Fate of prions in soil: Trapped conformation of full-length ovine prion protein induced by adsorption on clays

Revault, M.; Quiquampoix, Hervé; Baron, Marie‐Hélène; Noinville, Sylvie

doi:10.1016/j.bbagen.2005.05.005

Cited by 55 publications

(50 citation statements)

References 36 publications

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“…Either the infective or the benign forms of prion proteins are able to strongly bind to mineral [8][9][10][11][12] and organic soil components [13][14][15]. PrP Sc can be displaced from environmental compartments to soil, but this does not necessarily decrease its infectivity [10,16].…”

Section: Introductionmentioning

confidence: 99%

Interaction of a Recombinant Prion Protein with Organo-Mineral Complexes as Assessed by FT-IR and CPMAS 13C NMR Analysis

Russo¹,

Gianfreda²,

Conte³

et al. 2010

TOMRJ

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Prion proteins are considered as the main agents for the Transmissible Spongiform Encephalopathies (TSE). The misfolded form, PrP Sc , which is also indicated as the etiological agent for TSE, exhibits high resistance to degradation in environmental processes. Soil contamination by prion proteins is a real environmental issue since contaminated soils can become potential reservoir and diffuser for TSE infectivity. In this work, the interaction of prion protein with organomineral complexes was studied by using a recombinant non pathogenic prion protein and a model soil system. This latter was represented by a soil manganese mineral coated with polymerized catechol. FT-IR spectra showed amide I and II signals which revealed protein involvement in catechol polymers coating manganese oxide surface. CPMAS 13 C-NMR was applied to follow the complexation of the protein to the soil-like system. All the signals were attributed to C-N in peptidic bonds, alkyl chains and methyl groups. The NMR spectrum of the prion protein interacting directly with birnessite revealed disappearance of signals due to the paramagnetic nature of manganese oxide or protein abiotic degradation, while the presence of organic matter strongly reduced the disappearance of prion protein signals.

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Section: Introductionmentioning

confidence: 99%

Interaction of a Recombinant Prion Protein with Organo-Mineral Complexes as Assessed by FT-IR and CPMAS 13C NMR Analysis

Russo¹,

Gianfreda²,

Conte³

et al. 2010

TOMRJ

View full text Add to dashboard Cite

show abstract

“…98 Because the N-terminal domain is known to be flexibly-disordered and contains a high number of positively-charged amino acids, it may play a significant role in electrostatic attraction to negatively-charged mineral surfaces. 70 The N-terminal domain is lost upon desorption of PrP Sc from clay, 68 and PK-digestion is required to desorb maximal PrP Sc from clay and sandy soils. 74 More full-length recPrP adsorbs to montmorillonite than N-terminal truncated recPrP.…”

Section: Routes Of Entry Occurrence and Detection In The Environmentmentioning

confidence: 99%

“…RecPrP studies have identified electrostatic attraction between positively-charged peptides and negatively-charged mineral surfaces as the most significant adsorption mechanism. 70,71 However, since the three-dimensional structure of PrP Sc remains unknown, it is a challenge to model the specific mechanisms that are significant in PrP Sc adsorption. It is known that PrP Sc is highly insoluble and aggregated, and hydrophobic interactions could therefore play a larger role in PrP Sc sorption to amorphous clay minerals.…”

Section: Routes Of Entry Occurrence and Detection In The Environmentmentioning

confidence: 99%

“…95 One study did find that recPrP does not form β-sheets or self-aggregate, as seen in vitro, when adsorbed to clay. 70 More must be done to determine what conformational changes (if any) occur to PrP Sc when it binds to minerals and how these changes affect agent survival and infectivity.…”

Section: Routes Of Entry Occurrence and Detection In The Environmentmentioning

confidence: 99%

“…The N-domain has been shown to affect PrP aggregation, 92 and evidence suggests the N-domain might play a role in sorption to soils. 68,70,73,74,76 Therefore, both full-length and truncated prions should be used to study environmental fate.…”

Section: Routes Of Entry Occurrence and Detection In The Environmentmentioning

confidence: 99%

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Prions in the environment

Saunders

Bartelt–Hunt

Bartz

2008

Prion

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Scrapie and CWD are horizontally transmissible, and the environment likely serves as a stable reservoir of infectious prions, facilitating a sustained incidence of CWD in free-ranging cervid populations and complicating efforts to eliminate disease in captive herds. Prions will enter the environment through mortalities and/ or shedding from live hosts. Unfortunately, a sensitive detection method to identify prion contamination in environmental samples has not yet been developed. An environmentally-relevant prion model must be used in experimental studies. Changes in PrP Sc structure upon environmental exposure may be as significant as changes in PrP Sc quantity, since the structure can directly affect infectivity and disease pathology. Prions strongly bind to soil and remain infectious. Conformational changes upon adsorption, competitive sorption and potential for desorption and transport all warrant further investigation. Mitigation of contaminated carcasses or soil might be accomplished with enzyme treatments or composting in lieu of incineration.

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Impact of Extraction Methods on the Detectable Protein Complement of Metaproteomic Analyses of Marine Sediments

et al. 2017

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Metaproteomic analysis targets proteins, the catalytic entities in the habitat, thereby providing direct insights into the metabolic activity of the community studied. A major challenge still remaining for metaproteomics is the effective and comprehensive extraction of proteins from environmental samples, due to their high complexity with respect to organismic diversity and abundance range. Moreover, in certain habitats, the inherent matrix may interfere with protein extraction. In recent years, several studies reported different protein extraction methods for soils known for their complex geochemistry, but only three analyzed marine sediments that generally comprise different though similarly complex geochemistry. In this study, the impact of four different extraction methods was investigated for coastal North Sea and deep sea Pacific Ocean sediments. The extraction methods comprised (i) phenol, (ii) SDS, (iii) a mixture of SDS and phenol, and (iv) urea and thiourea. Prior to extraction, a cell and protein standard (CPS) was added to the sediment samples to trace recovery of proteins from different subcellular locations as well as dissolved BSA. While each extraction method detected distinct peptide complements, SDS-phenol extraction generally achieved highest protein yield and most comprehensive CPS protein identification. Application of two different methods was shown to further improve proteome coverage.

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Fate of prions in soil: Trapped conformation of full-length ovine prion protein induced by adsorption on clays

Cited by 55 publications

References 36 publications

Interaction of a Recombinant Prion Protein with Organo-Mineral Complexes as Assessed by FT-IR and CPMAS 13C NMR Analysis

Interaction of a Recombinant Prion Protein with Organo-Mineral Complexes as Assessed by FT-IR and CPMAS 13C NMR Analysis

Prions in the environment

Impact of Extraction Methods on the Detectable Protein Complement of Metaproteomic Analyses of Marine Sediments

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