Alternate thermoregulation and functional binding of Escherichia coli type 1 fimbriae in environmental and animal isolates

Abstract Type 1 fimbriae (T1F) are well characterised cell surface organelles expressed by Escherichia coli and required for adherence to mannosylated host tissue. They satisfy molecular Koch's postulates as a virulence determinant and a host-adapted role has been reinforced by reports that T1F...

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Veröffentlicht in:FEMS microbiology letters 2016-11, Vol.363 (22), p.fnw251
Hauptverfasser: Marshall, Jacqueline, Rossez, Yannick, Mainda, Geoffrey, Gally, David L., Daniell, Tim J., Holden, Nicola J.
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container_issue 22
container_start_page fnw251
container_title FEMS microbiology letters
container_volume 363
creator Marshall, Jacqueline
Rossez, Yannick
Mainda, Geoffrey
Gally, David L.
Daniell, Tim J.
Holden, Nicola J.
description Abstract Type 1 fimbriae (T1F) are well characterised cell surface organelles expressed by Escherichia coli and required for adherence to mannosylated host tissue. They satisfy molecular Koch's postulates as a virulence determinant and a host-adapted role has been reinforced by reports that T1F expression is repressed at submammalian temperatures. Analysis of a group of 136 environmental and animal E. coli isolates that express T1F at 37°C showed that 28% are also capable of expression at 20°C, in a phase variable manner. The heterogeneous proportions varied widely, and although growth temperature impacted the total proportion expressing T1F, there was no direct correlation between growth at 37°C and 20°C, indicative of differences in thermoregulation of the genetic switch (fimS) that controls phase variation. Specificities of the adhesin (FimH) also varied between the isolates: most bound to α-(1-3) mannan and yeast extracts as expected, but some recognised β-(1-4)-mannans and N-linked glycoproteins from plants, and T1F from two of the isolates mediated binding to plant roots. The results expand our view of a well-described adherence factor to show alternative expression profiles and adhesin specificities, which in turn may confer an advantage for certain isolates in alternative hosts and habitats. Our work challenges the dogma that a well-characterised adherence factor is only expressed at mammalian-relevant temperatures and provides evidence for alternative functional targets for binding.
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They satisfy molecular Koch's postulates as a virulence determinant and a host-adapted role has been reinforced by reports that T1F expression is repressed at submammalian temperatures. Analysis of a group of 136 environmental and animal E. coli isolates that express T1F at 37°C showed that 28% are also capable of expression at 20°C, in a phase variable manner. The heterogeneous proportions varied widely, and although growth temperature impacted the total proportion expressing T1F, there was no direct correlation between growth at 37°C and 20°C, indicative of differences in thermoregulation of the genetic switch (fimS) that controls phase variation. Specificities of the adhesin (FimH) also varied between the isolates: most bound to α-(1-3) mannan and yeast extracts as expected, but some recognised β-(1-4)-mannans and N-linked glycoproteins from plants, and T1F from two of the isolates mediated binding to plant roots. The results expand our view of a well-described adherence factor to show alternative expression profiles and adhesin specificities, which in turn may confer an advantage for certain isolates in alternative hosts and habitats. Our work challenges the dogma that a well-characterised adherence factor is only expressed at mammalian-relevant temperatures and provides evidence for alternative functional targets for binding.</description><identifier>ISSN: 1574-6968</identifier><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1093/femsle/fnw251</identifier><identifier>PMID: 27810882</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Adhesins, Escherichia coli - genetics ; Adhesins, Escherichia coli - metabolism ; Adhesion ; Bacteria ; Bacterial Adhesion - physiology ; Binding ; Cell Extracts - chemistry ; Cell surface ; E coli ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - isolation &amp; purification ; Escherichia coli - metabolism ; Fimbriae Proteins - metabolism ; Fimbriae, Bacterial - metabolism ; Glycoproteins ; Glycoproteins - metabolism ; Mannan ; Mannans - metabolism ; Mannose - metabolism ; Microbiology ; Organelles ; Phase variations ; Pili ; Plant roots ; Plant Roots - metabolism ; Plant Roots - microbiology ; Protein Binding ; Temperature ; Thermoregulation ; Virulence ; Yeast ; Yeasts</subject><ispartof>FEMS microbiology letters, 2016-11, Vol.363 (22), p.fnw251</ispartof><rights>FEMS 2016. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com 2016</rights><rights>FEMS 2016. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.</rights><rights>Copyright Oxford University Press, UK Nov 2016</rights><rights>FEMS 2016. All rights reserved. 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identifier ISSN: 1574-6968
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subjects Adhesins, Escherichia coli - genetics
Adhesins, Escherichia coli - metabolism
Adhesion
Bacteria
Bacterial Adhesion - physiology
Binding
Cell Extracts - chemistry
Cell surface
E coli
Escherichia coli
Escherichia coli - genetics
Escherichia coli - isolation & purification
Escherichia coli - metabolism
Fimbriae Proteins - metabolism
Fimbriae, Bacterial - metabolism
Glycoproteins
Glycoproteins - metabolism
Mannan
Mannans - metabolism
Mannose - metabolism
Microbiology
Organelles
Phase variations
Pili
Plant roots
Plant Roots - metabolism
Plant Roots - microbiology
Protein Binding
Temperature
Thermoregulation
Virulence
Yeast
Yeasts
title Alternate thermoregulation and functional binding of Escherichia coli type 1 fimbriae in environmental and animal isolates
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