Biofilm-associated proteins: from the gut biofilms to neurodegeneration

Human microbiota form a biofilm with substantial consequences for health and disease. Numerous studies have indicated that microbial communities produce functional amyloids as part of their biofilm extracellular scaffolds. The overlooked interplay between bacterial amyloids and the host may have det...

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Detalles Bibliográficos
Autor: Valle Turrillas, Jaione
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/396268
Acceso en línea:http://hdl.handle.net/10261/396268
https://api.elsevier.com/content/abstract/scopus_id/85217003913
Access Level:acceso abierto
Palabra clave:Amyloid
Biofilm
Biofilm-associated protein
Gut microbiota
α-synuclein
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spelling Biofilm-associated proteins: from the gut biofilms to neurodegenerationValle Turrillas, JaioneAmyloidBiofilmBiofilm-associated proteinGut microbiotaα-synucleinHuman microbiota form a biofilm with substantial consequences for health and disease. Numerous studies have indicated that microbial communities produce functional amyloids as part of their biofilm extracellular scaffolds. The overlooked interplay between bacterial amyloids and the host may have detrimental consequences for the host, including neurodegeneration. This work gives an overview of the biofilm-associated amyloids expressed by the gut microbiota and their potential role in neurodegeneration. It discusses the biofilm-associated proteins (BAPs) of the gut microbiota, maps the amyloidogenic domains of these proteins, and analyzes the presence of bap genes within accessory genomes linked with transposable elements. Furthermore, the evidence supporting the existence of amyloids in the gut are presented. Finally, it explores the potential interactions between BAPs and α-synuclein, extending the literature on amyloid cross-kingdom interactions. Based on these findings, this study propose that BAP amyloids act as transmissible catalysts, facilitating the misfolding, accumulation, and spread of α-synuclein aggregates. This review contributes to the understanding of complex interactions among the microbiota, transmissible elements, and host, which is crucial for developing novel therapeutic approaches to combat microbiota-related diseases and improve overall health outcomes.The work was supported by the Ministerio de Ciencia e Innovación. [PID2021-124248OB-I00]Peer reviewedTaylor & FrancisAgencia Estatal de Investigación (España)Ministerio de Ciencia e Innovación (España)Valle Turrillas, Jaione [0000-0003-3115-0207]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/396268https://api.elsevier.com/content/abstract/scopus_id/85217003913reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-124248OB-I00The underlying dataset has been published as supplementary material of the article in the publisher platform at https://doi.org/10.1080/19490976.2025.2461721© 2025 CSIC. Published with license by Taylor & Francis Group, LLC.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use,distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the AcceptedManuscript in a repository by the author(s) or with their consent.https://doi.org/10.1080/19490976.2025.2461721Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3962682026-05-22T06:33:51Z
dc.title.none.fl_str_mv Biofilm-associated proteins: from the gut biofilms to neurodegeneration
title Biofilm-associated proteins: from the gut biofilms to neurodegeneration
spellingShingle Biofilm-associated proteins: from the gut biofilms to neurodegeneration
Valle Turrillas, Jaione
Amyloid
Biofilm
Biofilm-associated protein
Gut microbiota
α-synuclein
title_short Biofilm-associated proteins: from the gut biofilms to neurodegeneration
title_full Biofilm-associated proteins: from the gut biofilms to neurodegeneration
title_fullStr Biofilm-associated proteins: from the gut biofilms to neurodegeneration
title_full_unstemmed Biofilm-associated proteins: from the gut biofilms to neurodegeneration
title_sort Biofilm-associated proteins: from the gut biofilms to neurodegeneration
dc.creator.none.fl_str_mv Valle Turrillas, Jaione
author Valle Turrillas, Jaione
author_facet Valle Turrillas, Jaione
author_role author
dc.contributor.none.fl_str_mv Agencia Estatal de Investigación (España)
Ministerio de Ciencia e Innovación (España)
Valle Turrillas, Jaione [0000-0003-3115-0207]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Amyloid
Biofilm
Biofilm-associated protein
Gut microbiota
α-synuclein
topic Amyloid
Biofilm
Biofilm-associated protein
Gut microbiota
α-synuclein
description Human microbiota form a biofilm with substantial consequences for health and disease. Numerous studies have indicated that microbial communities produce functional amyloids as part of their biofilm extracellular scaffolds. The overlooked interplay between bacterial amyloids and the host may have detrimental consequences for the host, including neurodegeneration. This work gives an overview of the biofilm-associated amyloids expressed by the gut microbiota and their potential role in neurodegeneration. It discusses the biofilm-associated proteins (BAPs) of the gut microbiota, maps the amyloidogenic domains of these proteins, and analyzes the presence of bap genes within accessory genomes linked with transposable elements. Furthermore, the evidence supporting the existence of amyloids in the gut are presented. Finally, it explores the potential interactions between BAPs and α-synuclein, extending the literature on amyloid cross-kingdom interactions. Based on these findings, this study propose that BAP amyloids act as transmissible catalysts, facilitating the misfolding, accumulation, and spread of α-synuclein aggregates. This review contributes to the understanding of complex interactions among the microbiota, transmissible elements, and host, which is crucial for developing novel therapeutic approaches to combat microbiota-related diseases and improve overall health outcomes.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/396268
https://api.elsevier.com/content/abstract/scopus_id/85217003913
url http://hdl.handle.net/10261/396268
https://api.elsevier.com/content/abstract/scopus_id/85217003913
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-124248OB-I00
The underlying dataset has been published as supplementary material of the article in the publisher platform at https://doi.org/10.1080/19490976.2025.2461721© 2025 CSIC. Published with license by Taylor & Francis Group, LLC.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use,distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the AcceptedManuscript in a repository by the author(s) or with their consent.
https://doi.org/10.1080/19490976.2025.2461721
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
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