NR ATJN
AU Rao,M.A.; Ricciardella,M.; Violante,A.; Gianfreda,L.
TI Fate of prion protein in soil: interaction with organo and organo-mineral complexes
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Decontamination DEC-20
PT Konferenz-Poster
AB
Prion protein (PrP), the main agent of Transmissible Spongiform Encephalopathies (TSE), may remain in soil in an active form, becoming the soil a potential reservoir of TSE infectivity. In the framework of an European project, investigations are being performed to understand processes and factors that control the interactions of PrP with organo and organo-mineral soil components by using a recombinant, non pathogenic form of PrP.
Adsorption studies of PrP were performed onto a montmorillonite (Mt), an Al(OH)x-Mt complex (6 mmol Al per g Mt) and two organo-mineral complexes obtained by coprecipitating at pH 6.0 Al, gallic (GA) or tannic (TA) acid in the presence of Mt [Al(OH)x-GA-Mt and Al(OH)x-TA-Mt; GA or TA/Al molar ratio of 0.1]. The sequence of protein adsorption onto the sorbents at all the studied pHs was as follows: Mt >> Al(OH)x-GA-Mt >= Al(OH)x-Mt > Al(OH)x-TA-Mt.
Further studies were carried out on the polymerisation of catechol, a very common humus starting material, by birnessite, a strong oxidative catalyst of phenol polymerization, for simulating processes naturally occurring in soil and involving biopolymers such as proteins and enzymes. Catechol and birnessite were incubated under different buffered experimental conditions in terms of initial catechol concentration (1-5 mM), incubation time (1-24 h), and amount of birnessite (0.2-5 mg ml-1). A consistent entrapment of PrP molecules occurred in catechol polymers, depending on the polymerization intensity. The amount of the entrapped protein increased up to 100% with 3 and 5 mM catechol. Protein molecules were also consistently adsorbed (55%) on birnessite surfaces.
Desorption studies performed with phosphate at pH 7.0 and 8.0 showed that prion protein was quite persistently associated with both organic aggregates and pre-formed organo-mineral complexes.
IN Das normale Prionprotein bindet gut an die Tonart Montmorillonit, an das nach dem schottischen Ort Birness genannte Manganoxid-Mineral Birnessit sowie an den ebenfalls in vielen Böden reichlich vorhandenen pflanzlichen Gerbstoff Catechin.
AD M.A.Rao, M.Ricciardella, A.Violante, L.Gianfreda, Dipartimento di Scienze del Suolo, della Pianta e dell'Ambiente, Università degli Studi di Napoli Frederico II, Portici, Italy
SP englisch
PO Deutschland