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dc.contributor.authorMakarava, N.
dc.contributor.authorChang, J.C.-Y.
dc.contributor.authorBaskakov, I.V.
dc.date.accessioned2020-02-10T15:17:15Z
dc.date.available2020-02-10T15:17:15Z
dc.date.issued2020
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85078845459&doi=10.3390%2fijms21030828&partnerID=40&md5=59a6239d5bedae0fd0b2f573ec72d134
dc.identifier.urihttp://hdl.handle.net/10713/11981
dc.description.abstractMammalian 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. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.en_US
dc.description.sponsorshipThis research was funded by the National Institute of Health Grants R01 NS045585 and R01 AI128925.en_US
dc.description.urihttps://doi.org/10.3390/ijms21030828en_US
dc.language.isoen_USen_US
dc.publisherMDPI AGen_US
dc.relation.ispartofInternational Journal of Molecular Sciences
dc.subjectN-linked glycansen_US
dc.subjectPrion diseaseen_US
dc.subjectPrion strainsen_US
dc.subjectPrionsen_US
dc.subjectSialic aciden_US
dc.subjectSialylationen_US
dc.subjectThalamusen_US
dc.subjectTwo-dimensional gel electrophoresisen_US
dc.titleRegion-specific sialylation pattern of prion strains provides novel insight into prion neurotropismen_US
dc.typeArticleen_US
dc.identifier.doi10.3390/ijms21030828


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