Influenza virus peptide-Major Histocompatibility Complex (pMHC) (Influenza pMHC)

Influenza virus peptide antigens presented on host Major Histocompatibility Complex (MHC) molecules are essential targets for the cellular immune system's recognition of infected cells. During the viral life cycle, internal proteins such as Nucleoprotein (NP) and Matrix 1 (M1) are degraded by the proteasome into short peptides, which are then transported into the endoplasmic reticulum and loaded onto MHC Class I molecules for surface display (Rock et al., 2016). These peptide-MHC (pMHC) complexes serve as the primary ligands for CD8+ T-cell receptors, signaling the presence of intracellular infection and triggering a cytotoxic response. Unlike surface glycoproteins like hemagglutinin, these internal peptides are highly conserved across different influenza strains, making them ideal targets for universal influenza vaccines and novel immunotherapies (Grant et al., 2013). Therapeutic approaches include the development of Immune mobilizing monoclonal TCRs Against Virus (ImmTAVs) and T-cell-inducing vaccines that aim to provide broad protection against seasonal and pandemic influenza (Liddy et al., 2012). However, the effectiveness of these therapies is often limited by the high diversity of human leukocyte antigen (HLA) alleles and the potential for the virus to undergo mutational escape within the targeted epitopes.

Other names

Influenza HLA-peptide complexInfluenza epitope-MHC complexInfluenza antigen-MHC complexViral pMHC

Recognition of the specific viral peptide-MHC complex by engineered T-cell receptors (TCRs) or TCR-mimetic antibodies, which triggers the activation of cytotoxic T lymphocytes (CTLs) to induce apoptosis in the infected host cell (Liddy et al., 2012; Health et al., 2017).