Severe acute respiratory syndrome coronavirus 2 spike glycoprotein conserved epitopes (SARS-CoV-2 S protein conserved epitopes)

The Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein is a trimeric class I fusion protein that mediates viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor (Hoffmann et al., 2020). Conserved epitopes within this protein are specific, invariant regions that remain relatively unchanged across different viral variants and related sarbecoviruses, such as the S2 subunit fusion peptide and certain cryptic sites within the receptor-binding domain (RBD) (Veesler et al., 2020). These epitopes are critical targets for the development of broadly neutralizing antibodies (bnAbs) and variant-proof vaccines designed to provide durable protection against the evolving landscape of COVID-19 (Cameroni et al., 2022). Therapeutic agents, such as Sotrovimab, target these conserved regions to sterically hinder receptor binding or prevent the structural rearrangements necessary for viral-host membrane fusion (Pinto et al., 2020; Walls et al., 2020). Identifying and targeting these invariant structural features is essential for mitigating viral escape and ensuring the long-term efficacy of countermeasures against emerging variants of concern (Harvey et al., 2021).

Other names

SARS-CoV-2 spike protein conserved regionsPan-sarbecovirus epitopesSARS-CoV-2 spike protein invariant regionsBroadly neutralizing epitopes of SARS-CoV-2SARS-CoV-2 S2 subunit conserved epitopesSARS-CoV-2 S protein

Neutralization of viral entry by blocking the interaction between the receptor-binding domain (RBD) and the host ACE2 receptor, or by inhibiting the conformational changes required for membrane fusion in the S2 subunit (Walls et al., 2020; Pinto et al., 2020).