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 & Conceptual Biology 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?
Researchers in the Collins, Lawson, White, Barnham and Cappai Laboratories in the Pathology Department at the University of Melbourne are studying various aspects of prion diseases and their transmission to better understand the chemical processes involved and identify potential therapies. The Department also monitors the occurrence of CJD in Australia and hosts the Australian National CJD Registry.
Dr Simon Hawke of the Sydney Medical School 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.
Boxes
Box 1. Public health issues
Box 2. The Australian Quarantine Inspection Service and the need for quarantine
Related site
Research labs (University of Melbourne, Australia)
Page updated November 2011.