2.7 Å cryo-EM structure of ex vivo RML prion fibrils

Szymon W. Manka; Wenjuan Zhang; Adam Wenborn; Jemma Betts; Susan Joiner; Helen R. Saibil; John Collinge; Jonathan D. F. Wadsworth

doi:10.1038/s41467-022-30457-7

Nature Communications (Jul 2022)

2.7 Å cryo-EM structure of ex vivo RML prion fibrils

Szymon W. Manka,
Wenjuan Zhang,
Adam Wenborn,
Jemma Betts,
Susan Joiner,
Helen R. Saibil,
John Collinge,
Jonathan D. F. Wadsworth

Affiliations

Szymon W. Manka: MRC Prion Unit at UCL, Institute of Prion Diseases, University College London
Wenjuan Zhang: MRC Prion Unit at UCL, Institute of Prion Diseases, University College London
Adam Wenborn: MRC Prion Unit at UCL, Institute of Prion Diseases, University College London
Jemma Betts: MRC Prion Unit at UCL, Institute of Prion Diseases, University College London
Susan Joiner: MRC Prion Unit at UCL, Institute of Prion Diseases, University College London
Helen R. Saibil: Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London
John Collinge: MRC Prion Unit at UCL, Institute of Prion Diseases, University College London
Jonathan D. F. Wadsworth: MRC Prion Unit at UCL, Institute of Prion Diseases, University College London

DOI: https://doi.org/10.1038/s41467-022-30457-7
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 11

Abstract

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High-resolution structures of mammalian prions have remained elusive. Here, Manka et al. report the cryo-EM structure of infectious RML prion fibrils from mice. Structural similarity with recently reported infectious 263K prion fibrils from hamsters now suggests a common prion architecture.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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