Lorne Protein: Workshopping protein folding

This year's Lorne Protein conference was preceded by a one-day workshop-style event, the Biomolecular Dynamics and Interactions Symposium, at the new Bio21 Molecular Science and Biotechnology Institute in Melbourne's Parkville.

The organiser, Prof Leann Tilley, of La Trobe University, says the symposium will focus on two related hot topics: protein folding, and amyloid-forming proteins.

Misfolded proteins that aggregate to form amyloid plaques and tangles in brain tissue cause inherited diseases like Creutzfeldt-Jakob (CJD) and Alzheimer's, and infectious diseases like bovine spongiform encephalopathy (BSE) or mad cow disease, and its human equivalent, variant CJD.

One of the symposium's leading overseas speakers, Prof Sheena Radford, of the University of Leeds, is studying a protein called beta2-microgloblin (b2M) that causes crippling complications in renal dialysis patients.

The protein tends to form fibrils, that are normally removed by the kidney, but builds up in patients undergoing long-term dialysis. Radford is investigating the molecular basis of b2M amyloid fibril formation.

Tilley says it is now clear that not all amyloid-forming proteins are aberrant, misfolded proteins. Dr Cate McPhee, of the Oxford Centre for Molecular Sciences in the UK, who will speak at the workshop and the main conference, has shown that amyloid fibril formation is a general property of polypeptide.

Tilley's colleague at La Trobe University, veteran malaria researcher Prof Robin Anders, will describe an amyloid fibril-forming protein on the surface of the malaria parasite, Plasmodium falciparum, that appears to serve an important biological function. The protein is a strong candidate for incorporation in a malaria vaccine.