SARS-CoV-2 spike protein receptor-binding motif (SARS-CoV-2 S RBM)

The SARS-CoV-2 spike protein receptor-binding motif (RBM) is a critical sub-region of the receptor-binding domain (RBD) that directly mediates the interaction with the human angiotensin-converting enzyme 2 (ACE2) receptor [UniProt P0DTC2]. Located within the S1 subunit of the spike glycoprotein, the RBM consists of approximately 70 amino acids (residues 438-506) that form the contact surface for the host cell [Lan et al., Nature 2020]. This interface is the primary determinant of viral tropism and infectivity, making it the most significant target for neutralizing antibodies produced by the immune system or administered as therapeutics [NIH COVID-19 Treatment Guidelines]. Most COVID-19 vaccines and monoclonal antibody treatments, such as Bamlanivimab and Casirivimab, are designed to bind to the RBM, thereby blocking viral attachment and entry [FDA Drug Information]. However, the RBM is highly prone to mutations, which can lead to the emergence of variants that exhibit increased binding affinity for ACE2 or escape from neutralizing antibodies [Harvey et al., Nature Reviews Microbiology 2021]. Understanding the structural and functional dynamics of the RBM is essential for the development of next-generation vaccines and broad-spectrum antiviral therapies.

Other names

Spike protein RBMSARS-CoV-2 S RBMReceptor-binding motifS1 protein RBMSARS-CoV-2 S-RBM

Neutralization of viral entry by competitively inhibiting the interaction between the viral spike protein and the host cell angiotensin-converting enzyme 2 (ACE2) receptor.