Influence of high pressure treatment on the infectivity of prion proteins

Project

Food and consumer protection

This project contributes to the research aim 'Food and consumer protection'. Which funding institutions are active for this aim? What are the sub-aims? Take a look:
Food and consumer protection

Project code: MRI-OG-08-10
Contract period: 01.01.2002 - 31.12.2008
Purpose of research: Basic research

Incorrect folded proteins are named as the cause of transmissible spongiform encephalopathy like BSE in cattle, scrapie in sheep, and Creuzfeld-Jakob-disease in humans. The causing agent of these most times deadly ending diseases of the nervous system is an isoform of the cellular prion protein called PrPSc (Sc = Scrapie). These pathogenic proteins are highly resistant against usually used methods to degrade conventional pathogens. Suitable inactivation procedures, e.g. steam sterilisation = 133 °C, are aggressive, with a consequent loss in quality and texture in the treated tissues. Mild inactivation technologies for prion proteins like high hydrostatic pressure could be an advantage for further processing of infectious material. Furthermore, there are no temperature induced effects on the treated material like vitamin loss, loss of nutrients, and changes in taste, colour, and texture. In addition high hydrostatic pressure is able to induce a change in conformation of proteins. The aim of the research project is to investigate the possibility to inactivate infectious prion proteins by changing the confirmation with high hydrostatic pressure.

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