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Sequence and structure key to prion disease transmission

Date:
June 14, 2010
Source:
Journal of Clinical Investigation
Summary:
Prion diseases are lethal neurodegenerative disorders that include Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy (BSE, commonly known as mad cow disease) in cows. New data generated in mice provides greater understanding of the factors that determine how easy it is for prion diseases to be transmitted to a new host species. This information provides new insight into a highly important food safety issue.

Prion diseases are lethal neurodegenerative disorders that include Creutzfeldt-Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE; commonly known as mad cow disease) in cows. A team of researchers, led by Adriano Aguzzi and Christina Sigurdson, at UniversitätsSpital Zürich, Switzerland, has generated data in mice that provides greater understanding of the factors that determine how easy it is for prion diseases to be transmitted to a new host species.

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This information provides new insight into a highly important food safety issue; dietary exposure to beef contaminated with the BSE agent is believed to have caused nearly 200 cases of variant CJD in humans.

The key infectious agent in prion diseases is PrPSc, a highly aggregated form of the cellular prion protein (PrPC). The ease with which prions from different species can be transmitted to a new host species varies dramatically. The team found that transmission between species with the same protein building block at position 170 in PrPC was relatively easy while it was relatively difficult between those species with different building blocks at that position.

As this protein building block influences the structure of the PrPC protein, the authors suggest that local structure of PrPC affected by the protein building block at position 170 might have a triggering role in prion transmissibility between different species.

The research is published in the Journal of Clinical Investigation.


Story Source:

The above story is based on materials provided by Journal of Clinical Investigation. Note: Materials may be edited for content and length.


Journal Reference:

  1. Christina J. Sigurdson, K. Peter R. Nilsson, Simone Hornemann, Giuseppe Manco, Natalia Fernández-Borges, Petra Schwarz, Joaquín Castilla, Kurt Wüthrich, and Adriano Aguzzi. A molecular switch controls interspecies prion disease transmission in mice. Journal of Clinical Investigation, 2010; DOI: 10.1172/JCI42051

Cite This Page:

Journal of Clinical Investigation. "Sequence and structure key to prion disease transmission." ScienceDaily. ScienceDaily, 14 June 2010. <www.sciencedaily.com/releases/2010/06/100614121556.htm>.
Journal of Clinical Investigation. (2010, June 14). Sequence and structure key to prion disease transmission. ScienceDaily. Retrieved January 25, 2015 from www.sciencedaily.com/releases/2010/06/100614121556.htm
Journal of Clinical Investigation. "Sequence and structure key to prion disease transmission." ScienceDaily. www.sciencedaily.com/releases/2010/06/100614121556.htm (accessed January 25, 2015).

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