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The SARS-CoV-2 membrane (M) protein is the most abundant structural protein of the virus and is essential for viral assembly and morphogenesis (UniProt P0DTC5). Peptide epitopes derived from the M protein are processed intracellularly and presented on the cell surface by Human Leukocyte Antigen (HLA) class I molecules (PubMed: 32887270). These peptide-HLA complexes serve as critical targets for the cellular immune system, specifically for CD8+ cytotoxic T lymphocytes (PubMed: 33053386). Recognition of these epitopes by T-cell receptors (TCRs) triggers the destruction of infected cells and the release of antiviral cytokines. Because the M protein is highly conserved across different SARS-CoV-2 variants, these epitopes are significant targets for developing variant-proof vaccines and T-cell-based immunotherapies (PubMed: 34795225). Therapeutic strategies include peptide-based vaccines designed to elicit broad T-cell responses and engineered TCR-T cell therapies that specifically recognize these M-peptide-HLA complexes.
Recognition by CD8+ T-cell receptors (TCRs) leading to the activation of cytotoxic T lymphocytes and subsequent lysis of virally infected cells.
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