Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion.
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.
Sabaté
Raimon
R
Departament de Bioquímica I Biologia Molecular and Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain. Raimon.Sabate@uab.cat
Espargaró
Alba
A
Saupe
Sven J
SJ
Ventura
Salvador
S
D000682:Amyloid / Q000737:chemistry*; D019286:Endopeptidase K / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry*; D002479:Inclusion Bodies / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011328:Prions / Q000737:chemistry*; D017434:Protein Structure, Tertiary
D000682:Amyloid; D005656:Fungal Proteins; C083891:HET-S protein, Podospora anserina; D011328:Prions; D019286:Endopeptidase K