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Dr Louise Boyle

Dr Louise Boyle

Wellcome Trust Senior Research Fellow

Research focus: Molecular mechanisms controlling peptide selection for immune recognition

Department of Pathology
University of Cambridge
Tennis Court Road

Office Phone: 01223 (3)33705

Research themes


Research Interests

Major Histocompatibility Complex (MHC) class I molecules play a fundamental role orchestrating the immune system and inducing protective immune responses against tumours and pathogens.  They do this by presenting peptides derived from pathogenic and tumourgenic proteins to the immune system. My aim is to determine the molecular mechanisms controlling peptide selection by MHC molecules.  This has important translational potential given the importance of MHC molecules in infectious disease, cancer and autoimmunity.

Research into the MHC antigen processing and presentation pathway during the past two decades has identified key components essential for peptide loading onto MHC class I molecules.  Tapasin was thought to be the only MHC class I specific chaperone in the antigen processing and presentation pathway, and therefore has been considered the key molecule controlling peptide presentation to the immune system.  However, we have discovered a completely novel MHC class I specific component in the antigen processing and presentation pathway, a protein called TAPBPR. More recently, we have determined that TAPBPR shares the same binding site on MHC class I as tapasin.  This implicates TAPBPR in peptide selection and challenges the precise role of tapasin in the MHC class I pathway. Collectively, our data suggest that the current model of antigen presentation by MHC class I is incomplete.  

Our work is currently focused on understanding the precise function of TAPBPR in the MHC presentation pathway.

Research Supervision

Current Lab members

Key Publications

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. 

Abualrous ET, Fritzsche S, Hein Z, Al-Balushi MS, Reinink P, Boyle LH, Wellbrock U, Antoniou AN, Springer S (2015). F pocket flexibility influences the tapasin dependence of two differentially disease-associated MHC Class I proteins. Eur J Immunol. 45:1248-57

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.

Garstka MA, Fritzsche S, Lenart I, Hein Z, Jankevicius G, Boyle LH, Elliott T, Trowsdale J, Antoniou AN, Zacharias M, Springer S (2011).Tapasin dependence of major histocompatibility complex class I molecules correlates with their conformational flexibility. FASEB J. 25:3989-98. 

Burr ML, Cano F, Svobodova S, Boyle LH, Boname JM, Lehner PJ (2011). HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation. Proc Natl Acad Sci U S A. 108:2034-9. 

Rhodes DA, Boyle LH, Boname JM, Lehner PJ, Trowsdale J (2010). Ubiquitination of lysine-331 by Kaposi's sarcoma-associated herpesvirus protein K5 targets HFE for lysosomal degradation. Proc Natl Acad Sci U S A. 107:16240-5.