Web of Science: 10 citas, Scopus: 9 citas, Google Scholar: citas,
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria
Macedo, Bruno (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Cordeiro, Yraima (Universidade Federal do Rio de Janeiro. Faculdade de Farmácia)
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)

Fecha: 2015
Resumen: Background: An increasing number of proteins are being shown to assemble into amyloid structures that lead to pathological states. Among them, mammalian prions outstand due to their ability to transmit the pathogenic conformation, becoming thus infectious. The structural conversion of the cellular prion protein (PrP), into its misfolded pathogenic form (PrP) is the central event of prion-driven pathologies. The study of the structural properties of intracellular amyloid aggregates in general and of prion-like ones in particular is a challenging task. In this context, the evidence that the inclusion bodies formed by amyloid proteins in bacteria display amyloid-like structural and functional properties make them a privileged system to model intracellular amyloid aggregation. - Results: Here we provide the first demonstration that recombinant murine PrP and its C-terminal domain (90-231) attain amyloid conformations inside bacteria. Moreover, the inclusions formed by these two PrP proteins display conformational diversity, since they differ in fibril morphology, binding affinity to amyloid dyes, stability, resistance to proteinase K digestion and neurotoxicity. - Conclusions: Overall, our results suggest that modelling PrP amyloid formation in microbial cell factories might open an avenue for a better understanding of the structural features modulating the pathogenic impact of this intriguing protein.
Nota: Altres ajuts: ICREA Academia 2009 to S.V
Nota: Número d'acord de subvenció MINECO/BFU2013-44763P
Derechos: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. Creative Commons
Lengua: Anglès
Documento: article ; recerca ; publishedVersion
Materia: Mammalian prions ; Protein aggregation ; Protein conformation ; Inclusion bodies ; Amyloids ; E. coli
Publicado en: Microbial cell factories, Vol. 14 (2015) , art. 174, ISSN 1475-2859

DOI: 10.1186/s12934-015-0361-y
PMID: 26536866


16 p, 3.8 MB

El registro aparece en las colecciones:
Documentos de investigación > Documentos de los grupos de investigación de la UAB > Centros y grupos de investigación (producción científica) > Ciencias de la salud y biociencias > Instituto de Biotecnología y de Biomedicina (IBB)
Artículos > Artículos de investigación
Artículos > Artículos publicados

 Registro creado el 2020-06-22, última modificación el 2020-08-02



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