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4 results on '"Saibil HR"'

1. Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin

Author

Leung C, Dudkina NV, Lukoyanova N, Hodel AW, Farabella I, Pandurangan AP, Jahan N, Pires Damaso M, Osmanovi&#7, D, Reboul CF, Dunstone MA, Andrew PW, Lonnen R, Topf M, Saibil HR, Hoogenboom BW., Leung C, Dudkina NV, Lukoyanova N, Hodel AW, Farabella I, Pandurangan AP, Jahan N, Pires Damaso M, Osmanovi D, Reboul CF, Dunstone MA, Andrew PW, Lonnen R, Topf M, Saibil HR, and Hoogenboom BW.

Published
2014

3. Ex vivo mammalian prions are formed of paired double helical prion protein fibrils

Author

Terry, C, Wenborn, A, Gros, N, Sells, J, Joiner, S, Hosszu, LLP, Tattum, MH, Panico, S, Clare, DK, Collinge, J, Saibil, HR, Wadsworth, JDF, Terry, Cassandra, Wenborn, Adam, Gros, Nathalie, Sells, Jessica, Joiner, Susan, Hosszu, Laszlo L. P, Tattum, M. Howard, Panico, Salvatore, Clare, Daniel K, Collinge, John, Saibil, Helen R, and Wadsworth, Jonathan D. F.

Subjects
Biochemistry & Molecular Biology, Science & Technology, TRANSMISSION, STRAINS, animal diseases, prion disease, electron tomography, PROPAGATION, DISEASE, nervous system diseases, MODEL, prion, TITER, lcsh:Biology (General), prion protein, prion structure, ASSAY, Life Sciences & Biomedicine, lcsh:QH301-705.5, SCRAPIE PRIONS
Abstract

Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained obscure. Recently, we developed novel methods to obtain exceptionally pure preparations of prions from mouse brain and showed that pathogenic PrP in these high-titre preparations is assembled into rod-like assemblies. Here, we have used precise cell culture-based prion infectivity assays to define the physical relationship between the PrP rods and prion infectivity and have used electron tomography to define their architecture. We show that infectious PrP rods isolated from multiple prion strains have a common hierarchical assembly comprising twisted pairs of short fibres with repeating substructure. The architecture of the PrP rods provides a new structural basis for understanding prion infectivity and can explain the inability to systematically generate high-titre synthetic prions from recombinant PrP.

Published
2016

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