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Open AccessArticle

Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism

1
Center for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD 21201, USA
2
Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, MD, 21201, USA
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(3), 828; https://doi.org/10.3390/ijms21030828
Received: 18 December 2019 / Revised: 10 January 2020 / Accepted: 23 January 2020 / Published: 28 January 2020
(This article belongs to the Special Issue The Role of Glycosylation in Host-Microbial Interactions)
Mammalian prions are unconventional infectious agents that invade and replicate in an organism by recruiting a normal form of a prion protein (PrPC) and converting it into misfolded, disease-associated state referred to as PrPSc. PrPC is posttranslationally modified with two N-linked glycans. Prion strains replicate by selecting substrates from a large pool of PrPC sialoglycoforms expressed by a host. Brain regions have different vulnerability to prion infection, however, molecular mechanisms underlying selective vulnerability is not well understood. Toward addressing this question, the current study looked into a possibility that sialylation of PrPSc might be involved in defining selective vulnerability of brain regions. The current work found that in 22L -infected animals, PrPSc is indeed sialylated in a region dependent manner. PrPSc in hippocampus and cortex was more sialylated than PrPSc from thalamus and stem. Similar trends were also observed in brain materials from RML- and ME7-infected animals. The current study established that PrPSc sialylation status is indeed region-specific. Together with previous studies demonstrating that low sialylation status accelerates prion replication, this work suggests that high vulnerability of certain brain region to prion infection could be attributed to their low sialylation status. View Full-Text
Keywords: prions; prion disease; N-linked glycans; sialic acid; sialylation; prion strains; thalamus; two-dimensional gel electrophoresis prions; prion disease; N-linked glycans; sialic acid; sialylation; prion strains; thalamus; two-dimensional gel electrophoresis
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Makarava, N.; Chang, J. .-Y.; Baskakov, I.V. Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism. Int. J. Mol. Sci. 2020, 21, 828.

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