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

The SARS-CoV-2 spike protein receptor-binding motif (RBM) is a specific region within the receptor-binding domain (RBD) of the S1 subunit of the viral spike protein. It serves as the primary interface for direct contact with the human angiotensin-converting enzyme 2 (ACE2) receptor, which is the gateway for the virus to enter host cells (Lan et al., 2020, Nature). Due to its essential role in viral attachment, the RBM is the most critical target for neutralizing antibodies elicited by natural infection or vaccination (Barnes et al., 2020, Nature). Therapeutic strategies, particularly monoclonal antibodies like bamlanivimab and casirivimab, specifically target the RBM to block its interaction with ACE2, thereby preventing infection (Hansen et al., 2020, Science). However, the RBM is highly prone to mutations, which can lead to the development of variants that evade immune detection or reduce the efficacy of existing treatments (Harvey et al., 2021, Nature Reviews Microbiology). The motif typically encompasses residues 438 to 506 of the spike protein, forming a concave surface that accommodates the N-terminal helix of ACE2 (Shang et al., 2020, Nature). Mutations in this region, such as E484K or N501Y, have been shown to significantly alter binding affinity and immune recognition (Starr et al., 2020, Cell). Understanding the structural dynamics of the RBM is vital for the ongoing development of broad-spectrum vaccines and therapeutics against evolving strains of the virus.

Other names

SARS-CoV-2 S-RBMSpike protein RBMACE2-binding motifReceptor-binding motif of the spike protein

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