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Identification of the Highly Polymorphic Prion Protein Gene () in Frogs ).

Animals (Basel)

January 2025

Department of Biological Sciences, Andong National University, Andong 36729, Republic of Korea.

Prion diseases are fatal neurodegenerative diseases that can be transmitted by infectious protein particles, PrPs, encoded by the endogenous prion protein gene (). The origin of prion seeds is unclear, especially in non-human hosts, and this identification is pivotal to preventing the spread of prion diseases from host animals. Recently, an abnormally high amyloid propensity in prion proteins (PrPs) was found in a frog, of which the genetic variations in the gene have not been investigated.

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Unlocking Neuroinflammation: A Balanced Art for Therapeutics of Prion Disease.

ACS Chem Neurosci

January 2025

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.

Neuroinflammation plays a dual role in prion diseases, contributing both to the clearance of misfolded scrapie-like prion protein and to neuropathology through chronic activation of inflammatory pathways. Key mechanisms, including M-CSF/CSF1R signaling, NLRP3 inflammasome activation, and the Galectin-3/TREM2 axis, etc., highlight the complexity of targeting neuroinflammation for therapeutic intervention.

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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.

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Activation of IP10/CXCR3 Signaling is Highly Coincidental with PrP Deposition in the Brains of Scrapie-Infected Mice.

Biomed 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.

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Current diagnostic methods for prion diseases only work in late stages of the disease when neurodegeneration is irreversible. Therefore, biomarkers that can detect the disease before the onset of clinical symptoms are necessary. High-throughput discovery proteomics is of great interest in the search for such molecules.

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