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

The SARS-CoV-2 spike glycoprotein S1 subunit receptor-binding domain (RBD) is a critical viral component responsible for initiating infection by binding to the human host cell receptor, angiotensin-converting enzyme 2 (ACE2) (NIH, 2020; Frontiers, 2022). Located within the S1 subunit of the trimeric spike protein, the RBD undergoes conformational changes between 'open' and 'closed' states to facilitate receptor access (NIH, 2020; Frontiers, 2022). This interaction is the primary determinant of viral tropism and infectivity, making the RBD the most significant target for the development of vaccines and therapeutic monoclonal antibodies (NIH, 2021; Frontiers, 2021). Most neutralizing antibodies work by sterically hindering the RBD-ACE2 interface, thereby preventing viral entry into the host cell (NIH, 2021). However, the RBD is highly susceptible to mutations, leading to the emergence of variants of concern that can evade existing immune responses and reduce the efficacy of therapeutic interventions (Frontiers, 2022; NIH, 2021). Understanding the structural dynamics and mutational landscape of the RBD remains essential for the design of broad-spectrum antivirals and next-generation vaccines (Frontiers, 2022).

Other names

SARS-CoV-2 RBDSpike protein RBDS-RBDReceptor-binding domain of the spike proteinS1-RBDSARS-CoV-2 spike protein S1 subunit receptor-binding domain

Neutralization of viral entry by competitively or sterically blocking the interaction between the viral RBD and the host ACE2 receptor.