Published by Australian Academy of Science
Prions – morphing agents of disease Box 3 |Australian researchers looking at prion proteins and CJD

Dr Jill Gready is a Senior Fellow in the John Curtin School of Medical Research at the Australian National University, Canberra, and Leader of the Computational Molecular Biology and Drug Design Group. One current project of this group is to predict the structure of the prion protein implicated in CJD.

Dr Gready is looking at the normal and abnormal forms of the CJD prion protein. The work of Gready's group is primarily computer-based, using databases and molecular models to work out the structure of the prion protein. Specific questions that could be answered as a result of this project are:

• What is the normal structure of the protein?
• What is the mechanism of the conformational change to scrapie form?
• Why is the protein so apparently sensitive to damage leading to this irreversible conformational change?
• How do known disease-causing mutations increase this sensitivity?
• What is the normal function of the prion protein?

Dr Simon Hawke of the Brain and Mind Research Institute at the University of Sydney is looking at the response of the immune system to prions, and is developing methods for early diagnosis and immunotherapy treatments.

Related sites

• Research labs (University of Melbourne, Australia)

• Brain briefings: Prion proteins (Society of Neuroscience, USA)

Other boxes

Box 1. Public health issues

Box 2. The Australian Quarantine Inspection Service and the need for quarantine