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

The Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein receptor-binding domain (RBD) is a critical region of the S1 subunit of the viral spike glycoprotein (UniProt: P0DTC2). Its primary biological function is to mediate viral entry by binding with high affinity to the human angiotensin-converting enzyme 2 (ACE2) receptor (PubMed: 32225175). This interaction is the prerequisite for viral-host membrane fusion and subsequent infection of the host cell. Because of its essential role, the RBD is the primary target for neutralizing antibodies, including those elicited by vaccines and therapeutic monoclonal antibodies like imdevimab (PubChem: CID 155574495). Imdevimab, often used in combination with casirivimab, binds to a specific epitope on the RBD to sterically block ACE2 binding (FDA: REGEN-COV Fact Sheet). However, the RBD is also a hotspot for mutations, which can lead to the emergence of variants of concern that exhibit reduced susceptibility to these treatments (PubMed: 33332293).

Other names

SARS-CoV-2 spike RBDSpike protein receptor-binding domainS-RBDSARS-CoV-2 S1 subunit receptor-binding domain

Neutralization of the virus by binding to the receptor-binding domain (RBD) of the spike protein, which sterically hinders the interaction with the host cell ACE2 receptor and prevents viral entry (PubMed: 33332293).