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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Multifaceted Role of Sialylation in Prion Diseases

Ilia V Baskakov1, Elizaveta Katorcha1

  • 1Department of Anatomy and Neurobiology, Center for Biomedical Engineering and Technology, University of Maryland School of Medicine Baltimore, MD, USA.

Frontiers in Neuroscience
|August 24, 2016
PubMed

Insights

Sialylation of prion protein (PrP) glycans influences prion diseases by affecting infectivity, replication barriers, and strain characteristics. Understanding sialylation

Area of Science:

  • Neuroscience
  • Biochemistry
  • Infectious Diseases

Background:

  • Prion diseases are linked to misfolded prion protein (PrPSc).
  • Sialylation of PrP N-linked glycans is known but its role in pathogenesis is unclear.
  • Sialic acids are increasingly recognized for their role in host-pathogen interactions.

Purpose of the Study:

  • To review the current understanding of sialylation's role in prion protein (PrP) diseases.
  • To explore how PrP sialylation impacts prion infectivity, replication, and strain characteristics.

Main Methods:

  • Literature review of studies on prion protein sialylation.
  • Analysis of factors controlling PrPSc sialylation.
  • Critical review of sialylation's potential roles in transmission, tropism, toxicity, and disease etiology.

Main Results:

  • Sialylation of PrPSc glycans correlates with prion infectivity.
  • Glycan sialylation influences the prion replication barrier and defines strain-specific glycoform ratios.
  • Sialylation may play a role in interspecies transmission, lymphotropism, and toxicity.

Conclusions:

  • Sialylation is a critical factor in prion disease pathogenesis, influencing infectivity and strain diversity.
  • Further research into sialylation's role may offer insights into prion disease etiology, including sporadic forms.
Keywords:
amyloidneuraminidaseprion diseaseprionssialic acidsialylationsialyltransferasespecies barrier

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