2014
DOI: 10.1016/j.soilbio.2013.10.005
|View full text |Cite
|
Sign up to set email alerts
|

Humic substances interfere with detection of pathogenic prion protein

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

1
11
0

Year Published

2014
2014
2018
2018

Publication Types

Select...
5

Relationship

3
2

Authors

Journals

citations
Cited by 6 publications
(12 citation statements)
references
References 47 publications
1
11
0
Order By: Relevance
“…As shown by mild thermal denaturation, FA inhibit the conversion of recPrP to a PK-resistant PrP Sc -like conformation, which is not available for cell internalization when bound to FA [32]. A recent study has reported that HA-adsorbed PrP Sc strains resulted slightly less infectious when intracerebrally inoculated in hamsters [55]. Nevertheless, further investigations in living organisms are needed to verify this hypothesis.…”
Section: Discussionmentioning
confidence: 99%
“…As shown by mild thermal denaturation, FA inhibit the conversion of recPrP to a PK-resistant PrP Sc -like conformation, which is not available for cell internalization when bound to FA [32]. A recent study has reported that HA-adsorbed PrP Sc strains resulted slightly less infectious when intracerebrally inoculated in hamsters [55]. Nevertheless, further investigations in living organisms are needed to verify this hypothesis.…”
Section: Discussionmentioning
confidence: 99%
“…There are several potential explanations for the observed decline in PrP CWD signal upon incubation with humic acids. One possibility is that a component of SOM interferes with PrP CWD during immunoblotting which could alter migration, limit entry into the gel, or interfere with membrane transfer [27]. We found that PrP CWD migrated as expected (20–35 kDa) with or without HA, thus altered migration during SDS-PAGE is not the reason for decreasing PrP signal.…”
Section: Resultsmentioning
confidence: 60%
“…Another study [25] has shown HA-like substances copolymerize with recPrP and irreversibly incorporate it into their structure, creating complexes which decrease the efficiency of recPrP recovery. The PrP insolubilization and co-precipitation by aggregation with HA without altering PrP secondary structure, which potentially can decrease prion detectability and reduce their bioavailability, also were discussed [26,27]. Similar prion interactions with another high-organic matrix (e.g.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Although not confirmed in natural environment, this hypothesis found supports in previous study in animal models showing that prions bound to a soil rich in HS are less infectious than PrP Sc adsorbed to montmorillonite [ 19 ]. Another study has reported that HA-adsorbed PrP Sc strains resulted slightly less infectious when intracerebrally inoculated in hamsters [ 30 ]. However, if HS-bound prions retain infectivity upon oral ingestion in ruminants and in cervids is still debated [ 20 ].…”
Section: Introductionmentioning
confidence: 99%