SARS-CoV-2 Spike glycoprotein receptor-binding domain (S-RBD) (S-RBD)

The SARS-CoV-2 Spike glycoprotein receptor-binding domain (S-RBD) is a key functional unit within the S1 subunit of the viral spike protein [Kenyon College, 2023; NIH, 2021]. Its primary biological role is to facilitate viral attachment to host cells by binding specifically to the human angiotensin-converting enzyme 2 (ACE2) receptor [bioRxiv, 2020; NIH, 2020]. This interaction is the initial and essential step for viral entry, leading to the development of COVID-19 [MDPI, 2024]. Due to its critical role in infection and its high accessibility on the viral surface, the S-RBD is the immunodominant target for neutralizing antibodies produced during natural infection or vaccination [Beckman Coulter, 2020; NIH, 2021]. Therapeutic interventions, such as monoclonal antibodies (e.g., casirivimab and imdevimab), are designed to bind the RBD and sterically hinder its interaction with ACE2 [NIH, 2021]. However, the S-RBD is also a hotspot for mutations, leading to the emergence of variants that can escape neutralization and challenge the long-term efficacy of vaccines and therapeutics [NIH, 2021]. Understanding the structural and functional dynamics of the S-RBD remains vital for the development of next-generation COVID-19 countermeasures [bioRxiv, 2020; NIH, 2020].

Other names

Spike protein RBDSARS-CoV-2 S-RBDReceptor-binding domain of the spike proteinS1-RBD

Neutralization of viral particles by blocking the interaction between the receptor-binding domain (RBD) and the host cell receptor ACE2, thereby preventing viral entry and infection [NIH, 2020; MDPI, 2024].