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Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion
Sabaté, Raimon (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecularar)

Data: 2009
Resum: 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.
Drets: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades. Creative Commons
Llengua: Anglès.
Document: article ; publishedVersion
Publicat a: Microbial cell factories, Vol. 8, N. 56 (October 2009) , p. 1-10, ISSN 1475-2859

DOI: 10.1186/1475-2859-8-56

10 p, 5.7 MB

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