Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.

Escherichia coli and a few other members of the Enterobacteriales can produce functional amyloids known as curli. These extracellular fibrils are involved in biofilm formation and studies have shown that they may act as virulence factors during infections. It is not known whether curli fibrils are r...

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Autores principales:	Morten S Dueholm, Mads Albertsen, Daniel Otzen, Per Halkjær Nielsen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e81b0066346f4b48953d4c204ace2931
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spelling	oai:doaj.org-article:e81b0066346f4b48953d4c204ace29312021-11-18T08:05:23ZCurli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.1932-620310.1371/journal.pone.0051274https://doaj.org/article/e81b0066346f4b48953d4c204ace29312012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23251478/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Escherichia coli and a few other members of the Enterobacteriales can produce functional amyloids known as curli. These extracellular fibrils are involved in biofilm formation and studies have shown that they may act as virulence factors during infections. It is not known whether curli fibrils are restricted to the Enterobacteriales or if they are phylogenetically widespread. The growing number of genome-sequenced bacteria spanning many phylogenetic groups allows a reliable bioinformatic investigation of the phylogenetic diversity of the curli system. Here we show that the curli system is phylogenetically much more widespread than initially assumed, spanning at least four phyla. Curli fibrils may consequently be encountered frequently in environmental as well as pathogenic biofilms, which was supported by identification of curli genes in public metagenomes from a diverse range of habitats. Identification and comparison of curli subunit (CsgA/B) homologs show that these proteins allow a high degree of freedom in their primary protein structure, although a modular structure of tightly spaced repeat regions containing conserved glutamine, asparagine and glycine residues has to be preserved. In addition, a high degree of variability within the operon structure of curli subunits between bacterial taxa suggests that the curli fibrils might have evolved to fulfill specific functions. Variations in the genetic organization of curli genes are also seen among different bacterial genera. This suggests that some genera may utilize alternative regulatory pathways for curli expression. Comparison of phylogenetic trees of Csg proteins and the 16S rRNA genes of the corresponding bacteria showed remarkably similar overall topography, suggesting that horizontal gene transfer is a minor player in the spreading of the curli system.Morten S DueholmMads AlbertsenDaniel OtzenPer Halkjær NielsenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 12, p e51274 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Morten S Dueholm Mads Albertsen Daniel Otzen Per Halkjær Nielsen Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.
description	Escherichia coli and a few other members of the Enterobacteriales can produce functional amyloids known as curli. These extracellular fibrils are involved in biofilm formation and studies have shown that they may act as virulence factors during infections. It is not known whether curli fibrils are restricted to the Enterobacteriales or if they are phylogenetically widespread. The growing number of genome-sequenced bacteria spanning many phylogenetic groups allows a reliable bioinformatic investigation of the phylogenetic diversity of the curli system. Here we show that the curli system is phylogenetically much more widespread than initially assumed, spanning at least four phyla. Curli fibrils may consequently be encountered frequently in environmental as well as pathogenic biofilms, which was supported by identification of curli genes in public metagenomes from a diverse range of habitats. Identification and comparison of curli subunit (CsgA/B) homologs show that these proteins allow a high degree of freedom in their primary protein structure, although a modular structure of tightly spaced repeat regions containing conserved glutamine, asparagine and glycine residues has to be preserved. In addition, a high degree of variability within the operon structure of curli subunits between bacterial taxa suggests that the curli fibrils might have evolved to fulfill specific functions. Variations in the genetic organization of curli genes are also seen among different bacterial genera. This suggests that some genera may utilize alternative regulatory pathways for curli expression. Comparison of phylogenetic trees of Csg proteins and the 16S rRNA genes of the corresponding bacteria showed remarkably similar overall topography, suggesting that horizontal gene transfer is a minor player in the spreading of the curli system.
format	article
author	Morten S Dueholm Mads Albertsen Daniel Otzen Per Halkjær Nielsen
author_facet	Morten S Dueholm Mads Albertsen Daniel Otzen Per Halkjær Nielsen
author_sort	Morten S Dueholm
title	Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.
title_short	Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.
title_full	Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.
title_fullStr	Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.
title_full_unstemmed	Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.
title_sort	curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/e81b0066346f4b48953d4c204ace2931
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Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure.

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