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Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO

Bacteria secrete flagella subunits and deliver virulence effectors via type III export systems. During flagellar filament assembly, a chaperone escort mechanism has been proposed to enhance the export of early, minor flagellar filament components by selectively binding and cycling their chaperones....

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Detalles Bibliográficos
Autores principales: Evans, Lewis DB, Hughes, Colin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3500872/
https://www.ncbi.nlm.nih.gov/pubmed/19260965
http://dx.doi.org/10.1111/j.1574-6968.2009.01535.x
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author Evans, Lewis DB
Hughes, Colin
author_facet Evans, Lewis DB
Hughes, Colin
author_sort Evans, Lewis DB
collection PubMed
description Bacteria secrete flagella subunits and deliver virulence effectors via type III export systems. During flagellar filament assembly, a chaperone escort mechanism has been proposed to enhance the export of early, minor flagellar filament components by selectively binding and cycling their chaperones. Here we identify virulence orthologues of the flagellar chaperone escort FliJ and show that the orthologues Salmonella InvI and Yersinia YscO are, like FliJ, essential for their type III export pathway and similarly, do not bind export substrates. Like FliJ, they recognize a subset of export chaperones, in particular those of the host membrane translocon components required for subsequent effector delivery.
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spelling pubmed-35008722012-11-26 Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO Evans, Lewis DB Hughes, Colin FEMS Microbiol Lett Research Letters Bacteria secrete flagella subunits and deliver virulence effectors via type III export systems. During flagellar filament assembly, a chaperone escort mechanism has been proposed to enhance the export of early, minor flagellar filament components by selectively binding and cycling their chaperones. Here we identify virulence orthologues of the flagellar chaperone escort FliJ and show that the orthologues Salmonella InvI and Yersinia YscO are, like FliJ, essential for their type III export pathway and similarly, do not bind export substrates. Like FliJ, they recognize a subset of export chaperones, in particular those of the host membrane translocon components required for subsequent effector delivery. Blackwell Publishing Ltd 2009-04 2009-03-02 /pmc/articles/PMC3500872/ /pubmed/19260965 http://dx.doi.org/10.1111/j.1574-6968.2009.01535.x Text en © 2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
spellingShingle Research Letters
Evans, Lewis DB
Hughes, Colin
Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
title Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
title_full Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
title_fullStr Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
title_full_unstemmed Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
title_short Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
title_sort selective binding of virulence type iii export chaperones by flij escort orthologues invi and ysco
topic Research Letters
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3500872/
https://www.ncbi.nlm.nih.gov/pubmed/19260965
http://dx.doi.org/10.1111/j.1574-6968.2009.01535.x
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