MHC-I antigen processing and presentation in viral immune detection and evasion

Peptide presentation on major histocompatibility complex (MHC)-I molecules is central to mounting effective antiviral immune responses. However, our understanding of the antigen processing and presentation (APP) pathway in virus-infected cells is incomplete. In addition to ER aminopeptidases (ERAPs) and tapasin, TAPBPR was recently characterised as a third MHC-I peptide editor. TAPBPR shapes the cellular MHC-I immunopeptidome presented at the cell surface, but its role in viral infections remains unexplored. Additionally, proteomic datasets clearly demonstrate that there are uncharacterised interactions between APP components and viral proteins that may impact immune recognition of infected cells. My overarching aim is to explore the complex dynamics between viruses and MHC-I APP proteins in immune detection and evasion.