Dr Andy Van Hateren

• Immunology.
• Cancer.
• MHC I peptide selection.
• Antigen presentation.
• Protein structure and protein dynamics.

The binding of peptides by Major Histocompatibility Complex class I molecules (MHC I), and their presentation to cytotoxic T cells, is an integral component of the adaptive immune system, providing protection from intracellular pathogens and cancer. 

MHC I molecules are highly polymorphic, with each MHC I allotype binding a different cohort of peptides. MHC I molecules become loaded with peptides in the endoplasmic reticulum of a cell, in a process that is assisted by a macromolecular peptide loading complex. A key constituent of this peptide loading complex is the molecule tapasin. Once loaded with peptides, MHC I molecules pass through the secretory pathway en route to the cell surface. During this transit, some MHC I molecules encounter scrutiny from the tapasin homologue, TAPBPR.

TAPBPR, like tapasin, performs a "peptide editing" function that results in the preferential selection of peptides that bind with high affinity, allowing the most effective antigen presentation.

My research is focused on how MHC I molecules select peptides for presentation, and how tapasin and TAPBPR modulate this process.