SARS-CoV-2-derived peptide epitopes presented by human MHC class I and II molecules (SARS-CoV-2 pMHC epitopes)

SARS-CoV-2-derived peptide epitopes presented by human Major Histocompatibility Complex (MHC) class I and II molecules are the fundamental units recognized by the cellular arm of the adaptive immune system. These epitopes are short amino acid sequences derived from viral proteins—including Spike (S), Nucleocapsid (N), and Membrane (M)—that are processed by host cells and displayed on the cell surface (Grifoni et al., 2020, Cell). MHC class I molecules typically present these peptides to CD8+ cytotoxic T cells to induce the destruction of infected cells, while MHC class II molecules present them to CD4+ helper T cells to coordinate antibody production and long-term immune memory (Saini et al., 2021, Science Immunology). Because these complexes are essential for viral clearance and protection, they serve as the primary targets for T-cell-based vaccines and TCR-engineered cellular therapies (Nelde et al., 2021, Nature Communications). Therapeutic strategies, such as mRNA and peptide vaccines, aim to induce or mimic the presentation of these epitopes to prime the immune system against the virus (Sahin et al., 2020, Nature). However, the high diversity of human Leukocyte Antigen (HLA) alleles and the potential for viral mutations to alter peptide binding or TCR recognition present significant challenges for ensuring broad and durable population coverage (Altmann & Boyton, 2020, Science).

Other names

SARS-CoV-2 T-cell epitopesHLA-presented SARS-CoV-2 peptidesSARS-CoV-2 immunodominant peptidesCOVID-19 peptide-MHC complexesSARS-CoV-2 HLA ligands

Activation of T-cell mediated immunity through the specific binding of peptide-MHC complexes to T-cell receptors (TCRs) on CD4+ and CD8+ T cells.