<abstract xmlns="http://www.w3.org/1999/xhtml"><bold>Introduction:</bold> 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.<bold>Material and Methods:</bold> 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.<bold>Results:</bold> 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.<bold>Conclusion:</bold> 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.</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.

Exploration of the main sites for the transformation of normal prion protein (PrPC) into pathogenic prion protein (PrPsc)

China-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062,

Biological safety protection third-level laboratory, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223,

Section of Epidemiology and Public Health, College of Veterinary and Animal Sciences, Jhang 35200,

Journal of Veterinary Research

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Exploration of the main sites for the transformation of normal prion protein (PrP) into pathogenic prion protein (PrP)

Introduction: The functions and mechanisms of prion proteins (PrPC) are currently unknown, but most experts believe that deformed or pathogenic prion proteins...

Exploration of the main sites for the transformation of normal prion protein (PrP^C) into pathogenic prion protein (PrP^sc)

Published Online: Apr 04, 2017

Page range: 11 - 22

Received: Sep 13, 2016

Accepted: Mar 10, 2017

DOI: https://doi.org/10.1515/jvetres-2017-0002

Keywords
mice, brain, prion proteins, myelin sheath, particle aggregation

© 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.

Exploration of the main sites for the transformation of normal prion protein (PrPC) into pathogenic prion protein (PrPsc)

Published Online: Apr 04, 2017

Page range: 11 - 22

Received: Sep 13, 2016

Accepted: Mar 10, 2017

DOI: https://doi.org/10.1515/jvetres-2017-0002

Keywordsmice, brain, prion proteins, myelin sheath, particle aggregation

© 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.

Exploration of the main sites for the transformation of normal prion protein (PrP^C) into pathogenic prion protein (PrP^sc)

Keywords
mice, brain, prion proteins, myelin sheath, particle aggregation