NR ATJE
AU Tsiroulnikov,K.; Rezaei,H.; Bonch-Osmolovskaya,E.; Grosclaude,J.; Gousterova,A.; Barbier,G.; Chobert,J.M.; Dormont,D.; Clayette,P.; Haertle,T.
TI Hydrolysis of the amyloid prion protein and non-pathogenic MBM by anaerobic thermophilic prokaryotes and Streptomyces subsp.
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Decontamination DEC-11
PT Konferenz-Poster
AB Transmissible spongiform encephalopathies are caused by accumulation of highly resistant miss folded amyloid prion protein PrPres and can be initiated by penetration of such pathogen molecules from infected tissue to intact organism. Decontamination of animal meal containing amyloid prion protein is proposed thanks to the use of proteolytic enzymes secreted by thermophilic bacteria Thermoanaerobacter, Thermosipho and Thermococcus subsp. and mesophilic soil bacteria Streptomyces subsp. Keratins a and b, which remind amyloid structures were used as the substrates for the screening for microorganisms able to grow on keratins and producing efficient proteases specific for hydrolysis of beta sheeted proteic structures hence amyloids. Secretion of keratin-degrading proteases was evidenced by zymogram method. Enzymes from thermophilic strains VC13, VC15, S290 and Streptomyces subsp. S6 were strongly active against amyloid recombinant ovine prion protein and animal meal proteins. Studied proteases displayed broad primary specificities hydrolyzing low-molecular mass peptide model substrates. Strong amyloidolytic activity of detected proteases was confirmed by experiments of hydrolysis of PrPres in SAFs produced from brain homogenates of mice infected with the 6PB1 BSE strain. The proteases from Thermoanaerobacter subsp. S290 and Streptomyces subsp. S6 are the best candidates for neutralization/elimination of amyloids in MBM and other protein containing substances and materials.
IN Nicht nur anaeriobe thermophile (bevorzugt über 50° arbeitende) Bakterien wie Thermoanaerobacter, Thermosipho and Thermococcus subsp, sondern auch mesophile (bevorzugt bei 30-40° arbeitende) gram-positive Streptomyces-Bodenbakterien scheinenmit ihren Proteasen in der Lage zu sein, Prionen abzubauen.
AD Kirill Tsiroulnikov, Jean-Marc Chobert, Thomas Haertle, Unité Biopolymeres Interactions Assemblages, Institut National de la Recherche Agronomique, B.P. 71627, 44316 Nantes Cedex 3, France.; Human Rezaei, Jeanne Grosclaude, Virologie et Immunologie Moléculaires (VIM), Institut National de la Recherche Agronomique, 78352 Jouy-en-Josas, France.; Elisaveta Bonch-Osmolovskaya, Institute of Microbiology, RAS, Prospekt 60 Let Oktyabrya 7/2, 117811 Moscow, Russia; Kirill Tsiroulnikov, Laboratory of Proteolytic Enzyme Chemistry, Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry of RAS, Moscow, Russia; Georges Barbier, Laboratoire de Microbiologie et de Biotechnologie des Extrêmophiles, IFREMER, Centre de Brest, B.P. 70, 29280 Plouzané, France; Pascal Clayette, SPI-BIO c/o Service de Neurovirologie, CEA, Fontenay aux Roses Cedex, France; Dominique Dormont, Service de Neurovirologie, CEA, CRSSA, Université Paris XI, EPHE, Fontenay aux Roses Cedex, France in memoriam; Adrina Gousterova, Institute of Microbiology, Bulg. Acad. Sciences, 1113-Sofia, Bl.27, Bulgaria
SP englisch
PO Deutschland