Transmission of BSE by blood transfusion in sheep

Houston, Fiona; Foster, Jim; Chong, Angela; Hunter, Nora; Bostock, Christopher J.

doi:10.1016/s0140-6736(00)02719-7

Cited by 500 publications

(312 citation statements)

References 5 publications

Supporting

Mentioning

289

Contrasting

Unclassified

Order By: Relevance

“…This is the first published report, to our knowledge, of immunochemically detectable PrP Sc amplified from blood cells from sheep naturally infected with scrapie using PMCA. Detection of PrP Sc in blood is consistent with the demonstration of infectivity by blood transfusion from infected sheep (Houston et al, 2000;Hunter et al, 2002) in which disease was transmitted in both the plasma and buffy coat fractions from symptomatic and pre-symptomatic animals. In blood we were able to detect PrP Sc amplified after 144 cycles from 10 6 cells (~0.5 ml of blood) in 100 % of sheep tested.…”

Section: Discussionsupporting

confidence: 78%

In vitro amplification of PrPSc derived from the brain and blood of sheep infected with scrapie

Thorne

Terry

2008

Journal of General Virology

101

116

View full text Add to dashboard Cite

Scrapie is a fatal, naturally transmissible, neurodegenerative prion disease that affects sheep and goats and is characterized by the accumulation of a misfolded protein, PrPSc, converted from host-encoded PrPc, in the central nervous system of affected animals. Highly efficient in vitro conversion of host PrPc to PrPSc has been achieved in models of scrapie and in natural prion diseases by protein misfolding cyclic amplification (PMCA). Here, we demonstrate amplification, by serial PMCA, of PrPSc from individual sources of scrapie-infected sheep. Efficiency of amplification was affected by the pairing of the source of PrPSc with the control brain substrate of different genotypes of PrP. In line with previous studies, efficiency of amplification was greatly enhanced with the addition of a synthetic polyanion, polyadenylic acid (PolyA), facilitating rapid detection of low levels of PrPSc from body fluids such as blood. To this end PrPSc was amplified, in a 3 day PMCA assay, from blood leukocyte preparations from VRQ/VRQ scrapie-affected sheep at clinical end point. While PolyA-assisted PMCA resulted in spontaneous conversion of PrPc, we were able to distinguish blood samples from unaffected and affected sheep under controlled conditions. This study demonstrates that highly efficient amplification of PrPSc can be achieved for ovine scrapie from both brain and blood from naturally infected sheep and shows potential applications for improvements in current diagnostics and pre-mortem testing.

show abstract

Section: Discussionsupporting

confidence: 78%

In vitro amplification of PrPSc derived from the brain and blood of sheep infected with scrapie

Thorne

Terry

2008

Journal of General Virology

101

116

View full text Add to dashboard Cite

show abstract

“…A recent report showed that blood from CWD-infected deer contained infectivity and could transmit prion disease via a blood transfusion [50]. This finding recapitulates findings of blood infectivity transferred via transfusion from vCJD affected humans [61] and experimental from scrapie sick sheep [32], and indicates that prion transport throughout the body may include the blood as a potential vehicle.…”

Section: Cwd Prion Spread and Target Organssupporting

confidence: 75%

A prion disease of cervids: Chronic wasting disease

2008

View full text Add to dashboard Cite

-Chronic wasting disease (CWD) is a prion disease of deer, elk, and moose, initially recognized in Colorado mule deer. The discovery of CWD beyond the borders of Colorado and Wyoming, in Canada and as far east as New York, has led to its emergence as a prion disease of international importance. Epidemiological studies indicate that CWD is horizontally transmitted among free-ranging animals, potentially indirectly by prion-containing secreta or excreta contaminating the environment. Experimental CWD transmission attempts to other wild and domestic mammals and to transgenic mice expressing the prion protein of cattle, sheep, and humans have shed light on CWD species barriers. Transgenic mice expressing the cervid prion protein have proven useful for assessing the genetic influences of Prnp polymorphisms on CWD susceptibility. Accumulating evidence of CWD pathogenesis indicates that the misfolded prion protein or prion infectivity seems to be widely disseminated in many nonneural organs and in blood. This review highlights contemporary research findings in this prion disease of free-ranging wildlife.

show abstract

“…Three human-to-human transmissions of variant Creutzfeldt-Jakob disease were reported in the United Kingdom in the past two years [1][2][3] . TSE infectivity in blood was also demonstrated in natural and experimental animal models such hamster 4,5 , mouse 6 , and sheep 7 . This funding has supported the development of a prototype assay for TSE infection using hamsters infected with the 263K stain of scrapie.…”

Section: Introductionmentioning

confidence: 85%

Development of an Assay for the Detection of PrPres in Blood and Urine Based on PMCA Assay and ELISA Methods

Rohwer¹,

Gregori²

2008

View full text Add to dashboard Cite

Public reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden to Department of Defense, Washington Headquarters Services, Directorate for Information Operations and Reports (0704-0188), 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to any penalty for failing to comply with a collection of information if it does not display a currently valid OMB control number. PLEASE DO NOT RETURN YOUR FORM TO THE ABOVE ADDRESS. REPORT DATE (DD-MM-YYYY) SPONSORING / MONITORING AGENCY NAME(S) AND ADDRESS(ES) 10. SPONSOR/MONITOR'S ACRONYM(S) U.S. Army Medical Research and Materiel Command Fort Detrick, Maryland 21702-5012 SPONSOR/MONITOR'S REPORT NUMBER(S) DISTRIBUTION / AVAILABILITY STATEMENTApproved for Public Release; Distribution Unlimited SUPPLEMENTARY NOTES ABSTRACTThe focus of this program is the development of a pre-clinical blood-based TSE diagnostic. The assay is been developed with plasma from hamsters infected with the 263K strain of scrapie. The assay has shown high sensitivity and specificity and good reproducibility. In this funding period we addressed two critical issues: Proteinase K (PK) digestion to discriminate PrPc, the normal form of the protein and PrPres the infection-specific form of the protein and denaturation of PrPres in plasma. The first issue was partially resolved when we discovered that PK digestion of plasma PrPc can be conducted without addition of SDS. We can now titer plasma and determine which PK condition is appropriate to digests all PrPc and no infectivity. We also identified the condition for plasma PrPres denaturation. We are currently developing the reagents and protocols for a "proof of principle" titration in plasma after PK digestion. This is the last step in the development of a complete plasma diagnostic assay. In a large, long term, "limiting dilution" titration of untreated, whole urine from scrapie infected hamsters, we have now conclusively shown that urine from TSE infected animals contains significant levels of infectivity and we will have a precise titer in another 6 months. Urine could thereby be an alternative substrate for disease detection. Bladder and kidney are also infectious.

show abstract

Transmission of BSE by blood transfusion in sheep

Cited by 500 publications

References 5 publications

In vitro amplification of PrPSc derived from the brain and blood of sheep infected with scrapie

In vitro amplification of PrPSc derived from the brain and blood of sheep infected with scrapie

A prion disease of cervids: Chronic wasting disease

Development of an Assay for the Detection of PrPres in Blood and Urine Based on PMCA Assay and ELISA Methods

Contact Info

Product

Resources

About