2006 ASBMB Fellowship: Fleur Tynan

Fleur Tynan began her career in biochemistry as an Honours student, studying under the supervision of Professor Jamie Rossjohn at Monash University. Here she combined structural and biophysical techniques to examine the unusual domain architecture of TnpX, a DNA recombinase from an uncharacterised group of large serine recombinases. Following this work, Fleur moved on to examine the structure of myelin oligodendrocyte glycoprotein (MOG), a key autoantigen involved in multiple sclerosis. Fleur compared the structure of MOG with similar and related proteins to further understand the relationship between MOG and the breakdown of immunotolerance which is observed in multiple sclerosis. It was during this work that Fleur decided to pursue a career using the powerful technique of crystallography.

Fleur began a PhD project with Professor Rossjohn examining the structural basis of the immune response against Epstein Barr virus (EBV). Her interests lie in the presentation of unusually lengthy viral epitopes by MHC molecules, and how TCRs are able to accommodate them, yet still maintain such extreme specificity for an MHC. Her research has led to publications in Nature Immunology, Journal of Experimental Medicine and Journal of Biological Chemistry. Her most significant work has been the structure solution of the SB27 TCR in complex with the MHC molecule HLA-B*3508 presenting an EBV peptide 13 residues in length. This structure revealed for the first time a mechanism by which the TCR can accommodate a lengthy, bulging epitope and also highlights a potential minimal footprint of MHC restriction. This work has been acknowledged through the presentation of the international Ludo Frevel Crystallography Scholarship and this ASBMB Fellowship, which will allow her to present some recent findings at the International Union of Biochemistry and Molecular Biology conference in Kyoto, Japan.

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This page last modified: October 10, 2008.