Infectious Prions in the Saliva and Blood of Deer with Chronic Wasting Disease

Mathiason, Candace K.; Powers, Jenny G.; Dahmes, Sallie J.; Osborn, David A; Miller, Karl V.; Warren, Robert J.; Mason, Gary L.; Hays, Sheila A.; Hayes-Klug, Jeanette; Seelig, Davis; Wild, Margaret A.; Wolfe, Lisa L.; Spraker, Terry R.; Miller, Michael W.; Sigurdson, Christina J.; Telling, Glenn C.; Hoover, Edward A.

doi:10.1126/science.1132661

Cited by 456 publications

(465 citation statements)

References 24 publications

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“…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: 77%

“…Potential transmission mechanisms range from spread via direct contact among animals to environmental exposure through grazing in areas contaminated by prioninfected secretions, excretions (saliva, urine, feces), tissues (placenta), or decomposed carcasses. Recently, in a breakthrough finding, saliva from CWD-infected deer was shown to transmit prion disease [50]. An additional experiment by Miller et al showed that CWDinfected carcasses allowed to decay naturally in confined pastures can lead to CWD infections in captive deer, demonstrating the potential for environmental contamination to spread infection [55].…”

Section: Disease Control Challenges Posed By Cwdmentioning

confidence: 99%

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A prion disease of cervids: Chronic wasting disease

2008

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-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.

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Section: Cwd Prion Spread and Target Organssupporting

confidence: 77%

Section: Disease Control Challenges Posed By Cwdmentioning

confidence: 99%

A prion disease of cervids: Chronic wasting disease

2008

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“…Some endemic pockets have been notified. Body fluids are infectious and saliva is suspected to favor the horizontal, particularly efficient, dissemination of the disease [132]. At variance with scrapie, the placenta is poorly infectious, suggesting that transmission from mother-to-lamb might be rather low [135].…”

Section: Strain Diversity In Cwd?mentioning

confidence: 99%

Prion agent diversity and species barrier

2008

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-Mammalian prions are the infectious agents responsible for transmissible spongiform encephalopathies (TSE), a group of fatal, neurodegenerative diseases, affecting both domestic animals and humans. The most widely accepted view to date is that these agents lack a nucleic acid genome and consist primarily of PrP Sc , a misfolded, aggregated form of the host-encoded cellular prion protein (PrP C ) that propagates by autocatalytic conversion and accumulates mainly in the brain. The BSE epizooty, allied with the emergence of its human counterpart, variant CJD, has focused much attention on two characteristics that prions share with conventional infectious agents. First, the existence of multiple prion strains that impose, after inoculation in the same host, specific and stable phenotypic traits such as incubation period, molecular pattern of PrP Sc and neuropathology. Prion strains are thought to be enciphered within distinct PrP Sc conformers. Second, a transmission barrier exists that restricts the propagation of prions between different species. Here we discuss the possible situations resulting from the confrontation between species barrier and prion strain diversity, the molecular mechanisms involved and the potential of interspecies transmission of animal prions, including recently discovered forms of TSE in ruminants.prion / strain / misfolding / species barrier / PrP Table of Mammalian prion diseases or transmissible spongiform encephalopathies (TSE) form a group of related, invariably fatal neurodegenerative disorders of both animals and humans. The brain pathology consists of spongiosis, astrocytosis, neuronal loss and neural tissue from affected individuals contains an infectious agent, the prion, setting these diseases apart from other neurodegenerative diseases. Prion replication is thought to involve in essence the self-perpetuating conversion of the host-encoded cellular prion protein (PrP C ) into a misfolded form (PrP Sc ) that tends to aggregate and may be neurotoxic (for reviews [1,157]). Prion replication may also occur in lymphoid tissues but is there poorly if not pathogenic (for review [126], [133]). PrP C is a protein with two variably occupied glycosylation sites. It is attached at the outer of the plasma membrane by a glycosylphosphatidylinositol anchor. Its secondary structure is rich in alpha-helix and the protein is likely to be in a monomeric state in mild detergents. While its precise physiological function has not been assigned, PrP C is essential for prion replication and neurotoxicity to occur [57,129]. Upon infection, PrP C is refolded -without apparent post-translational modification -into beta-sheet -rich PrP Sc , initially in the presence of exogenous PrP Sc and then by an autocatalytic process. It leads to the formation of aggregates, sometimes of amyloid type, that can be differentiated from PrP C because of their partial resistance to protease digestion and of their insolubility into non-denaturing detergents [153]. Proteinase K, the most commonly used protease, di...

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“…Multiple studies showed that TSE infectivity is present in the blood of experimental rodents, sheep with natural and experimental scrapie and experimental BSE, and deer affected with chronic wasting disease (CWD) (15)(16)(17)(18)(19)(20). PrP TSE has been successfully detected in the following: in whole blood of experimentally infected mice and hamsters, in sheep with natural scrapie and experimental BSE, and in white-tailed deer afflicted with CWD (21)(22)(23); in buffy coats of hamsters and sheep experimentally infected with scrapie (24 -26), as well as in plasma of mice and hamsters with scrapie; and in sheep and white-tailed deer naturally and experimentally infected with scrapie and CWD, respectively (27)(28)(29)(30).…”

mentioning

confidence: 99%

First Demonstration of Transmissible Spongiform Encephalopathy-associated Prion Protein (PrPTSE) in Extracellular Vesicles from Plasma of Mice Infected with Mouse-adapted Variant Creutzfeldt-Jakob Disease by in Vitro Amplification

Saá

Yakovleva

Castro

et al. 2014

Journal of Biological Chemistry

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Background: Prions can be transmitted by blood transfusion, but their origin and distribution in blood are unknown. Results: Prions were detected in plasma extracellular vesicles from preclinical and clinically sick mice. Conclusion: Prions associate with blood-circulating extracellular vesicles. Significance: These findings provide information about prion distribution in blood and set the groundwork for novel prion removal and disease diagnosis technologies.

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Infectious Prions in the Saliva and Blood of Deer with Chronic Wasting Disease

Cited by 456 publications

References 24 publications

A prion disease of cervids: Chronic wasting disease

A prion disease of cervids: Chronic wasting disease

Prion agent diversity and species barrier

First Demonstration of Transmissible Spongiform Encephalopathy-associated Prion Protein (PrPTSE) in Extracellular Vesicles from Plasma of Mice Infected with Mouse-adapted Variant Creutzfeldt-Jakob Disease by in Vitro Amplification

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