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Updated: Dec 8, 2025
Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
Role of sialylation in prion disease pathogenesis and prion structure
1Department of Anatomy and Neurobiology, and Center for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD, United States.
Abstract:
Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein or PrPC. Sialylation of the prion protein, a terminal modification of N-linked glycans, was discovered more than 30 years ago, yet the role of sialylation in prion pathogenesis is not well understood. This chapter summarizes current knowledge on the role of sialylation of the prion protein in prion diseases. First, we discuss recent data suggesting that sialylation of PrPSc N-linked glycans determines the fate of prion infection in an organism and control prion lymphotropism. Second, emerging evidence pointing out at the role N-glycans in neuroinflammation are discussed. Thirds, this chapter reviews a mechanism postulating that sialylated N-linked glycans are important players in defining strain-specific structures. A new hypothesis according to which individual strain-specific PrPSc structures govern selection of PrPC sialoglycoforms is discussed. Finally, this chapter explain how N-glycan sialylation control the prion replication and strain interference. In summary, comprehensive review of our knowledge on N-linked glycans and their sialylation provided in this chapter helps to answer important questions of prion biology that have been puzzling for years.
Insights
Sialylation of the prion protein (PrP) influences prion disease outcomes, including infection spread and neuroinflammation. Understanding N-glycan sialylation is key to prion biology and controlling prion replication.
Area of Science:
- Neuroscience
- Biochemistry
- Infectious Diseases
Background:
- Mammalian prions (PrPSc) are misfolded proteins crucial in prion diseases.
- Sialylation, a modification of N-linked glycans on prion proteins (PrPC), has an unclear role in disease pathogenesis.
- Prion protein sialylation is a key area for understanding prion biology.
Purpose of the Study:
- To summarize current knowledge on the role of prion protein sialylation in prion diseases.
- To explore how N-glycan sialylation impacts prion infection, lymphotropism, and neuroinflammation.
- To discuss mechanisms of strain-specific prion structures and replication control.
Main Methods:
- Review of existing scientific literature and data on prion protein sialylation.
- Analysis of emerging evidence on N-glycans and neuroinflammation.
- Discussion of proposed mechanisms and hypotheses regarding prion-host interactions.
Main Results:
- PrPSc N-linked glycan sialylation influences prion infection fate and lymphotropism.
- N-glycans play a role in prion-induced neuroinflammation.
- Sialylated N-linked glycans are critical for defining prion strain structures.
- Prion strain structures may select specific PrPC sialoglycoforms.
Conclusions:
- N-glycan sialylation is a critical factor in controlling prion replication and strain interference.
- Understanding sialylation provides insights into long-standing questions in prion biology.
- This review highlights the importance of sialylation in prion pathogenesis and offers new avenues for research.
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