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Title: Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion
Author: Sabaté Lagunas, Raimon
Espargaró Colomé, Alba
Saupe, Sven J.
Ventura, Salvador
Keywords: Amiloïdosi
Issue Date: 28-Oct-2009
Publisher: BioMed Central
Abstract: The formation of amyloid aggregates is related to the onset of a number of human diseases. Recent studies provide compelling evidence for the existence of related fibrillar structures in bacterial inclusion bodies (IBs). Bacteria might thus provide a biologically relevant and tuneable system to study amyloid aggregation and how to interfere with it. Particularly suited for such studies are protein models for which structural information is available in both IBs and amyloid states. The only high-resolution structure of an infectious amyloid state reported to date is that of the HET-s prion forming domain (PFD). Importantly, recent solid-state NMR data indicates that the structure of HET-s PFD in IBs closely resembles that of the infectious fibrils. Here we present an exhaustive conformational characterization of HET-s IBs in order to establish the aggregation of this prion in bacteria as a consistent cellular model in which the effect of autologous or heterologous protein quality machineries and/or anti-aggregational and anti-prionic drugs can be further studied.
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It is part of: Microbial Cell Factories, 2009, vol. 8, p. 56
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ISSN: 1475-2859
Appears in Collections:Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)

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