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Uptake of Prions into Plants

Posted Sep 27 2013 5:13pm
Presentation Abstract  

 

 
Title: Uptake of Prions into Plants 

 

Session Title: Current Science of Chronic Wasting Disease: What Have We Learned in the Last 5 Years? 

 

Session Number: 27 

 

Session Time: Monday, Oct 07, 2013, 8:30 AM -12:20 PM 

 

Presentation Time: Monday, Oct 07, 2013, 11:00 AM -11:20 AM 

 

Presentation Number: 8 

 

Author(s): Christopher Johnson, U.S. Geological Survey, Madison, WI, Contact: cjjohnson@usgs.gov 

 

Abstract Body:

 

Chronic wasting disease (CWD) and scrapie-infected animals shed infectious prions during both the preclinical and clinical phases of disease. Contamination of environments with prions released from animals or from infected carcasses appears to contribute to the transmission of these diseases. Previous work has suggested that soil may serve as an environmental disease reservoir. Vegetation is ubiquitous in CWD-contaminated environments and plants are known to absorb a variety of substances from soil, ranging from nutrients to contaminants. The uptake of proteins from soil into plants has been documented for many years and we have been investigating the uptake of prions into plants in vitro. Using laser scanning confocal microscopy, we observed root uptake of fluorescently-tagged, abnormal prion protein in the model plant Arabidopsis thaliana, as well as the crop plants alfalfa (Medicago sativa), barley (Hordeum vulgare) and tomato (Solanum lycopersicum). Using serial protein misfolding cyclic amplification, a sensitive biochemical prion detection method, we have found evidence of prions in aerial tissues from these species, as well as maize (Zea mays). Both stems and leaves of A. thaliana grown in culture media containing prions are infectious when injected into mice and oral bioassays are underway for A. thaliana and other plants. Our results suggest that prions are taken up by plants and that contaminated plants may represent a previously unrecognized risk of human, domestic species and wildlife exposure to CWD and scrapie agents.

 



 

 


Prion2013

 

 

Friday, August 09, 2013

 

***CWD TSE prion, plants, vegetables, and the potential for environmental contamination

 


 

 

 
PRION2013 CONGRESSIONAL ABSTRACTS CWD

 

 

Sunday, August 25, 2013

 

HD.13: CWD infection in the spleen of humanized transgenic mice

 

Liuting Qing and Qingzhong Kong

 

Case Western Reserve University; Cleveland, OH USA

 

Chronic wasting disease (CWD) is a widespread prion disease in free-ranging and captive cervid species in North America, and there is evidence suggesting the existence of multiple CWD strains. The susceptibility of human CNS and peripheral organs to the various CWD prion strains remains largely unclear. Current literature suggests that the classical CWD strain is unlikely to infect human brain, but the potential for peripheral infection by CWD in humans is unknown. We detected protease-resistant PrpSc in the spleens of a few humanized transgenic mice that were intracerebrally inoculated with natural CWD isolates, but PrpSc was not detected in the brains of any of the CWD-inoculated mice. Our ongoing bioassays in humanized Tg mice indicate that intracerebral challenge with such PrpSc-positive humanized mouse spleen already led to prion disease in most animals. These results indicate that the CWD prion may have the potential to infect human peripheral lymphoid tissues.

 

 

Oral.15: Molecular barriers to zoonotic prion transmission: Comparison of the ability of sheep, cattle and deer prion disease isolates to convert normal human prion protein to its pathological isoform in a cell-free system

 

Marcelo A.Barria,1 Aru Balachandran,2 Masanori Morita,3 Tetsuyuki Kitamoto,4 Rona Barron,5 Jean Manson,5 Richard Kniqht,1 James W. lronside1 and Mark W. Head1

 

1National CJD Research and Surveillance Unit; Centre for Clinical Brain Sciences; School of Clinical Sciences; The University of Edinburgh; Edinburgh, UK; 2National and OIE Reference Laboratory for Scrapie and CWD; Canadian Food Inspection Agency; Ottawa Laboratory; Fallowfield. ON Canada; 3Infectious Pathogen Research Section; Central Research Laboratory; Japan Blood Products Organization; Kobe, Japan; 4Department of Neurological Science; Tohoku University Graduate School of Medicine; Sendai. Japan; 5Neurobiology Division; The Roslin Institute and R(D)SVS; University of Edinburgh; Easter Bush; Midlothian; Edinburgh, UK

 

Background. Bovine spongiform encephalopathy (BSE) is a known zoonotic prion disease, resulting in variant Creurzfeldt- Jakob disease (vCJD) in humans. In contrast, classical scrapie in sheep is thought to offer little or no danger to human health. However, a widening range of prion diseases have been recognized in cattle, sheep and deer. The risks posed by individual animal prion diseases to human health cannot be determined a priori and are difficult to assess empirically. The fundamemal event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein (PrPC) to its pathological isoform (PrPSc). Here we report the use of a rapid molecular conversion assay to test whether brain specimens from different animal prion diseases are capable of seeding the conversion of human PrPC ro PrPSc.

 

Material and Methods. Classical BSE (C-type BSE), H-type BSE, L-type BSE, classical scrapie, atypical scrapie, chronic wasting disease and vCJD brain homogenates were tested for their ability to seed conversion of human PrPC to PrPSc in protein misfolding cyclic amplification (PMCA) reactions. Newly formed human PrPSc was detected by protease digestion and western blotting using the antibody 3F4.

 

Results. C-type BSE and vCJD were found to efficiently convert PrPC to PrPSc. Scrapie failed to convert human PrPC to PrPSc. Of the other animal prion diseases tested only chronic wasting disease appeared to have the capability ro convert human PrPC to PrPSc. The results were consistent whether the human PrPC came from human brain, humanised transgenic mouse brain or from cultured human cells and the effect was more pronounced for PrPC with methionine at codon 129 compared with that with valine.

 

Conclusion. Our results show that none of the tested animal prion disease isolates are as efficient as C-type BSE and vCJD in converting human prion protein in this in vitro assay. However, they also show that there is no absolute barrier ro conversion of human prion protein in the case of chronic wasting disease.

 

 

 

PRION2013 CONGRESSIONAL ABSTRACTS CWD

 

 

Sunday, August 25, 2013

 

***Chronic Wasting Disease CWD risk factors, humans, domestic cats, blood, and mother to offspring transmission

 


 

 

Sunday, July 21, 2013

 

*** As Chronic Wasting Disease CWD rises in deer herd, what about risk for humans?

 


 

 

 
> sCJDMM1-2 should be considered as a separate entity at this time.

 

> All of the Heidenhain variants were of the methionine/ methionine type 1 molecular subtype.

 

 


 

 


 

 

 

PRION2013 CONGRESSIONAL ABSTRACTS CWD

 

 

 

Thursday, August 08, 2013

 

Characterization of the first case of naturally occurring chronic wasting disease in a captive red deer (Cervus elaphus) in North America

 


 

 

Sunday, September 01, 2013

 

hunting over gut piles and CWD TSE prion disease

 


 

 

Wednesday, September 04, 2013

 

cwd - cervid captive livestock escapes, loose and on the run in the wild...

 


 

 

Tuesday, September 10, 2013

 

Review and Updates of the USDA-APHIS Veterinary Services (VS) National Chronice Wasting Disease (CWD) Program 2012-2013

 


 

 

 

Sunday, August 11, 2013

 

Creutzfeldt-Jakob Disease CJD cases rising North America updated report August 2013

 

Creutzfeldt-Jakob Disease CJD cases rising North America with Canada seeing an extreme increase of 48% between 2008 and 2010

 


 

 

 

Friday, August 16, 2013

 

*** Creutzfeldt-Jakob disease (CJD) biannual update August 2013 U.K. and Contaminated blood products induce a highly atypical prion disease devoid of PrPres in primates

 


 

 

 

Sunday, September 08, 2013

 

Iatrogenic Creutzfeldt-Jakob disease via surgical instruments and decontamination possibilities for the TSE prion

 


 

 

 

Tuesday, September 17, 2013

 

USAHA 116TH ANNUAL MEETING October 18 – 24, 2012 CWD, Scrapie, BSE, TSE prion (September 17, 2013)

 


 

 

 

*** The potential impact of prion diseases on human health was greatly magnified by the recognition that interspecies transfer of BSE to humans by beef ingestion resulted in vCJD. While changes in animal feed constituents and slaughter practices appear to have curtailed vCJD, there is concern that CWD of free-ranging deer and elk in the U.S. might also cross the species barrier. Thus, consuming venison could be a source of human prion disease. Whether BSE and CWD represent interspecies scrapie transfer or are newly arisen prion diseases is unknown. Therefore, the possibility of transmission of prion disease through other food animals cannot be ruled out. There is evidence that vCJD can be transmitted through blood transfusion. There is likely a pool of unknown size of asymptomatic individuals infected with vCJD, and there may be asymptomatic individuals infected with the CWD equivalent. These circumstances represent a potential threat to blood, blood products, and plasma supplies.

 

 


 

 
 

Wednesday, September 25, 2013

 

Wisconsin Hunters will again be able to have adult deer tested for chronic wasting disease CWD

 


 

 

kind regards, terry
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