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The Sarbecovirus spike protein receptor-binding domain (RBD) is a critical structural component of the spike (S) glycoprotein found on the surface of viruses in the Sarbecovirus subgenus, including SARS-CoV and SARS-CoV-2. The RBD is responsible for mediating viral entry into host cells by binding to the human Angiotensin-Converting Enzyme 2 (ACE2) receptor. Because it contains the primary epitopes for neutralizing antibodies, the RBD is a major target for vaccine development and monoclonal antibody therapies. The specific mention of RBDs from seven non-SARS-CoV-2 sarbecoviruses (such as SARS-CoV, WIV1, RaTG13, SHC014, Pangolin-GD, Pangolin-GX, and RmYN02) refers to a multi-antigen approach used in pan-sarbecovirus vaccine candidates like the mosaic-8 nanoparticle. This strategy aims to elicit broad-spectrum immunity by presenting a diverse array of RBDs to the immune system, thereby favoring the production of antibodies that target conserved, cross-reactive epitopes rather than strain-specific ones. Such therapeutics are designed to provide protection against both current SARS-CoV-2 variants and potential future zoonotic spillover events from the broader sarbecovirus reservoir.
Neutralization of viral entry by blocking the interaction between the viral spike receptor-binding domain (RBD) and the host cell receptor, typically Angiotensin-Converting Enzyme 2 (ACE2).
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