading to membrane fusion and subsequent infection [12, 14]. Consequently, the RBD is the principal target for neutralizing antibodies generated by natural infection or vaccination, as well as for therapeutic monoclonal antibodies [2, 7, 8]. These therapeutic agents typically function by blocking the RBD-ACE2 interface, thereby preventing viral entry [1, 13]. However, the RBD is highly susceptible to mutations, which can lead to the emergence of variants of concern that exhibit increased transmissibility or reduced sensitivity to existing treatments [9, 11]. Additionally, research suggests that the RBD may independently contribute to disease pathology by triggering pro-inflammatory responses and disrupting endothelial barriers, such as the blood-brain barrier [15, 19].

Other names

SARS-CoV-2 spike receptor-binding domainSpike RBDS-RBDSARS-CoV-2 S1-RBD2019-nCoV RBDSpike glycoprotein receptor-binding domainS glycoprotein receptor-binding domain

Neutralization of viral entry by blocking the interaction between the viral receptor-binding domain and the host angiotensin-converting enzyme 2 (ACE2) receptor.