3-D look at prions may lead to cure

3-D look at prions may lead to cure

THE work of two University of Alberta researchers and their teams has contributed to an important next step in finding a cure for deadly prion-folding diseases.

The laboratories of University of Alberta professors Michael James in the department of biochemistry and Nat Kav in the department of agricultural, food and nutritional science collaborated to produce mini-antibodies and antibody fragments using data provided by principal researchers in Switzerland.

The fragments were then used by the lead researchers at the Institute of Neuropathology in Zurich, Switzerland, to study interactions between the antibodies and the prion protein and how it results in cell death.

The work conducted at Alberta helps open the door to designing a molecule that would block prion infection, the university said.

"We hope to design a chemical compound that would bind to some part of the prion molecule to prevent the conversion of the normal form of the protein to the disease-causing form," James said.

Prion protein infections, caused by structural misfolding within the prion protein, lead to fatal neurodegenerative disorders such as Creutzfeldt-Jakob disease in people, bovine spongiform encephalopathy (BSE) in cattle and chronic wasting disease in deer. There is currently no cure for prion diseases.

Using recombinant DNA technology, Kav and his lab produced the mini-antibodies and antibody fragments. Using a process called X-ray crystallography, James's lab was able to identify the three-dimensional structure of where antibodies and antibody fragments bind to the prion molecule, pinpointing regions that are susceptible to changing to a diseased state.

The discovery makes it possible to begin designing ways to prevent prion disease, ranging from developing a treatment for people to creating a preventative additive for livestock feed, the announcement said.

Volume:85 Issue:32

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