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SARS-CoV-2 epitopes are specific molecular regions of the Severe Acute Respiratory Syndrome Coronavirus 2 that are recognized by the host's immune system, specifically by B-cell receptors (antibodies) and T-cell receptors. The most significant epitopes are located on the Spike (S) protein, particularly within the Receptor Binding Domain (RBD) and the N-terminal domain (NTD), which are critical for the virus's ability to bind to the human Angiotensin-Converting Enzyme 2 (ACE2) receptor and enter host cells (Huang et al., 2020). These epitopes serve as the primary targets for the majority of COVID-19 vaccines and therapeutic monoclonal antibodies, which aim to neutralize the virus by preventing its attachment or fusion with the host cell membrane (Kyriakidis et al., 2021). Beyond the Spike protein, epitopes on the Nucleocapsid (N), Membrane (M), and Envelope (E) proteins also play vital roles in eliciting T-cell responses and are frequently used in diagnostic assays (Grifoni et al., 2020). A major challenge in targeting these epitopes is the high rate of viral mutation, which leads to antigenic drift and the emergence of variants that can evade neutralizing antibodies (Harvey et al., 2021). Consequently, ongoing research focuses on identifying conserved epitopes across different coronaviruses to develop broad-spectrum vaccines and therapies (Taylor et al., 2021).
Neutralization of viral entry by blocking receptor binding or fusion, and induction of adaptive immune responses including antibody production and T-cell activation.
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