Researchers in Switzerland map key protein

A research team at the Federal Institute of Technology in Zurich has mapped a three-dimensional structure of a human prion protein which plays a key role in the development of the human form of mad cow disease, Creutzfeldt Jakob disease.

A research team at the Swiss Federal Institute of Technology in Zurich has managed to map a three-dimensional structure of a human prion protein. This is the protein that plays an important part in the development of the human form of mad cow disease, Creutzfeldt Jakob disease.

The research, carried out at the Institute of Molecular Biology and Biophysics, has found that human prion proteins are similar in form to those prion proteins already discovered in laboratory mice and hamsters.

“This enables us to compare this structure with the corresponding protein structure from laboratory animals,” the head of the research team, Kurt Wüthrich said. “In future, it will enable us to make detailed comparisons with cattle, and this should give us a deeper insight into the so-called species barrier.”

And Professor Wüthrich says that we are not that far away from getting a clearer picture of the possible links between mad cow disease and CJD.

“Our next step is to finish the structure determination for the bovine prion protein. This will be finished within a matter of weeks, or at most, months,” he said.

The Swiss National Science Foundation, which helped fund the research, said that differences between the human prion and animal prion were found in those areas suspected of being points of departure for the transformation of a healthy prion into its sick state.

But Professor Wüthrich warns that a cure for CJD is still a long way off: “Our results are a contribution to an understanding of prion diseases, in particular the species barrier. But I think we a long way away from a practical application.”

Researchers at the Zurich institute were the first to provide a three-dimensional picture of a mouse prion protein two years ago. The present studies were made, as then, by using nuclear magnetic resonance spectroscopy.

The findings have been published in the United States magazine “Proceedings of the National Academy of Sciences” in Washington.