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

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The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers. / Taglialegna, Agustina; Matilla-Cuenca, Leticia; Dorado-Morales, Pedro; Navarro, Susanna; Ventura, Salvador; Garnett, James A.; Lasa, Iñigo; Valle, Jaione.

In: npj Biofilms and Microbiomes, Vol. 6, No. 1, 15, 01.12.2020.

Research output: Contribution to journalArticlepeer-review

Harvard

Taglialegna, A, Matilla-Cuenca, L, Dorado-Morales, P, Navarro, S, Ventura, S, Garnett, JA, Lasa, I & Valle, J 2020, 'The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers', npj Biofilms and Microbiomes, vol. 6, no. 1, 15. https://doi.org/10.1038/s41522-020-0125-2

APA

Taglialegna, A., Matilla-Cuenca, L., Dorado-Morales, P., Navarro, S., Ventura, S., Garnett, J. A., Lasa, I., & Valle, J. (2020). The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers. npj Biofilms and Microbiomes, 6(1), [15]. https://doi.org/10.1038/s41522-020-0125-2

Vancouver

Taglialegna A, Matilla-Cuenca L, Dorado-Morales P, Navarro S, Ventura S, Garnett JA et al. The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers. npj Biofilms and Microbiomes. 2020 Dec 1;6(1). 15. https://doi.org/10.1038/s41522-020-0125-2

Author

Taglialegna, Agustina ; Matilla-Cuenca, Leticia ; Dorado-Morales, Pedro ; Navarro, Susanna ; Ventura, Salvador ; Garnett, James A. ; Lasa, Iñigo ; Valle, Jaione. / The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers. In: npj Biofilms and Microbiomes. 2020 ; Vol. 6, No. 1.

Bibtex Download

@article{c71d720a701b4fbfa23d1525be5331f4,
title = "The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers",
abstract = "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.",
author = "Agustina Taglialegna and Leticia Matilla-Cuenca and Pedro Dorado-Morales and Susanna Navarro and Salvador Ventura and Garnett, {James A.} and I{\~n}igo Lasa and Jaione Valle",
year = "2020",
month = dec,
day = "1",
doi = "10.1038/s41522-020-0125-2",
language = "English",
volume = "6",
journal = "npj Biofilms and Microbiomes",
issn = "2055-5008",
publisher = "Nature Publishing Group",
number = "1",

}

RIS (suitable for import to EndNote) Download

TY - JOUR

T1 - The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers

AU - Taglialegna, Agustina

AU - Matilla-Cuenca, Leticia

AU - Dorado-Morales, Pedro

AU - Navarro, Susanna

AU - Ventura, Salvador

AU - Garnett, James A.

AU - Lasa, Iñigo

AU - Valle, Jaione

PY - 2020/12/1

Y1 - 2020/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85082532349&partnerID=8YFLogxK

U2 - 10.1038/s41522-020-0125-2

DO - 10.1038/s41522-020-0125-2

M3 - Article

C2 - 32221298

AN - SCOPUS:85082532349

VL - 6

JO - npj Biofilms and Microbiomes

JF - npj Biofilms and Microbiomes

SN - 2055-5008

IS - 1

M1 - 15

ER -

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