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Coronavirus T-cell epitopes are short peptide fragments derived from viral proteins, such as the Spike (S), Nucleocapsid (N), and Membrane (M) proteins, that are recognized by the host immune system (Grifoni et al., 2020, Cell). These peptides are processed and presented on the surface of infected cells or professional antigen-presenting cells by Major Histocompatibility Complex (MHC) Class I and Class II molecules (Sette & Crotty, 2021, Nature). When a T-cell receptor (TCR) binds to a specific epitope-MHC complex, it triggers T-cell activation, leading to the destruction of infected cells by CD8+ cytotoxic T-cells or the coordination of the broader immune response by CD4+ helper T-cells. In therapeutic development, these epitopes are critical components of vaccines and T-cell therapies designed to provide broad and durable protection against various coronavirus strains, including SARS-CoV-2 (NIH, 2021). Identifying conserved epitopes is particularly important for developing pan-coronavirus vaccines that remain effective despite viral mutations. These epitopes serve as the fundamental units for eliciting cellular immunity, which is essential for preventing severe disease and ensuring long-term immunological memory (Sette & Crotty, 2021, Cell).
Induction of adaptive cellular immunity through the presentation of viral peptides by MHC molecules to T-cell receptors, leading to the activation of CD4+ and CD8+ T-cells.
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