The fraction (P4) containing scrapie infectivity was obtained by treatment of scrapie-infected mouse brains with the detergent sarcosyl, differential centrifugation, and proteolytic enzyme digestion. Scrapie infectivity in the P4 fraction was purified 239-2,390 times with respect to protein. Similar fractions were also prepared from the brain of a sheep naturally infected with scrapie. Morphological observation of the P4 fractions revealed that the main components were unique rods of 3-5 X 60-200 nm, which resembled scrapie-associated fibrils (SAF) or prion rods. The P4 fractions formed three major broad bands of polypeptides with molecular weights (MWs) of about 24.5K, 21K, and 17K dalton (Kd) in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and some low MW polypeptides were also present in the fraction. Rabbits immunized with this fraction prepared from mouse brains raised antibodies against the three major polypeptides.
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http://dx.doi.org/10.1111/j.1348-0421.1986.tb00927.x | DOI Listing |
Genet Sel Evol
December 2024
Faculty of Agricultural Sciences, Agricultural University of Iceland, 311, Borgarnes, Iceland.
Background: Scrapie is an infectious prion disease in sheep. Selective breeding for resistant genotypes of the prion protein gene (PRNP) is an effective way to prevent scrapie outbreaks. Genotyping all selection candidates in a population is expensive but existing pedigree records can help infer the probabilities of genotypes in relatives of genotyped animals.
View Article and Find Full Text PDFFront 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 PDFBiomed Environ Sci
November 2024
National Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, NHC Key Laboratory for Medical Virology and Viral Diseases, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 102206, China;Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Zhejiang University, Hangzhou 100084, Zhejiang, China;Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan 430071, Hubei, China;China Academy of Chinese Medical Sciences, Beijing 100700, China;Shanghai Institute of Infectious Disease and Biosafety, Shanghai 200003, China.
Objective: To analyze the relationship between Chemokine IP10 and its receptor CXCR3 during prion infection.
Methods: We investigated the increases in IP10 signals, primarily localized in neurons within the brains of scrapie-infected mice, using western blotting, ELISA, co-immunoprecipitation, immunohistochemistry, immunofluorescence assays, and RT-PCR.
Results: Both CXCR3 levels and activation were significantly higher in the brains of scrapie-infected mice and prion-infected SMB-S15 cells.
Arch Microbiol
November 2024
Department of Biological Sciences, Munster Technological University, Bishopstown, Cork, T12 P928, Ireland.
Prions are proteinaceous infectious particles implicated in fatal neurodegenerative disorders known as prion diseases. Herein, we provide an overview of prion biology, emphasizing the structural, functional, and evolutionary aspects of prions, along with their potential applications in protein engineering. Understanding the structure-function relationships of both healthy and disease-associated prion proteins enables a deeper understanding of the mechanisms of prion-induced neurotoxicity.
View Article and Find Full Text PDFJ Assoc Physicians India
November 2024
Associate Professor, Department of General Medicine, Medical College Baroda, Vadodara, Gujarat, India.
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