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In Vitro and In Vivo Evidence towards Fibronectin's Protective Effects against Prion Infection.

M Carmen Garza1,2, Sang-Gyun Kang1,3, Chiye Kim1,3

  • 1Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB T6G 2M8, Canada.

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Extracellular fibronectin (FN) may prevent prion diseases by limiting the replication of the pathogenic prion protein (PrPSc). Low FN levels in muscle tissue may increase susceptibility to prion infection, highlighting the role of extracellular matrix in prion tropism.

Keywords:
extracellular matrix (ECM)k fibronectinmusclemyotubeprionreserve cellsscrapietropism

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Area of Science:

  • Neuroscience
  • Infectious Diseases
  • Biochemistry

Background:

  • Prion diseases are characterized by pathogenic prion protein (PrPSc) accumulation in the central nervous system and peripheral tissues.
  • PrPSc presence in peripheral tissues, including muscle, raises public health concerns regarding potential transmission through food.
  • Muscle tissue's role in prion propagation is not fully understood, necessitating research into factors influencing prion infection establishment.

Purpose of the Study:

  • To investigate factors influencing prion replication in muscle tissue using in vitro myotube cultures.
  • To identify specific proteins in the extracellular matrix that interact with PrPSc and affect its infectivity.
  • To determine the role of fibronectin (FN) in modulating prion susceptibility in muscle cells and tissues.

Main Methods:

  • Utilized differentiated C2C12 myoblast cell line (dC2C12) for in vitro myotube cultures.
  • Examined the association of PrPSc with extracellular matrix proteins, particularly fibronectin (FN).
  • Assessed prion infectivity using standard scrapie cell assays and conducted immunohistopathological analyses on scrapie-infected sheep tissues.

Main Results:

  • PrPSc was found to be tightly associated with extracellular matrix proteins, primarily fibronectin (FN).
  • Interaction of PrPSc with FN significantly decreased prion infectivity in vitro.
  • Prion-resistant cells exhibited a FN-rich extracellular matrix, while prion-susceptible myotubes had low FN levels.
  • Scrapie-infected sheep tissues showed prion susceptibility correlated with undetectable FN levels, with PrPSc deposits absent in FN-expressing tissues.

Conclusions:

  • Extracellular fibronectin (FN) may function as a natural barrier, inhibiting prion replication.
  • The composition of the extracellular matrix, specifically FN content, is a critical determinant of prion tropism in different tissues.
  • Understanding the role of extracellular matrix components like FN is crucial for assessing and mitigating the risk of prion transmission through muscle tissue.