Taglialegna, Agustina
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Taglialegna
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Agustina
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Producción Agraria
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Publication Open Access The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers(Nature Research, 2020) Taglialegna, Agustina; Matilla Cuenca, Leticia; Dorado Morales, Pedro; Navarro, Susanna; Ventura, Salvador; Garnett, James A.; Lasa Uzcudun, Íñigo; Valle Turrillas, Jaione; Ciencias de la Salud; Osasun ZientziakFunctional 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.Publication Open Access Staphylococcal Bap proteins build amyloid scaffold biofilm matrices in response to environmental signals(Public Library of Science, 2016) Taglialegna, Agustina; Navarro, Susanna; Ventura, Salvador; Garnett, James A.; Matthews, Steve; Penadés, José R.; Lasa Uzcudun, Íñigo; Valle Turrillas, Jaione; IdAB. Instituto de Agrobiotecnología / Agrobioteknologiako InstitutuaMajor components of the biofilm matrix scaffold are proteins that assemble to create a unified structure that maintain bacteria attached to each other and to surfaces. We provide evidence that a surface protein present in several staphylococcal species forms functional amyloid aggregates to build the biofilm matrix in response to specific environmental conditions. Under low Ca2+ concentrations and acidic pH, Bap is processed and forms insoluble aggregates with amyloidogenic properties. When the Ca2+ concentration increases, metal-coordinated Bap adopts a structurally more stable conformation and as a consequence, the N-terminal region is unable to assemble into amyloid aggregates. The control of Bap cleavage and assembly helps to regulate biofilm matrix development as a function of environmental changes.