SARS-CoV-2 Spike protein S1 subunit, receptor-binding domain (SARS-CoV-2 S1 RBD)

The SARS-CoV-2 Spike protein S1 subunit, receptor-binding domain (RBD) is a key structural component of the SARS-CoV-2 virus, the causative agent of COVID-19 (UniProt P0DTC2) [1]. It is located within the S1 subunit of the spike glycoprotein and is responsible for recognizing and binding to the human Angiotensin-Converting Enzyme 2 (ACE2) receptor on the surface of host cells (PMC7332446) [2]. This binding event is the initial and essential step for viral attachment and subsequent entry into the host cell. Because of its critical role in infection, the RBD is the primary target for the host immune response and the focus of most vaccine and monoclonal antibody development efforts. Therapeutic agents, such as neutralizing monoclonal antibodies, are designed to bind specifically to the RBD to sterically hinder its interaction with ACE2 (FDA, 2021) [4]. However, the RBD is also a hotspot for mutations, leading to the emergence of variants of concern that can evade existing immunity and therapeutic interventions (Nature Communications, 2021) [5].

Other names

RBDSpike RBDS1-RBDSARS-CoV-2 S-RBDReceptor-binding domain of the spike protein

Neutralization of viral particles by blocking the interaction between the receptor-binding domain and the host ACE2 receptor, thereby preventing viral entry into host cells (Nature, 2020) [3].