SARS-CoV-2 structural protein-derived peptide-MHC complex (SARS-CoV-2 pMHC)

SARS-CoV-2 structural antigens presented via host Major Histocompatibility Complex (MHC) molecules represent the primary interface for cellular immune recognition (Sette & Crotty, 2021, Cell). These antigens are derived from the virus's structural proteins, including the Spike (S), Envelope (E), Membrane (M), and Nucleocapsid (N) proteins, which are processed into short peptides by the host cell's proteasomal or endosomal machinery (Grifoni et al., 2020, Cell). Once loaded onto MHC Class I or Class II molecules, these peptide-MHC (pMHC) complexes are displayed on the cell surface for surveillance by CD8+ and CD4+ T cells, respectively (Le Bert et al., 2020, Nature). Recognition of these complexes by specific T-cell receptors (TCRs) triggers an adaptive immune response, leading to the destruction of infected cells and the secretion of pro-inflammatory cytokines. This target is central to the efficacy of most COVID-19 vaccines, such as BNT162b2 and mRNA-1273, which aim to prime the immune system to recognize these specific pMHC signatures (Sahin et al., 2020, Nature). Furthermore, identifying conserved epitopes within these structural proteins is crucial for developing "variant-proof" vaccines and T-cell-based immunotherapies. Therapeutic strategies often focus on enhancing the presentation of these antigens or engineering T cells to recognize them more effectively. The diversity of human HLA alleles means that the specific peptides presented can vary significantly between individuals, posing a challenge for universal vaccine design (Nelde et al., 2021, Nature Immunology).

Other names

SARS-CoV-2 structural antigens presented via host MHC to T cellsSARS-CoV-2 T-cell epitopesSARS-CoV-2 HLA-peptide complexesSARS-CoV-2 peptide-HLA complex

Induction of T-cell mediated cytotoxicity and cytokine production through T-cell receptor (TCR) recognition of viral peptides presented on MHC molecules (Sette & Crotty, 2021, Cell).