Major histocompatibility complex molecules presenting influenza-derived peptides (MHC-influenza peptide complex)

Major histocompatibility complex (MHC) molecules presenting influenza-derived peptides are essential structures for the immune recognition of influenza virus infections. These complexes are formed when viral proteins, such as the matrix protein (M1) or nucleoprotein (NP), are proteolytically degraded into peptides and loaded onto MHC Class I or Class II molecules within the endoplasmic reticulum or endocytic compartments (Janeway et al., Immunobiology, 2001). The resulting peptide-MHC (pMHC) complex is then transported to the cell surface, where it serves as a specific ligand for T-cell receptors (TCRs) on CD8+ or CD4+ T cells. In the context of influenza, the HLA-A*02:01-restricted M1 peptide (GILGFVFTL) is one of the most extensively studied epitopes due to its high conservation across different viral strains (Gotch et al., Nature, 1987). These complexes are primary targets for the development of universal influenza vaccines and advanced immunotherapies, including TCR-engineered T cells and bispecific molecules, which aim to provide broader protection than traditional antibody-mediated vaccines (Rosendahl Huber et al., Nature Communications, 2016). However, the high diversity of HLA alleles in the human population and the risk of viral escape through antigenic drift remain significant hurdles in targeting these complexes effectively.

Other names

HLA-influenza peptide complexpMHC complexInfluenza-specific peptide-MHC complexMHC-I/II influenza antigen complexInfluenza-derived pMHC

The MHC-influenza peptide complex acts as a ligand for the T-cell receptor (TCR). Recognition of this complex by CD8+ T cells (for MHC Class I) or CD4+ T cells (for MHC Class II) triggers T-cell activation, leading to the secretion of pro-inflammatory cytokines (e.g., IFN-gamma) and the targeted lysis of infected cells (Neefjes et al., Nature Reviews Immunology, 2011).