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Using new high sensitivity mass spectrometers housed in the Department of Biological Sciences together with facilities in the M-Scan Mass Spectrometry Research and Training Centre, Ascot, the Imperial research team headed by Professor Dell and Professor Howard Morris were able to identify the precise nature of glycosylation in C. jejuni, including the exact position where sugars are attached to proteins.

Colleagues in Zurich were then able to insert the C. jejuni glycosylation machinery into E coli and test whether it worked using mutational analysis.

"We have only begun to scratch the surface in understanding important role sugars play in our body," said Professor Dell. "Many common diseases including certain types of rheumatoid arthritis and muscular dystrophy have already been linked to disruption of the delicate balance of sugars displayed on the surface of proteins. Deciphering these complex interactions will be significantly aided by the new tool our research has developed."

Professor Brendan Wren of the London School of Hygiene and Tropical Medicine added:

"C. jejuni is recognised to be the major bacterial cause of gastro-intestinal diseases worldwide and can lead to the development of serious neurological disease. Despite the importance of the organism it is very poorly understood. Apart from its potential in glycoengineering, the newly characterised glycosylation system will also be useful in the development of vaccines to reduce the burden of Campylobacter-related disease".

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Contact: Judith H Moore
j.h.moore@ic.ac.uk
44-20-7594-6702
Imperial College London
28-Nov-2002