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Molecular insight into the mechanisms controlling presentation of viral and tumour antigens

Supervisor: Dr Louise Boyle
Based at Division of Immunology, Tennis Court Road

We are seeking a dedicated and enthusiastic PhD student to join our laboratory in the Department of Pathology, at the University of Cambridge. (http://www.path.cam.ac.uk/directory/louise-boyle). Our major research interest is characterising the mechanisms of peptide selection for immune recognition. We utilise a number of experimental methods, including biochemical, cellular, functional and structural studies, to improve our understanding of the major histocompatibility complex (MHC) antigen presentation pathway at a molecular level. This project will explore the influence of novel components of antigen processing pathway in inducing viral and tumour specific immune responses by professional antigen presenting cells.

Recent publications

Neerincx A & Boyle LH*. Properties of the tapasin homologue TAPBPR. Current Opinion in Immunology (2017) 46:97-102.

Neerincx A, Hermann C, Antrobus R, van Hateren A, Trauwein N, Stevanovic S, Elliott T, Deane JE, Boyle LH*. TAPBPR bridges UDP-glucose:glycoproteinglucosyltransferase 1 onto MHC class I to provide quality Control in the antigen presentation pathway. eLife (2017)6:e23049

Hermann C, van Hateren A, Trautwein N, Neerincx A, Duriez PJ, Stevanović S, Trowsdale J, Deane JE, Elliott T, Boyle LH*. TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst. eLife (2015) 4:e09617

Porter KM, Hermann C, Traherne JA, Boyle LH*. TAPBPR isoforms exhibit altered association with MHC class I. Immunology (2014) 142:289-99.

Hermann C, Strittmatter L, Deane JE, Boyle LH*. The binding of TAPBPR and tapasin to MHC class I is mutually exclusive. Journal of Immunology (2013) 191:5743-50.