SARS-CoV spike glycoprotein receptor-binding domain (RBD)

The SARS-CoV spike glycoprotein receptor-binding domain (RBD) is a critical functional unit located within the S1 subunit of the coronavirus spike protein. Its primary biological role is to mediate the high-affinity attachment of the virus to the host cell by binding to the human Angiotensin-converting enzyme 2 (ACE2) receptor. This binding event is the essential first step in the viral entry process, triggering conformational changes that allow the S2 subunit to facilitate membrane fusion. Because the RBD is exposed on the viral surface and is indispensable for infection, it serves as the principal target for neutralizing monoclonal antibodies and the majority of global vaccine efforts. Therapeutic agents, such as neutralizing antibodies, work by binding to the RBD and sterically blocking its interaction with ACE2, thereby preventing the virus from entering host cells. However, the RBD is highly susceptible to mutations, which can lead to the emergence of viral variants with enhanced transmissibility or the ability to evade existing immunity. Understanding the structural and functional dynamics of the RBD is therefore vital for the ongoing development of effective countermeasures against coronaviruses like SARS-CoV and SARS-CoV-2.

Other names

SARS-CoV-2 spike protein RBDSARS-CoV-1 spike protein RBDS-RBDSpike RBDReceptor-binding domain of the spike protein

Neutralization of viral entry by blocking the interaction between the viral receptor-binding domain (RBD) and the host cell receptor, Angiotensin-converting enzyme 2 (ACE2).