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dc.contributor.authorBaskakov, I.V.
dc.date.accessioned2019-09-19T18:35:43Z
dc.date.available2019-09-19T18:35:43Z
dc.date.issued2017
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85015898275&doi=10.1080%2f19336896.2017.1301338&partnerID=40&md5=6c7a56a6afcde142b9a52dd69061e1ff
dc.identifier.urihttp://hdl.handle.net/10713/10908
dc.description.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.en_US
dc.description.urihttps://doi.org/10.1080/19336896.2017.1301338en_US
dc.language.isoen_USen_US
dc.publisherTaylor and Francis Inc.en_US
dc.relation.ispartofPrion
dc.subjectcarbohydrate epitopesen_US
dc.subjectmicrogliaen_US
dc.subjectN-linked glycansen_US
dc.subjectprionen_US
dc.subjectprion diseasesen_US
dc.subjectsecondary lymphoid organsen_US
dc.subjectsialic aciden_US
dc.subjectsialylationen_US
dc.titleLimited understanding of the functional diversity of N-linked glycans as a major gap of prion biologyen_US
dc.typeArticleen_US
dc.identifier.doi10.1080/19336896.2017.1301338
dc.identifier.pmid28324664


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