Glycoform-Selective Prions in Sporadic and Genetic Variably Protease-Sensitive Prionopathies

Wang, Zerui; Yuan, Jing; Gilliland, Tricia; Gerasimenko, Maria; Shah, Syed Zahid Ali; Zou, Wen-Quan

doi:10.1007/978-3-031-20565-1_20

Prions and Diseases 2023

DOI: 10.1007/978-3-031-20565-1_20

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Glycoform-Selective Prions in Sporadic and Genetic Variably Protease-Sensitive Prionopathies

Zerui Wang

Jing Yuan

Tricia Gilliland

et al.

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Efficient transmission of human prion diseases to a glycan-free prion protein-expressing host

Cracco,

Cali,

Cohen

et al. 2023

Brain

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It is increasingly evident that the association of glycans with the prion protein (PrP), a major post-translational modification, significantly impacts the pathogenesis of prion diseases. A recent bioassay study has provided evidence that the presence of PrP glycans decreases spongiform degeneration (SD) and disease-related PrP (PrPD) deposition in a murine model. We challenged (PRNPN181Q/197Q) transgenic (Tg) mice expressing glycan-free human PrP (TgGlyc-), with isolates from sCJDMM2, sporadic fatal insomnia, and familial fatal insomnia, three human prion diseases that are distinct but share histotypic and PrPD features. TgGlyc- mice accurately replicated the basic histotypic features associated with the three diseases but the transmission was characterized by high attack rates, shortened incubation periods, and a greatly increased severity of the histopathology, including the presence of up to 40 times higher quantities of PrPD that formed prominent deposits. Although the engineered protease-resistant PrPD shared at least some features of the secondary structure and the presence of the anchorless PrPD variant with the wild-type PrPD, it exhibited different density gradient profiles of the PrPD aggregates and a higher stability index. The severity of the histopathological features including PrP deposition appeared to be related to the incubation period duration. These findings are clearly consistent with the protective role of the PrP glycans but also emphasize the complexity of the conformational changes that impact PrPD following glycan knock-out. Future studies will determine whether these features apply broadly to other human prion diseases or are PrPD-type dependent.

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Efficient transmission of human prion diseases to a glycan-free prion protein-expressing host

Cracco,

Cali,

Cohen

et al. 2023

Brain

View full text Add to dashboard Cite

show abstract

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Glycoform-Selective Prions in Sporadic and Genetic Variably Protease-Sensitive Prionopathies

Cited by 1 publication

References 68 publications

Efficient transmission of human prion diseases to a glycan-free prion protein-expressing host

Efficient transmission of human prion diseases to a glycan-free prion protein-expressing host

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