2003 Roche Medal: Jamie Rossjohn

RossjohnJamie travelled over the border from Wales to undertake his first degree and PhD at Bath University. During his PhD, Jamie was exposed to the world of X-ray crystallography, where under the supervision of Professor Garry Taylor, Professor Michael Danson and Dr David Hough, Jamie determined the crystal structure of glucose dehydrogenase from a thermophilic archaeon (Thermoplasm acidiphilum). Subsequently, Jamie was awarded a Royal Society Travel Fellowship to work at St Vincent's Institute of Medical Research, firstly in the laboratory of Professor Michael Parker, and subsequently establishing his own laboratory within the institute. During his postdoctoral training, Jamie was awarded an ARC postdoctoral fellowship, and he flourished under the guidance of Professor Parker. He initially worked on glutathione S-transferases, a class of detoxifying enzymes that have been implicated in the reduced efficacy of anti-cancer drugs, anti-parasitic drugs, antibiotic resistance and insecticide resistance.

Whilst at St Vincent's, Jamie commenced a series of studies on the pore-forming bacterial toxins, aerolysin and perfringolysin O (PFO). The work on PFO aided in unravelling the molecular mechanism of these toxins - specifically, how the toxin is converted from a water-soluble monomer to a membrane-bound oligomeric pore. Dr Rossjohn was awarded an RD Wright Fellowship, and extended his work to cell-surface receptors, and subsequently solved the structure of the N-terminal domain of the amyloid precursor protein (APP), and a pivotal region of the b-GM-CSF receptor. Dr Rossjohn's work on APP suggested that APP functions as a growth factor. The work on the GM-CSF receptor, which was solved in complex with a functional antagonist, gave the first structural insights into this receptor family.

The award of a Wellcome Trust Senior Research Fellowship launched Jamie's independent research career. Following his award, Jamie moved to Monash University in order to design, establish and head the Protein Crystallography Unit, located at the Department of Biochemistry and Molecular Biology. This was an intense period of activity that would not have been possible without the drive of James Whisstock and senior personnel within Monash. His current research activities are centred around receptor function and dysfunction, with a particular emphasis on structural immunology. In collaboration with Professor James McCluskey, and the team of researchers within the Monash/Melbourne structural immunology group, the crystal structure of an immunodominant T cell receptor was recently determined, as well as the alloreactive binary HLA B44 complexes.