The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers
Taglialegna, Agustina (Instituto de Agrobiotecnología)
Matilla-Cuenca, Leticia (Instituto de Agrobiotecnología)
Dorado-Morales, Pedro (Universidad Pública de Navarra. Departamento de Ciencias de la Salud)
Navarro, Susanna (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Garnett, James A. (King's College London)
Lasa, Iñigo (Universidad Pública de Navarra. Departamento de Ciencias de la Salud)
Valle, Jaione (Instituto de Agrobiotecnología)

Data:	2020
Resum:	Functional amyloids are considered as common building block structures of the biofilm matrix in different bacteria. In previous work, we have shown that the staphylococcal surface protein Bap, a member of the Biofilm-Associated Proteins (BAP) family, is processed and the fragments containing the N-terminal region become aggregation-prone and self-assemble into amyloid-like structures. Here, we report that Esp, a Bap-orthologous protein produced by Enterococcus faecalis, displays a similar amyloidogenic behavior. We demonstrate that at acidic pH the N-terminal region of Esp forms aggregates with an amyloid-like conformation, as evidenced by biophysical analysis and the binding of protein aggregates to amyloid-indicative dyes. Expression of a chimeric protein, with its Esp N-terminal domain anchored to the cell wall through the R domain of clumping factor A, showed that the Esp N-terminal region is sufficient to confer multicellular behavior through the formation of an extracellular amyloid-like material. These results suggest that the mechanism of amyloid-like aggregation to build the biofilm matrix might be widespread among BAP-like proteins. This amyloid-based mechanism may not only have strong relevance for bacteria lifestyle but could also contribute to the amyloid burden to which the human physiology is potentially exposed.
Ajuts:	Agencia Estatal de Investigación BIO2017-83035-R
Drets:	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.
Llengua:	Anglès
Document:	Article ; recerca ; Versió publicada
Publicat a:	npj biofilms and microbiomes, Vol. 6, issue 1 (2020) , art. 15, ISSN 2055-5008

DOI: 10.1038/s41522-020-0125-2
PMID: 32221298

12 p, 5.4 MB

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