The first transmissions of human prion diseases to rodents used guinea pigs (Gps, Cavia porcellus). Later, transgenic mice expressing human or chimeric human/mouse PrP replaced Gps, but the small size of the mouse limits some investigations. To investigate the fidelity of strain-specific prion transmission to Gps, we inoculated 'type 1' and 'type 2' prion strains into Gps, and we measured the incubation times and determined the strain-specified size of the unglycosylated, protease-resistant (r) PrP(Sc) fragment. Prions passaged once in Gps from cases of sporadic (s) Creutzfeldt-Jakob disease (CJD) and Gerstmann-Sträussler-Scheinker (GSS) disease caused by the P102L mutation were used, as well as human prions from a variant (v) CJD case, bovine prions from bovine spongiform encephalopathy (BSE) and mouse-passaged scrapie prions. Variant CJD and BSE prions transmitted to all the inoculated Gps with incubation times of 367 ± 4 and 436 ± 28 days, respectively. On second passage in Gps, vCJD and BSE prions caused disease in 287 ± 4 and 310 ± 4 days, whereas sCJD and GSS prions transmitted in 237 ± 4 and 279 ± 19 days, respectively. Although hamster Sc237 prions transmitted to two of three Gps after 574 and 792 days, mouse-passaged RML and 301V prion strains, the latter derived from BSE prions, failed to transmit disease to Gps. Those Gps inoculated with vCJD or BSE prions exhibited 'type 2' unglycosylated, rPrP(Sc) (19 kDa), whereas those receiving sCJD or GSS prions displayed 'type 1' prions (21 kDa), as determined by western blotting. Such strain-specific properties were maintained in Gps as well as mice expressing a chimeric human/mouse transgene. Gps may prove particularly useful in further studies of novel human prions such as those causing vCJD.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3164925 | PMC |
http://dx.doi.org/10.1038/labinvest.2011.89 | DOI Listing |
Front Vet Sci
November 2024
Department of Biological Sciences, Andong National University, Andong, Republic of Korea.
Background: Prion diseases are irreversible infectious neurodegenerative diseases caused by a contagious form of prion protein (PrP). Since chronic wasting disease (CWD)-infected white-tailed deer are strong carriers of the prion seed through corpses via scavenger animals, preemptive control based on genetic information for a culling system is necessary. However, the risk of CWD-related genetic variants has not been fully evaluated.
View Article and Find Full Text PDFCureus
November 2024
Acute Medicine, Peterborough City Hospital, Peterborough, GBR.
Creutzfeldt-Jakob disease (CJD) is a fatal neurodegenerative disorder that leads to rapid cognitive decline, dementia, and neurological deterioration. CJD has several forms, including sporadic CJD (sCJD), which accounts for most cases, and variant CJD (vCJD), linked to exposure to bovine spongiform encephalopathy (BSE or mad cow disease). The disease is caused by abnormal prion proteins, which damage the brain and lead to death.
View Article and Find Full Text PDFMicrobiol Immunol
January 2025
Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo, Japan.
Bovine spongiform encephalopathy (BSE) is a prion disease in cattle caused by classical-type (C-), L-type (L-), or H-type (H-) BSE prions. While C-BSE prions are zoonotic agents responsible for variant Creutzfeldt-Jakob disease, L- and H-BSE prions are believed not to be connected to human prion diseases. However, L-BSE prions have been shown to transmit to cynomolgus monkeys (Macaca fascicularis), suggesting they may have zoonotic potential.
View Article and Find Full Text PDFFront Vet Sci
October 2024
Research Centre for Encephalopathies and Transmissible Emerging Diseases. Institute for Health Research Aragón (IIS) - WOAH Reference Laboratory for BSE and Scrapie, University of Zaragoza, Zaragoza, Spain.
Introduction: According to the neuroinflammatory hypothesis, a cytokine-mediated host innate immune response may be involved in the mechanisms that contribute to the process of neurodegeneration. Specifically, regarding prion diseases, some experimental murine models have evidenced an altered profile of inflammatory intermediaries. However, the local inflammatory response has rarely been assessed, and never in tissues from different natural models throughout the progression of neurodegeneration.
View Article and Find Full Text PDFPathogens
July 2024
Friedrich-Loeffler-Institut, 17493 Greifswald-Isle of Riems, Germany.
After the detection of bovine spongiform encephalopathy (BSE), and a zoonotic transmissible spongiform encephalopathy (TSE) caused by the pathological prion protein (PrP) in two goats, the investigation of goat prions became of greater interest. Therefore, a broad collection of European goat TSE isolates, including atypical scrapie, CH1641 and goat BSE as reference prion strains were biochemically characterised and subsequently inoculated into seven rodent models for further analysis (already published results of this comprehensive study are reviewed here for comparative reasons). We report here the histopathological and immunohistochemical data of this goat TSE panel, obtained after the first passage in Tgshp IX (tg-shARQ) mice, which overexpress the ovine prion protein.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!