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Journal of Veterinary Research

formerly Bulletin of the Veterinary Institute in Pulawy

4 Issues per year


IMPACT FACTOR Bull Vet Inst Pulawy 2016: 0.462

CiteScore 2016: 0.46

SCImago Journal Rank (SJR) 2015: 0.230
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ISSN
2450-8608
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Exploration of the main sites for the transformation of normal prion protein (PrPC) into pathogenic prion protein (PrPsc)

Xi-Lin Liu
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
  • Other articles by this author:
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/ Xiao-Li Feng
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
  • Biological safety protection third-level laboratory, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China
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/ Guang-Ming Wang
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
  • Other articles by this author:
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/ Bin-Bin Gong
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
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/ Waqas Ahmad
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
  • Section of Epidemiology and Public Health, College of Veterinary and Animal Sciences, Jhang 35200, Pakistan
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/ Nan-Nan Liu
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
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/ Yuan-Yuan Zhang
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
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/ Li Yang
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
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/ Hong-Lin Ren
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
  • Email
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/ Shu-Sen Cui
  • China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China
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Published Online: 2017-04-04 | DOI: https://doi.org/10.1515/jvetres-2017-0002

Abstract

Introduction: The functions and mechanisms of prion proteins (PrPC) are currently unknown, but most experts believe that deformed or pathogenic prion proteins (PrPSc) originate from PrPC, and that there may be plural main sites for the conversion of normal PrPC into PrPSc. In order to better understand the mechanism of PrPC transformation to PrPSc, the most important step is to determine the replacement or substitution site.

Material and Methods: BALB/c mice were challenged with prion RML strain and from 90 days post-challenge (dpc) mice were sacrificed weekly until all of them had been at 160 dpc. The ultra-structure and pathological changes of the brain of experimental mice were observed and recorded by transmission electron microscopy.

Results: There were a large number of pathogen-like particles aggregated in the myelin sheath of the brain nerves, followed by delamination, hyperplasia, swelling, disintegration, phagocytic vacuolation, and other pathological lesions in the myelin sheath. The aggregated particles did not overflow from the myelin in unstained samples. The phenomenon of particle aggregation persisted all through the disease course, and was the earliest observed pathological change.

Conclusion: It was deduced that the myelin sheath and lipid rafts in brain nerves, including axons and dendrites, were the main sites for the conversion of PrPC to PrPSc, and the PrPSc should be formed directly by the conversion of protein conformation without the involvement of nucleic acids.

Keywords: mice; brain; prion proteins; myelin sheath; particle aggregation

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About the article

Received: 2016-09-13

Accepted: 2017-03-10

Published Online: 2017-04-04

Published in Print: 2017-03-01


Citation Information: Journal of Veterinary Research, ISSN (Online) 2450-8608, DOI: https://doi.org/10.1515/jvetres-2017-0002.

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© 2017 Xi-Lin Liu et al., published by De Gruyter Open. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. BY-NC-ND 3.0

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