Location and stability of a recombinant ovine prion protein in synthetic humic-like mineral complexes

Location and stability of a recombinant prion protein (recPrP) and its interaction with humic-like complexes were investigated by low-temperature ashing (LTA), thermal gravimetric (TG), and scanning electron microscopy (SEM) analyses. Humic-like complexes were obtained by abiotic polymerization of catechol, one of the possible precursors of soil humic matter, through the catalysis of birnessite, a manganese oxide common in soil environment. The recPrP was immobilized in organomineral complexes via sorption or entrapment. Complexes were treated by LTA, allowing the controlled removal of organic matter layer by layer, from the external to the internal side, with minimal disturbance of mineral constituents. Thermal gravimetric and SEM analyses were performed on specimens before and after LTA treatment. Entrapped recPrP, compared with sorbed, resulted less easily accessible to LTA treatment and showed a higher thermal stability by TGA analyses. On the basis of these findings, we hypothesize that the processes leading to newly formed organic complexes can enhance prion stability in soil and thus influence the environmental diffusion of infectivity.