Enzymatic degradation of a prion-like protein,Sup35NM-His6 |
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| Institution: | 1. Department of Biotechnology, BioResource International, Inc., 840, Main Campus Dr. Suite 3510, Raleigh, NC 27606, USA;2. Department of Poultry Science, North Carolina State University, Raleigh, NC 27695, USA;1. Key Laboratory of Micro-systems and Micro-structures Manufacturing of Ministry of Education, Harbin Institute of Technology, Harbin, Heilongjiang 150001, PR China;2. Center For Precision Engineering, Harbin Institute of Technology, Harbin, Heilongjiang 150001, PR China;1. Biological Sciences Division, Pacific Northwest National Laboratory, 3300 Stevens Dr., Richland, WA 99354, United States;2. Institute for Future Environments, Queensland University of Technology, Brisbane, Australia;3. Center for Tropical Crops and Biocommodities, Queensland University of Technology, Brisbane, Australia;1. Department of Earth and Planetary Sciences and McDonnell Center for the Space Sciences, Washington University in St. Louis, One Brookings Drive, St. Louis, MO 63130, USA;2. Geosciences Research Division, Scripps Institution of Oceanography, La Jolla, CA 92093-0244, USA;3. Astromaterials Research and Explorations Science Directorate, Acquisition and Curation, NASA Johnson Space Center, 2101 NASA Road 1, Houston, TX 77058, USA;4. Institut de Physique du Globe de Paris, Université Paris Diderot, Sorbonne Paris Cité, 1 rue Jussieu, 75238, Paris Cedex 05, France;1. State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China;2. University of the Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing 100049, China;3. China National Center for Biotechnology Development, Beijing 100036, PR China |
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| Abstract: | Recent studies indicate that enzymatic treatment of the infectious PrPSc prion under defined conditions could be an effective method to inactivate infectious prions. However, field studies on prion inactivation are hampered by restricted access to the dangerous and expensive infectious prion material. Hence, a surrogate marker for infectious prions would facilitate more practical prion inactivation research. Protein Sup35p, a non-pathogenic prion-like protein produced in yeast, has physical and chemical properties very similar to the BSE prion. Sup35NM-His6, a derivative of Sup35p, was produced from Escherichia coli by gene cloning, protein expression and purification. Monomeric Sup35NM-His6 is soluble. When aggregated, it forms prion-like amyloid, insoluble and resistant to proteases. Similar to BSE prion, a pre-heating step renders this protein digestible by proteinase K, subtilisin and keratinase but not collagenase and elastase. These results indicated that Sup35NM-His6, being simple and inexpensive to produce and non-pathogenic, can be a potential ideal candidate of prion surrogate protein in the study of prion inactivation and prevention of prion diseases. |
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