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Discovery of fibrillar adhesins across bacterial species
BACKGROUND: Fibrillar adhesins are long multidomain proteins that form filamentous structures at the cell surface of bacteria. They are an important yet understudied class of proteins composed of adhesive and stalk domains that mediate interactions of bacteria with their environment. This study aims...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8286594/ https://www.ncbi.nlm.nih.gov/pubmed/34275445 http://dx.doi.org/10.1186/s12864-021-07586-2 |
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author | Monzon, Vivian Lafita, Aleix Bateman, Alex |
author_facet | Monzon, Vivian Lafita, Aleix Bateman, Alex |
author_sort | Monzon, Vivian |
collection | PubMed |
description | BACKGROUND: Fibrillar adhesins are long multidomain proteins that form filamentous structures at the cell surface of bacteria. They are an important yet understudied class of proteins composed of adhesive and stalk domains that mediate interactions of bacteria with their environment. This study aims to characterize fibrillar adhesins in a wide range of bacterial phyla and to identify new fibrillar adhesin-like proteins to improve our understanding of host-bacteria interactions. RESULTS: Through careful literature and computational searches, we identified 82 stalk and 27 adhesive domain families in fibrillar adhesins. Based on the presence of these domains in the UniProt Reference Proteomes database, we identified and analysed 3,542 fibrillar adhesin-like proteins across species of the most common bacterial phyla. We further enumerate the adhesive and stalk domain combinations found in nature and demonstrate that fibrillar adhesins have complex and variable domain architectures, which differ across species. By analysing the domain architecture of fibrillar adhesins, we show that in Gram positive bacteria, adhesive domains are mostly positioned at the N-terminus and cell surface anchors at the C-terminus of the protein, while their positions are more variable in Gram negative bacteria. We provide an open repository of fibrillar adhesin-like proteins and domains to enable further studies of this class of bacterial surface proteins. CONCLUSION: This study provides a domain-based characterization of fibrillar adhesins and demonstrates that they are widely found in species across the main bacterial phyla. We have discovered numerous novel fibrillar adhesins and improved our understanding of pathogenic adhesion and invasion mechanisms. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at (10.1186/s12864-021-07586-2). |
format | Online Article Text |
id | pubmed-8286594 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-82865942021-07-19 Discovery of fibrillar adhesins across bacterial species Monzon, Vivian Lafita, Aleix Bateman, Alex BMC Genomics Research Article BACKGROUND: Fibrillar adhesins are long multidomain proteins that form filamentous structures at the cell surface of bacteria. They are an important yet understudied class of proteins composed of adhesive and stalk domains that mediate interactions of bacteria with their environment. This study aims to characterize fibrillar adhesins in a wide range of bacterial phyla and to identify new fibrillar adhesin-like proteins to improve our understanding of host-bacteria interactions. RESULTS: Through careful literature and computational searches, we identified 82 stalk and 27 adhesive domain families in fibrillar adhesins. Based on the presence of these domains in the UniProt Reference Proteomes database, we identified and analysed 3,542 fibrillar adhesin-like proteins across species of the most common bacterial phyla. We further enumerate the adhesive and stalk domain combinations found in nature and demonstrate that fibrillar adhesins have complex and variable domain architectures, which differ across species. By analysing the domain architecture of fibrillar adhesins, we show that in Gram positive bacteria, adhesive domains are mostly positioned at the N-terminus and cell surface anchors at the C-terminus of the protein, while their positions are more variable in Gram negative bacteria. We provide an open repository of fibrillar adhesin-like proteins and domains to enable further studies of this class of bacterial surface proteins. CONCLUSION: This study provides a domain-based characterization of fibrillar adhesins and demonstrates that they are widely found in species across the main bacterial phyla. We have discovered numerous novel fibrillar adhesins and improved our understanding of pathogenic adhesion and invasion mechanisms. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at (10.1186/s12864-021-07586-2). BioMed Central 2021-07-18 /pmc/articles/PMC8286594/ /pubmed/34275445 http://dx.doi.org/10.1186/s12864-021-07586-2 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Article Monzon, Vivian Lafita, Aleix Bateman, Alex Discovery of fibrillar adhesins across bacterial species |
title | Discovery of fibrillar adhesins across bacterial species |
title_full | Discovery of fibrillar adhesins across bacterial species |
title_fullStr | Discovery of fibrillar adhesins across bacterial species |
title_full_unstemmed | Discovery of fibrillar adhesins across bacterial species |
title_short | Discovery of fibrillar adhesins across bacterial species |
title_sort | discovery of fibrillar adhesins across bacterial species |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8286594/ https://www.ncbi.nlm.nih.gov/pubmed/34275445 http://dx.doi.org/10.1186/s12864-021-07586-2 |
work_keys_str_mv | AT monzonvivian discoveryoffibrillaradhesinsacrossbacterialspecies AT lafitaaleix discoveryoffibrillaradhesinsacrossbacterialspecies AT batemanalex discoveryoffibrillaradhesinsacrossbacterialspecies |