Limited understanding of the functional diversity of N-linked glycans as a major gap of prion biology
dc.contributor.author | Baskakov, I.V. | |
dc.date.accessioned | 2019-09-19T18:35:43Z | |
dc.date.available | 2019-09-19T18:35:43Z | |
dc.date.issued | 2017 | |
dc.identifier.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85015898275&doi=10.1080%2f19336896.2017.1301338&partnerID=40&md5=6c7a56a6afcde142b9a52dd69061e1ff | |
dc.identifier.uri | http://hdl.handle.net/10713/10908 | |
dc.description.abstract | Among 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. | en_US |
dc.description.uri | https://doi.org/10.1080/19336896.2017.1301338 | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | Taylor and Francis Inc. | en_US |
dc.relation.ispartof | Prion | |
dc.subject | carbohydrate epitopes | en_US |
dc.subject | microglia | en_US |
dc.subject | N-linked glycans | en_US |
dc.subject | prion | en_US |
dc.subject | prion diseases | en_US |
dc.subject | secondary lymphoid organs | en_US |
dc.subject | sialic acid | en_US |
dc.subject | sialylation | en_US |
dc.title | Limited understanding of the functional diversity of N-linked glycans as a major gap of prion biology | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1080/19336896.2017.1301338 | |
dc.identifier.pmid | 28324664 |