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  1. Article ; Online: Transmission of Raccoon-Passaged Chronic Wasting Disease Agent to White-Tailed Deer.

    Cassmann, Eric D / Frese, Alexis J / Moore, S Jo / Greenlee, Justin J

    Viruses

    2022  Volume 14, Issue 7

    Abstract: The transmission characteristics of prion diseases are influenced by host prion protein sequence and, therefore, the host species. Chronic wasting disease (CWD), a prion disease of cervids, has widespread geographical distribution throughout North ... ...

    Abstract The transmission characteristics of prion diseases are influenced by host prion protein sequence and, therefore, the host species. Chronic wasting disease (CWD), a prion disease of cervids, has widespread geographical distribution throughout North America and occurs in both wild and farmed populations. CWD prions contaminate the environment through scattered excrement and decomposing carcasses. Fresh carcasses with CWD prions are accessible by free-ranging mesopredators such as raccoons and may provide a route of exposure. Previous studies demonstrated the susceptibility of raccoons to CWD from white-tailed deer. In this study, we demonstrate that white-tailed deer replicate raccoon-passaged CWD prions which results in clinical disease similar to intraspecies CWD transmission. Six white-tailed deer were oronasally inoculated with brain homogenate from a raccoon with CWD. All six deer developed clinical disease, had widespread lymphoid distribution of misfolded CWD prions (PrP
    MeSH term(s) Animals ; Deer ; Prion Diseases ; Prions/metabolism ; Raccoons ; Wasting Disease, Chronic
    Chemical Substances Prions
    Language English
    Publishing date 2022-07-20
    Publishing country Switzerland
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14071578
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Experimental Oronasal Transmission of Chronic Wasting Disease Agent from White-Tailed Deer to Suffolk Sheep.

    Cassmann, Eric D / Moore, S Jo / Greenlee, Justin J

    Emerging infectious diseases

    2021  Volume 27, Issue 12, Page(s) 3156–3158

    Abstract: Chronic wasting disease (CWD) is a fatal prion disease of cervids. We examined host range of CWD by oronasally inoculating Suffolk sheep with brain homogenate from a CWD-positive white-tailed deer. Sixty months after inoculation, 1/7 sheep had ... ...

    Abstract Chronic wasting disease (CWD) is a fatal prion disease of cervids. We examined host range of CWD by oronasally inoculating Suffolk sheep with brain homogenate from a CWD-positive white-tailed deer. Sixty months after inoculation, 1/7 sheep had immunoreactivity against the misfolded form of prion protein in lymphoid tissue. Results were confirmed by mouse bioassay.
    MeSH term(s) Animals ; Deer ; Mice ; Prion Diseases ; Prions/genetics ; Sheep ; Wasting Disease, Chronic
    Chemical Substances Prions
    Language English
    Publishing date 2021-11-22
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1380686-5
    ISSN 1080-6059 ; 1080-6040
    ISSN (online) 1080-6059
    ISSN 1080-6040
    DOI 10.3201/eid2712.204978
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Disease phenotype of classical sheep scrapie is changed upon experimental passage through white-tailed deer.

    Kokemuller, Robyn D / Moore, S Jo / Bian, Jifeng / West Greenlee, M Heather / Greenlee, Justin J

    PLoS pathogens

    2023  Volume 19, Issue 12, Page(s) e1011815

    Abstract: Prion agents occur in strains that are encoded by the structure of the misfolded prion protein (PrPSc). Prion strains can influence disease phenotype and the potential for interspecies transmission. Little is known about the potential transmission of ... ...

    Abstract Prion agents occur in strains that are encoded by the structure of the misfolded prion protein (PrPSc). Prion strains can influence disease phenotype and the potential for interspecies transmission. Little is known about the potential transmission of prions between sheep and deer. Previously, the classical US scrapie isolate (No.13-7) had a 100% attack rate in white-tailed deer after oronasal challenge. The purpose of this study was to test the susceptibility of sheep to challenge with the scrapie agent after passage through white-tailed deer (WTD scrapie). Lambs of various prion protein genotypes were oronasally challenged with WTD scrapie. Sheep were euthanized and necropsied upon development of clinical signs or at the end of the experiment (72 months post-inoculation). Enzyme immunoassay, western blot, and immunohistochemistry demonstrated PrPSc in 4 of 10 sheep with the fastest incubation occurring in VRQ/VRQ sheep, which contrasts the original No.13-7 inoculum with a faster incubation in ARQ/ARQ sheep. Shorter incubation periods in VRQ/VRQ sheep than ARQ/ARQ sheep after passage through deer was suggestive of a phenotype change, so comparisons were made in ovinized mice and with sheep with known strains of classical sheep scrapie: No. 13-7 and x-124 (that has a more rapid incubation in VRQ/VRQ sheep). After mouse bioassay, the WTD scrapie and x-124 isolates have similar incubation periods and PrPSc conformational stability that are markedly different than the original No. 13-7 inoculum. Furthermore, brain tissues of sheep with WTD scrapie and x-124 scrapie have similar patterns of immunoreactivity that are distinct from sheep with No. 13-7 scrapie. Multiple lines of evidence suggest a phenotype switch when No. 13-7 scrapie prions are passaged through deer. This represents one example of interspecies transmission of prions resulting in the emergence or selection of new strain properties that could confound disease eradication and control efforts.
    MeSH term(s) Sheep ; Animals ; Mice ; Scrapie/metabolism ; Deer/metabolism ; Prion Proteins/genetics ; Prions/metabolism ; Genotype ; Phenotype
    Chemical Substances Prion Proteins ; Prions
    Language English
    Publishing date 2023-12-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011815
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Transmission of Raccoon-Passaged Chronic Wasting Disease Agent to White-Tailed Deer

    Cassmann, Eric D. / Frese, Alexis J. / Moore, S. Jo / Greenlee, Justin J.

    Viruses. 2022 July 20, v. 14, no. 7

    2022  

    Abstract: The transmission characteristics of prion diseases are influenced by host prion protein sequence and, therefore, the host species. Chronic wasting disease (CWD), a prion disease of cervids, has widespread geographical distribution throughout North ... ...

    Abstract The transmission characteristics of prion diseases are influenced by host prion protein sequence and, therefore, the host species. Chronic wasting disease (CWD), a prion disease of cervids, has widespread geographical distribution throughout North America and occurs in both wild and farmed populations. CWD prions contaminate the environment through scattered excrement and decomposing carcasses. Fresh carcasses with CWD prions are accessible by free-ranging mesopredators such as raccoons and may provide a route of exposure. Previous studies demonstrated the susceptibility of raccoons to CWD from white-tailed deer. In this study, we demonstrate that white-tailed deer replicate raccoon-passaged CWD prions which results in clinical disease similar to intraspecies CWD transmission. Six white-tailed deer were oronasally inoculated with brain homogenate from a raccoon with CWD. All six deer developed clinical disease, had widespread lymphoid distribution of misfolded CWD prions (PrPSᶜ), and had neuropathologic lesions with PrPSᶜ accumulation in the brain. The presence of PrPSᶜ was confirmed by immunohistochemistry, enzyme-linked immunoassay, and western blot. The western blot migration pattern of raccoon-passaged CWD was different from white-tailed deer CWD. Transmission of raccoon CWD back to white-tailed deer resulted in an interposed molecular phenotype that was measurably different from white-tailed deer CWD.
    Keywords Odocoileus virginianus ; Procyon lotor ; Western blotting ; amino acid sequences ; brain ; deer ; enzyme-linked immunosorbent assay ; excreta ; exposure pathways ; geographical distribution ; hosts ; immunohistochemistry ; mesopredators ; phenotype ; prions ; North America
    Language English
    Dates of publication 2022-0720
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14071578
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: Increased Attack Rates and Decreased Incubation Periods in Raccoons with Chronic Wasting Disease Passaged through Meadow Voles.

    Moore, S Jo / Carlson, Christina M / Schneider, Jay R / Johnson, Christopher J / Greenlee, Justin J

    Emerging infectious diseases

    2022  Volume 28, Issue 4, Page(s) 793–801

    Abstract: Chronic wasting disease (CWD) is a naturally-occurring neurodegenerative disease of cervids. Raccoons (Procyon lotor) and meadow voles (Microtus pennsylvanicus) have previously been shown to be susceptible to the CWD agent. To investigate the potential ... ...

    Abstract Chronic wasting disease (CWD) is a naturally-occurring neurodegenerative disease of cervids. Raccoons (Procyon lotor) and meadow voles (Microtus pennsylvanicus) have previously been shown to be susceptible to the CWD agent. To investigate the potential for transmission of the agent of CWD from white-tailed deer to voles and subsequently to raccoons, we intracranially inoculated raccoons with brain homogenate from a CWD-affected white-tailed deer (CWD
    MeSH term(s) Animals ; Arvicolinae ; Deer ; Incidence ; Infectious Disease Incubation Period ; Neurodegenerative Diseases ; Raccoons ; Wasting Disease, Chronic/epidemiology
    Language English
    Publishing date 2022-03-23
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1380686-5
    ISSN 1080-6059 ; 1080-6040
    ISSN (online) 1080-6059
    ISSN 1080-6040
    DOI 10.3201/eid2804.210271
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Transmission of the atypical/Nor98 scrapie agent to Suffolk sheep with VRQ/ARQ, ARQ/ARQ, and ARQ/ARR genotypes.

    Cassmann, Eric D / Mammadova, Najiba / Moore, S Jo / Benestad, Sylvie / Greenlee, Justin J

    PloS one

    2021  Volume 16, Issue 2, Page(s) e0246503

    Abstract: Scrapie is a transmissible spongiform encephalopathy that occurs in sheep. Atypical/Nor98 scrapie occurs in sheep that tend to be resistant to classical scrapie and it is thought to occur spontaneously. The purpose of this study was to test the ... ...

    Abstract Scrapie is a transmissible spongiform encephalopathy that occurs in sheep. Atypical/Nor98 scrapie occurs in sheep that tend to be resistant to classical scrapie and it is thought to occur spontaneously. The purpose of this study was to test the transmission of the Atypical/Nor98 scrapie agent in three genotypes of Suffolk sheep and characterize the distribution of misfolded prion protein (PrPSc). Ten sheep were intracranially inoculated with brain homogenate from a sheep with Atypical/Nor98 scrapie. All sheep with the ARQ/ARQ and ARQ/ARR genotypes developed Atypical/Nor98 scrapie confirmed by immunohistochemistry, and one sheep with the VRQ/ARQ genotype had detectable PrPSc consistent with Atypical/Nor98 scrapie at the experimental endpoint of 8 years. Sheep with mild early accumulations of PrPSc in the cerebellum had concomitant retinal PrPSc. Accordingly, large amounts of retinal PrPSc were identified in clinically affected sheep and sheep with dense accumulations of PrPSc in the cerebellum.
    MeSH term(s) Animals ; Genotype ; Haplotypes ; Polymorphism, Genetic ; Prion Proteins/genetics ; Scrapie/genetics ; Scrapie/transmission ; Sheep/genetics
    Chemical Substances Prion Proteins
    Language English
    Publishing date 2021-02-11
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0246503
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Swarming with grounding and deaths in pipistrelle bats.

    Duff, J P / Bell, C P / Barlow, A M / Moore, S Jo / Barnett, E A

    The Veterinary record

    2021  Volume 189, Issue 3, Page(s) 120

    MeSH term(s) Animals ; Behavior, Animal ; Chiroptera/psychology ; Death ; Female ; Government Agencies ; Male ; United Kingdom/epidemiology
    Language English
    Publishing date 2021-08-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 390015-0
    ISSN 2042-7670 ; 0042-4900
    ISSN (online) 2042-7670
    ISSN 0042-4900
    DOI 10.1002/vetr.807
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Sheep Are Susceptible to the Bovine Adapted Transmissible Mink Encephalopathy Agent by Intracranial Inoculation and Have Evidence of Infectivity in Lymphoid Tissues.

    Cassmann, Eric D / Moore, S Jo / Smith, Jodi D / Greenlee, Justin J

    Frontiers in veterinary science

    2019  Volume 6, Page(s) 430

    Abstract: Transmissible mink encephalopathy (TME) is a food borne prion disease. Epidemiological and experimental evidence suggests similarities between the agents of TME and L-BSE. This experiment demonstrates the susceptibility of four different genotypes of ... ...

    Abstract Transmissible mink encephalopathy (TME) is a food borne prion disease. Epidemiological and experimental evidence suggests similarities between the agents of TME and L-BSE. This experiment demonstrates the susceptibility of four different genotypes of sheep to the bovine adapted TME agent by intracranial inoculation. The four genotypes of sheep used in this experiment had polymorphisms corresponding to codons 136, 154, and 171 of the prion gene: V
    Language English
    Publishing date 2019-11-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2834243-4
    ISSN 2297-1769
    ISSN 2297-1769
    DOI 10.3389/fvets.2019.00430
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Raccoons accumulate PrP

    Moore, S Jo / Smith, Jodi D / Richt, Jürgen A / Greenlee, Justin J

    Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc

    2019  Volume 31, Issue 2, Page(s) 200–209

    Abstract: Prion diseases are neurodegenerative diseases characterized by the accumulation of misfolded prion protein ( ... ...

    Abstract Prion diseases are neurodegenerative diseases characterized by the accumulation of misfolded prion protein (PrP
    MeSH term(s) Animals ; Blotting, Western ; Brain ; Deer ; Disease Susceptibility ; Mink ; PrPSc Proteins/metabolism ; Prion Diseases/metabolism ; Prion Diseases/veterinary ; Raccoons ; Sheep ; Wasting Disease, Chronic/etiology ; Wasting Disease, Chronic/metabolism
    Chemical Substances PrPSc Proteins
    Language English
    Publishing date 2019-01-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 287603-6
    ISSN 1943-4936 ; 1040-6387
    ISSN (online) 1943-4936
    ISSN 1040-6387
    DOI 10.1177/1040638718825290
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Experimental inoculation of CD11c

    Mammadova, Najiba / Cassmann, Eric D / Moore, S Jo / Nicholson, Eric M / Greenlee, Justin J

    Access microbiology

    2020  Volume 2, Issue 9, Page(s) acmi000155

    Abstract: Many studies have demonstrated prion infectivity in whole blood and blood components in a variety of transmissible spongiform encephalopathies of livestock and rodents, and variant Creutzfeldt-Jakob disease in humans, as well as an association between ... ...

    Abstract Many studies have demonstrated prion infectivity in whole blood and blood components in a variety of transmissible spongiform encephalopathies of livestock and rodents, and variant Creutzfeldt-Jakob disease in humans, as well as an association between pathogenic prion protein (PrP
    Language English
    Publishing date 2020-07-28
    Publishing country England
    Document type Journal Article
    ISSN 2516-8290
    ISSN (online) 2516-8290
    DOI 10.1099/acmi.0.000155
    Database MEDical Literature Analysis and Retrieval System OnLINE

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