Severe acute respiratory syndrome coronavirus 2 spike glycoprotein receptor-binding domain (SARS-CoV-2 RBD) (SARS-CoV-2 RBD)

The Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein receptor-binding domain (RBD) is a critical functional region of the S1 subunit of the viral spike protein (UniProt P0DTC2). Its primary biological function is to facilitate viral entry into host cells by binding with high affinity to the human angiotensin-converting enzyme 2 (ACE2) receptor (PubMed: 32225175). This interaction is the essential first step of infection, making the RBD the primary target for neutralizing antibodies and vaccine-induced immunity. Tixagevimab is a long-acting monoclonal antibody that targets a specific epitope on the RBD, effectively blocking the virus from attaching to and infecting human cells (FDA: Evusheld EUA). Because the RBD is subject to high selective pressure, it frequently acquires mutations that can lead to immune evasion and reduced drug efficacy, as seen with various Omicron subvariants (PubMed: 35213357). Understanding the structural and functional characteristics of this target is vital for the ongoing development of therapeutics against COVID-19.

Other names

SARS-CoV-2 spike protein RBDSpike RBDS-RBDSurface glycoprotein receptor-binding domainSARS-CoV-2 S1 subunit RBDTixagevimab epitope

Tixagevimab binds to a specific epitope on the receptor-binding domain of the SARS-CoV-2 spike protein, which sterically inhibits the interaction between the virus and the human angiotensin-converting enzyme 2 (ACE2) receptor, thereby neutralizing the virus and preventing host cell entry (FDA: Evusheld EUA; PubMed: 32225175).