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The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers

AuthorsTaglialegna, Agustina ; Matilla-Cuenca, Leticia; Dorado-Morales, Pedro; Navarro, Susanna; Ventura, Salvador; Garnett, James A.; Lasa, Íñigo ; Valle Turrillas, Jaione
Issue Date2020
PublisherNature Publishing Group
Citationnpj Biofilms and Microbiomes 6: 15 (2020)
AbstractFunctional 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.
Publisher version (URL)http://dx.doi.org/10.1038/s41522-020-0125-2
Identifiersdoi: 10.1038/s41522-020-0125-2
e-issn: 2055-5008
Appears in Collections:(IDAB) Artículos
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