English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/166518
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Addressing intracellular Amyloidosis in bacteria with RepA-WH1, a prion-like protein

AuthorsMolina-García, Laura ; Gasset-Rosa, F. ; Moreno-del Álamo, María ; Moreno Díaz de la Espina, Susana ; Giraldo, R.
Immuno-electron microscopy
Intracellular amyloid
Templated fibrillation
Time-lapse microscopy
Issue Date2018
PublisherHumana Press
CitationMethods Mol Biol 1779:289-312 (2018)
AbstractBacteria are the simplest cellular model in which amyloidosis has been addressed. It is well documented that bacterial consortia (biofilms) assemble their extracellular matrix on an amyloid scaffold, yet very few intracellular amyloids are known in bacteria. Here, we describe the methods we have resorted to characterize in Escherichia coli cells the amyloidogenesis, propagation, and dynamics of the RepA-WH1 prionoid. This prion-like protein, a manifold domain from the plasmid replication protein RepA, itself capable of assembling a functional amyloid, causes when expressed in E. coli a synthetic amyloid proteinopathy, the first model for an amyloid disease with a purely bacterial origin. These protocols are useful to study other intracellular amyloids in bacteria.
Description25 p.-1 fig. This is a pre-print of an article published in Methods in Molecular Biology. The final authenticated version is available online at: https://doi.org/10.1007/978-1-4939-7816-8_18
Publisher version (URL)https://doi.org/10.1007/978-1-4939-7816-8_18
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
MethodsMolBiol_RGiraldo_preprint_2018.pdfPreprint2,38 MBAdobe PDFThumbnail
Show full item record
Review this work

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.