Biochemical evidence for the proteolytic degradation of infectious prion protein PrPsc in hamster brain homogenates by foodborne bacteria |
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| Authors: | Müller-Hellwig Simone Groschup Martin H Pichner Rohtraud Gareis Manfred Märtlbauer Erwin Scherer Siegfried Loessner Martin J |
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| Institution: | 1. Abteilung Mikrobiologie, Zentralinstitut für Ernährungs- und Lebensmittelforschung, Technische Universität München, D-85350 Freising-Weihenstephan, Germany;2. Friedrich-Loeffler-Institut, Institute for Novel and Emerging Diseases, D-17498 Insel Riems, Germany;3. Bundesforschungsanstalt für Ernährung und Lebensmittel, Institut für Mikrobiologie und Toxikologie, D-95326 Kulmbach, Germany;4. Ludwig-Maximilian Universität München, Lehrstuhl für Hygiene und Technologie der Milch, D-85754 Oberschleissheim, Germany;5. Institute for Food Science and Nutrition, Swiss Federal Institute of Technology (ETH), Schmelzbergstrasse 7, CH-8092 Zürich, Switzerland;1. Department of Chemical Engineering, University of California Santa Barbara, Santa Barbara, CA 93106, USA;2. Department of Electrical and Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA;3. Center for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, Maryland 21201;4. Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, Maryland 21201;5. Centre for Biological Threats and Special Pathogens, Robert Koch-Institute, 13353 Berlin, Germany;1. Mitchell Center for Alzheimer’s Disease and Related Brain Disorders, Department of Neurology, University of Texas Medical School at Houston, 6431 Fannin Street, Houston, TX 77030, USA;2. Prion Research Center, Department of Microbiology, Immunology, and Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA |
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| Abstract: | PrP(Sc) is a general term to describe the infectious agent causing transmissible spongiform encephalopathy (TSE), and the protease-resistant form of cellular PrP(C). In this study, we have identified several protease-secreting bacteria able to degrade PrP(Sc) under more or less native conditions (30 degrees C, pH 8), focusing on strains isolated mainly from cheese. One hundred and ninty-nine protease-secreting isolates belonging to the Actinomycetales and Bacillales were screened for the expression of PrP(Sc) degrading activity by a Western blot procedure. Only 6 strains belonging to the following species were found to exhibit such an activity: Arthrobacter nicotianae, Bacillus licheniformis, Brachybacterium conglomeratum, Brachybacterium tyrofermentans and Staphylococcus sciuri and Serratia spp. As revealed by a general protease assay based on dye-labeled Azocoll substrate, the PrP(Sc) degrading activity was not directly correlated to the total level of secreted proteolytic activity of these organisms. This indicates that specific proteases are required for the degradation of PrP(Sc). Our study also suggests the potential use of such starter bacteria or their proteases for application in PrP(Sc) degradation and decontamination under native conditions. |
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