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Title

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.
KeywordsBacteria;
Dot/Western-blot
Immuno-electron microscopy
Intracellular amyloid
Microfluidics
Prionoid/Prion-like
SDD-AGE
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
URIhttp://hdl.handle.net/10261/166518
ISSN1064-3745
E-ISSN1940-6029
Appears in Collections:(CIB) Artículos
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