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SARS-CoV-2-derived peptide epitopes are short amino acid sequences originating from the structural (Spike, Nucleocapsid, Membrane, Envelope) and non-structural proteins of the SARS-CoV-2 virus (Source: Grifoni et al., Cell, 2020). These peptides are the primary targets for the host's adaptive immune system, where they are presented by Major Histocompatibility Complex (MHC) molecules to T-cell receptors (TCRs) or recognized by B-cell receptors (BCRs) to initiate an immune response (Source: IEDB.org). In therapeutic development, these epitopes are used as the active components in peptide-based vaccines, such as CoVac-1, which are designed to elicit broad and potent T-cell immunity against COVID-19 (Source: Heitmann et al., Nature, 2022). They also play a crucial role in diagnostic monitoring, allowing for the quantification of T-cell responses via assays like ELISpot or MHC multimer staining (Source: NIH.gov). Because some epitopes are highly conserved across different coronaviruses, they are also being investigated for the development of pan-coronavirus vaccines. The selection of these epitopes is a critical step in ensuring vaccine efficacy across diverse human populations with varying HLA genotypes.
Peptide epitopes function as antigens that are processed and presented by MHC Class I and II molecules to CD8+ and CD4+ T cells, respectively, or recognized by B cells to stimulate the production of neutralizing antibodies and the establishment of immunological memory (Source: Grifoni et al., Cell, 2020; Heitmann et al., Nature, 2022).
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