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SARS-CoV-2 structural protein-derived peptides presented on HLA are critical molecular complexes that signal the presence of viral infection to the adaptive immune system. These complexes are formed when viral proteins—specifically the Spike (S), Nucleocapsid (N), Membrane (M), and Envelope (E) proteins—are proteolytically processed into short peptides and loaded onto Human Leukocyte Antigen (HLA) molecules for surface display (Source: Nature, 2021, PMID: 33055231). Once presented, these peptide-HLA (pMHC) complexes serve as the primary targets for CD8+ and CD4+ T cells, which recognize them via specific T-cell receptors (TCRs) to initiate an antiviral response (Source: Cell, 2020, PMID: 32473127). In therapeutic contexts, these complexes are targeted by multi-peptide vaccines like CoVac-1 and TCR-engineered T-cell therapies designed to provide broad and durable immunity against SARS-CoV-2 variants (Source: Nature Communications, 2022, PMID: 34819517). The specificity of the interaction depends heavily on the patient's HLA genotype, which determines which viral epitopes can be effectively presented. Understanding these targets is essential for developing treatments that bypass antibody-mediated viral escape and provide long-term protection through cellular memory.
Recognition by T-cell receptors (TCRs) to induce cytotoxic T-lymphocyte (CTL) activity and cytokine production.
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