Spike glycoprotein S1 subunit receptor-binding domain of SARS-CoV-2 (S1 RBD (Spike RBD))

The Spike glycoprotein S1 subunit receptor-binding domain of SARS-CoV-2 (Spike RBD) is a critical functional domain within the S1 subunit of the trimeric spike glycoprotein that decorates the surface of SARS-CoV-2 virions. The RBD is responsible for specific recognition and high-affinity binding to the host cell receptor angiotensin-converting enzyme 2 (ACE2), initiating viral attachment and enabling subsequent entry via membrane fusion. Structurally, it consists of a core β-sheet and an extended receptor-binding motif (RBM) that makes direct contact with ACE2. The RBD is the principal target of neutralizing antibodies elicited by infection and vaccination, and is the focus of most current COVID-19 monoclonal antibody therapeutics and vaccine designs. Sequence variations in this domain impact viral transmissibility, antibody escape, and cross-species transmission. The RBD's role as a main determinant of host tropism, infectivity, and immune response establishes it as an essential therapeutic and diagnostic target for COVID-19.

Other names

Spike protein receptor-binding domain (RBD)SARS-CoV-2 RBDS1 receptor-binding domainSpike S1 RBDSpike glycoprotein RBD

Blockade of ACE2 binding (neutralizing antibodies and ACE2 mimetics); Disruption of spike-ACE2 interaction (preventing virus attachment to host); Induction of immune response (vaccines using RBD as immunogen); Competitive inhibition (soluble ACE2 and receptor mimetics)