SARS-CoV-2 spike glycoprotein receptor-binding domain (RBD) (SARS-CoV-2 S-RBD)

The SARS-CoV-2 spike glycoprotein receptor-binding domain (RBD) is a key functional region of the S1 subunit of the spike protein, which facilitates viral entry into human cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor (Hansen et al., 2020, Science). Casirivimab is a potent neutralizing monoclonal antibody that binds to a specific epitope within the RBD, preventing the virus from attaching to host cells (FDA, 2021, REGEN-COV Fact Sheet). This interaction is vital for the infectivity of SARS-CoV-2, making the RBD a primary target for therapeutic and vaccine development. The casirivimab epitope is distinct and non-overlapping with other antibodies like imdevimab, allowing for combination therapies that reduce the risk of viral resistance (Baum et al., 2020, Science). However, the rapid evolution of the virus has led to mutations in the RBD that can disrupt antibody binding, a phenomenon known as viral escape, which has rendered casirivimab less effective against certain variants like Omicron (Planas et al., 2022, Nature Medicine). Monitoring these mutations is essential for maintaining the clinical utility of RBD-targeted therapies.

Other names

SARS-CoV-2 S1 protein receptor-binding domainSpike RBDCasirivimab binding siteREGN10933 epitopeSARS-CoV-2 S-RBD casirivimab epitope

Neutralization of viral entry by competitively inhibiting the interaction between the viral receptor-binding domain (RBD) and the human angiotensin-converting enzyme 2 (ACE2) receptor.