The role of TAPBPR in professional antigen presenting cells
Based at Department of Pathology, Tennis Court Road
Supervised by Dr Louise Boyle
The presentation of antigenic peptides to the immune system is crucial in generating protective responses against infection and cancer. Recently, we have discovered a protein called TAPBPR is a novel component of the antigen processing and presentation pathway and influences peptide selection on MHC class I molecules. This PhD project will fully explore the function of TAPBPR in immune cells, particularly Dendritic cells, using a wide-range of state of the art approaches and techniques. This work will reveal important novel insights into peptide selection for immune recognition key to infection control and detection of cancer.
Hermann C, van Hateren A, Trautwein N, Neerincx A, Duriez PJ, Stevanović S, Trowsdale J, Deane JE, Elliott T, Boyle LH (2015). TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst. Elife. Oct 6;4. doi: 10.7554/eLife.09617.
Hermann C, Trowsdale J, Boyle LH (2015). TAPBPR: a new player in the MHC class I presentation pathway. Tissue Antigens. 85:155-66.
Porter KM, Hermann C, Traherne JA, Boyle LH (2014).TAPBPR isoforms exhibit altered association with MHC class I.Immunology. 142:289-99
Hermann C, Strittmatter LM, Deane JE, Boyle LH (2013). The binding of TAPBPR and Tapasin to MHC class I is mutually exclusive. J Immunol. 191:5743-50.
Boyle LH, Hermann C, Boname JM, Porter KM, Patel PA, Burr ML, Duncan LM, Harbour ME, Rhodes DA, Skjødt K, Lehner PJ, Trowsdale J (2013). Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathway. Proc Natl Acad Sci U S A. 110:3465-70.
More information on the supervisor’s research can be found on their research group website