NR AURN
AU Müller-Hellwig,S.; Stegmann,K.; Scherer,S.
TI Stability of the BSE agent in foodstuff - Biochemical characterisation of bacterial proteases with PrPsc degradation potential
QU TSE-Forum, 6. Kongress - Nationale TSE-Forschungsplattform, Greifswald 26.6.-28.6.2006, Poster: Struktur und molekulare Mechanismen MOL-11
PT Konferenz-Poster
AB In order to protect consumers, a scientifically based risk assessment of animal derived products, particularly dairy products is required. In this context the stability of the infectious PrP-agent in food is of prime importance. The aim of our project focuses on food-borne bacteria able to degrade PrPsc. We started with a broad screening of several hundred bacteria and identified several protease-secreting stains able to degrade the prion protein under mild conditions. One hundred and ninety-nine protease-secreting isolates belonging to the Actinomycetales and Bacillales were screened for the expression of PrPsc degrading activity by Western blot. Only 6 strains belonging to the following species were found to exhibit such activity: Arthrobacter nicotianae, Bacillus licheniformis, Brachybacterium conglomeratum, Brachybacterium tyrofermentans and Staphylococcus sciuri and Serratia spp. We are currently characterising the active proteins in further detail, for which we purify them to homogeneity using different methods. One approach is native purification using various FPLC columns or affinity chromatography with specific monoclonal antibodies. Another approach is the expression of a fusion protein in E.coli. The purified proteins are used for degradation assays of PrPsc.
AD Simone Müller-Hellwig, Kerstin Stegmann und Siegfried Scherer, Abteilung Mikrobiologie, Zentralinstitut für Ernährungs- und Lebensmittelforschung (ZIEL), Technische Universität München, Weihenstephaner Berg 3, D-85350 Freising
SP englisch
PO Deutschland
OR Tagungsband