Limited understanding of the functional diversity of N-linked glycans as a major gap of prion biology
PublisherTaylor and Francis Inc.
MetadataShow full item record
AbstractAmong a broad range of hypotheses on the molecular nature of transmissible spongiform encephalopathy or scrapie agents discussed in 1960s was a hypothesis of self-replicating polysaccharides. While the studies of the past 40 years provided unambiguous proof that this is not the case, emerging evidence suggests that carbohydrates in the form of sialylated N-linked glycans, which are a constitutive part of mammalian prions or PrPSc, are essential in determining prion fate in an organism. The current extra-view article discusses recent advancements on the role of N-linked glycans and specifically their sialylation status in controlling prion fate. In addition, this manuscript introduces a new concept on the important role of strain-specific functional carbohydrate epitopes on the PrPSc surface as main determinants of strain-specific biologic features. According to this concept, individual strain-specific folding patterns of PrPSc govern selection of PrPC sialoglycoforms expressed by a host that can be accommodated within particular PrPSc structures. Strain-specific patterns of functional carbohydrate epitopes formed by N-linked glycans on PrPSc surfaces define strain-specific biologic features. As a constitutive part of PrPSc, the individual strain-specific patterns of carbohydrate epitopes propagate faithfully within a given host as long as individual strain-specific PrPSc structures are maintained, ensuring inheritance of strain-specific biologic features.
secondary lymphoid organs
Identifier to cite or link to this itemhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85015898275&doi=10.1080%2f19336896.2017.1301338&partnerID=40&md5=6c7a56a6afcde142b9a52dd69061e1ff; http://hdl.handle.net/10713/10908
- Prion Strain-Specific Structure and Pathology: A View from the Perspective of Glycobiology.
- Authors: Baskakov IV, Katorcha E, Makarava N
- Issue date: 2018 Dec 18
- Analyses of N-linked glycans of PrP<sup>Sc</sup> revealed predominantly 2,6-linked sialic acid residues.
- Authors: Katorcha E, Baskakov IV
- Issue date: 2017 Nov
- Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio.
- Authors: Katorcha E, Makarava N, Savtchenko R, Baskakov IV
- Issue date: 2015 Nov 18
- Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism.
- Authors: Makarava N, Chang JC, Baskakov IV
- Issue date: 2020 Jan 28
- Sialylation Controls Prion Fate <i>in Vivo</i>.
- Authors: Srivastava S, Katorcha E, Daus ML, Lasch P, Beekes M, Baskakov IV
- Issue date: 2017 Feb 10