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N-terminal Domain of Prion Protein Directs Its Oligomeric Association

Trevitt, Clare R. ; Hosszu, Laszlo L.P. ; Batchelor, Mark ; Panico, Silvia ; Terry, Cassandra ; Nicoll, Andrew J. ; Risse, Emmanuel ; Taylor, William A. ; Sandberg, Malin K. ; Al-Doujaily, Huda ; Linehan, Jacqueline M. ; Saibil, Helen R. ; Scott, David J. ; Collinge, John ; Waltho, Jonathan P. ; Clarke, Anthony R.

The Journal of biological chemistry, 2014-09, Vol.289 (37), p.25497-25508 [Periódico revisado por pares]

United States: Elsevier Inc

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Título:
N-terminal Domain of Prion Protein Directs Its Oligomeric Association
Autor: Trevitt, Clare R. ; Hosszu, Laszlo L.P. ; Batchelor, Mark ; Panico, Silvia ; Terry, Cassandra ; Nicoll, Andrew J. ; Risse, Emmanuel ; Taylor, William A. ; Sandberg, Malin K. ; Al-Doujaily, Huda ; Linehan, Jacqueline M. ; Saibil, Helen R. ; Scott, David J. ; Collinge, John ; Waltho, Jonathan P. ; Clarke, Anthony R.
Assuntos: Amyloid - chemistry ; Amyloid - metabolism ; Humans ; Hydrogen-Ion Concentration ; Prion Diseases - metabolism ; Prion Diseases - pathology ; Prions - chemistry ; Prions - metabolism ; Protein Folding ; Protein Structure and Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins - chemistry
É parte de: The Journal of biological chemistry, 2014-09, Vol.289 (37), p.25497-25508
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Present address: Dept. of Molecular Biology and Biotechnology, Krebs Institute for Biomolecular Research, University of Sheffield, Sheffield, S10 2TN, UK.
Director of D-Gen Limited.
Present address: Dept. of Life Sciences, Imperial College, London SW7 2AZ, UK.
Shareholders of D-Gen Limited, an academic spin-out company in the field of prion disease. D-Gen markets the ICSM35 antibody used in this study.
Supported in part by the Science and Technology Facilities Council (UK).
Both authors contributed equally to this manuscript.
Descrição: The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. It is increasingly recognized that small non-fibrillar β-sheet-rich oligomers of PrP may be of crucial importance in the prion disease process. Here, we characterize the structure of a well defined β-sheet-rich oligomer, containing ∼12 PrP molecules, and often enclosing a central cavity, formed using full-length recombinant PrP. The N-terminal region of prion protein (residues 23–90) is required for the formation of this distinct oligomer; a truncated form comprising residues 91–231 forms a broad distribution of aggregated species. No infectivity or toxicity was found using cell and animal model systems. This study demonstrates that examination of the full repertoire of conformers and assembly states that can be accessed by PrP under specific experimental conditions should ideally be done using the full-length protein.
Editor: United States: Elsevier Inc
Idioma: Inglês

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N-terminal Domain of Prion Protein Directs Its Oligomeric Association

United States: Elsevier Inc

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