Reporter 431, 15 February 1999
A cure for BSE could be brought one step closer by a new University study of the mysterious proteins at the source of the disease.
Biochemist Nigel Hooper has embarked on a three-year project to analyse the structure and function of prion proteins.
Prions are found in the nerve cells of healthy brain tissue, but in diseases such as BSE they change shape and become impossible for the body to break down. These misshapen rogue proteins force further normal prions to distort, and spread the disease through the brain.
Dr Hooper believes that studying the prions' original form may help halt this deadly conversion.
"Prions have only recently been identified as a disease-causing agent and much of the subsequent research has focused on identifying and treating the infectious form," he said.
"But we really need to discover what the prions normally do before we can be clear what the diseased proteins are not doing, or perhaps doing too much of."
Dr Hooper will not be working with infectious material, but believes there could be vital clues to diseases such as BSE hidden in the structure of the normal proteins.
Growing different versions of the proteins in cell cultures, and then breaking them apart with enzymes, will reveal their structure and help explain what causes them to change shape.
The research will also study the role played by copper. It was recently discovered that the normal prions bind large quantities of copper. This changes when the protein becomes infectious and Dr Hooper believes this may offer one of the best routes to a possible cure.
"If we can understand the copper storage enough to manipulate it then we might have a way of stopping the normal prions being converted."
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