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

The SARS-CoV-2 spike protein receptor-binding domain (RBD) is a critical component of the viral envelope that mediates attachment to host cells by specifically binding to the human Angiotensin-Converting Enzyme 2 (ACE2) receptor (Monteil et al., 2020, Cell). This interaction is the primary gateway for viral entry and subsequent infection, making the RBD a premier target for therapeutic intervention (Chan et al., 2020, Science). Using an ACE2 extracellular domain decoy involves administering a soluble form of the receptor that competes with the membrane-bound ACE2 on lung and other tissues (ClinicalTrials.gov, NCT04335136). By binding to the viral RBD, these decoys effectively neutralize the virus and prevent it from docking onto host cells. This approach is particularly robust against viral variants because mutations that reduce binding to the decoy would likely also reduce the virus's ability to bind its natural receptor (Zhang et al., 2021, Nature Communications). Beyond neutralization, soluble ACE2 may also provide a protective effect by regulating the renin-angiotensin system, which is often dysregulated during severe COVID-19 (Zheng et al., 2020, Intensive Care Med).

Other names

SARS-CoV-2 S-RBDSpike protein RBDS1 subunit receptor-binding domainSARS-CoV-2 S1-RBD

Competitive inhibition of viral entry by acting as a decoy receptor that binds to the SARS-CoV-2 spike protein receptor-binding domain, preventing its interaction with endogenous cellular ACE2 receptors.