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

The SARS-CoV-2 spike glycoprotein receptor-binding domain (RBD) contains a specific region known as the receptor-binding motif (RBM), which serves as the primary interface for interaction with the human Angiotensin-converting enzyme 2 (ACE2) receptor (UniProt: P0DTC2). This interaction is the critical first step for viral attachment and subsequent entry into host cells, making the RBM a high-priority target for therapeutic intervention and vaccine design (PubMed: 32225175). Most neutralizing antibodies elicited by natural infection or vaccination specifically target the RBM to block its binding to ACE2, thereby preventing infection (PubMed: 32540901). However, the RBM is also the most variable part of the spike protein, frequently accumulating mutations that allow the virus to evade the host immune system and existing monoclonal antibody therapies. Therapeutic strategies targeting this motif include monoclonal antibodies and subunit vaccines designed to induce a robust neutralizing response. Understanding the structural dynamics and mutational landscape of the RBM is essential for developing broad-spectrum treatments against evolving variants of the virus.

Other names

SARS-CoV-2 S protein RBD RBMSpike protein receptor-binding motifS1-RBD RBMSARS-CoV-2 RBMReceptor-binding motif of the SARS-CoV-2 spike protein

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