Flagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein

ABSTRACT Helicobacter pylori contains four genes that are predicted to encode proteins secreted by the autotransporter (type V) pathway. One of these, the pore-forming toxin VacA, has been studied in great detail, but thus far there has been very little investigation of three VacA-like proteins. We...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Jana N. Radin, Jennifer A. Gaddy, Christian González-Rivera, John T. Loh, Holly M. Scott Algood, Timothy L. Cover
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2013
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/c7f90886bfff46c68cfcad99ce886041
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:c7f90886bfff46c68cfcad99ce886041
record_format	dspace
spelling	oai:doaj.org-article:c7f90886bfff46c68cfcad99ce8860412021-11-15T15:40:28ZFlagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein10.1128/mBio.00613-122150-7511https://doaj.org/article/c7f90886bfff46c68cfcad99ce8860412013-05-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00613-12https://doaj.org/toc/2150-7511ABSTRACT Helicobacter pylori contains four genes that are predicted to encode proteins secreted by the autotransporter (type V) pathway. One of these, the pore-forming toxin VacA, has been studied in great detail, but thus far there has been very little investigation of three VacA-like proteins. We show here that all three VacA-like proteins are >250 kDa in mass and localized on the surface of H. pylori. The expression of the three vacA-like genes is upregulated during H. pylori colonization of the mouse stomach compared to H. pylori growth in vitro, and a wild-type H. pylori strain outcompeted each of the three corresponding isogenic mutant strains in its ability to colonize the mouse stomach. One of the VacA-like proteins localizes to a sheath that overlies the flagellar filament and bulb, and therefore, we designate it FaaA (flagella-associated autotransporter A). In comparison to a wild-type H. pylori strain, an isogenic faaA mutant strain exhibits decreased motility, decreased flagellar stability, and an increased proportion of flagella in a nonpolar site. The flagellar localization of FaaA differs markedly from the localization of other known autotransporters, and the current results reveal an important role of FaaA in flagellar localization and motility. IMPORTANCE The pathogenesis of most bacterial infections is dependent on the actions of secreted proteins, and proteins secreted by the autotransporter pathway constitute the largest family of secreted proteins in pathogenic Gram-negative bacteria. In this study, we analyzed three autotransporter proteins (VacA-like proteins) produced by Helicobacter pylori, a Gram-negative bacterium that colonizes the human stomach and contributes to the pathogenesis of gastric cancer and peptic ulcer disease. We demonstrate that these three proteins each enhance the capacity of H. pylori to colonize the stomach. Unexpectedly, one of these proteins (FaaA) is localized to a sheath that overlies H. pylori flagella. The absence of FaaA results in decreased H. pylori motility as well as a reduction in flagellar stability and a change in flagellar localization. The atypical localization of FaaA reflects a specialized function of this autotransporter designed to optimize H. pylori colonization of the gastric niche.Jana N. RadinJennifer A. GaddyChristian González-RiveraJohn T. LohHolly M. Scott AlgoodTimothy L. CoverAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 4, Iss 2 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Jana N. Radin Jennifer A. Gaddy Christian González-Rivera John T. Loh Holly M. Scott Algood Timothy L. Cover Flagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein
description	ABSTRACT Helicobacter pylori contains four genes that are predicted to encode proteins secreted by the autotransporter (type V) pathway. One of these, the pore-forming toxin VacA, has been studied in great detail, but thus far there has been very little investigation of three VacA-like proteins. We show here that all three VacA-like proteins are >250 kDa in mass and localized on the surface of H. pylori. The expression of the three vacA-like genes is upregulated during H. pylori colonization of the mouse stomach compared to H. pylori growth in vitro, and a wild-type H. pylori strain outcompeted each of the three corresponding isogenic mutant strains in its ability to colonize the mouse stomach. One of the VacA-like proteins localizes to a sheath that overlies the flagellar filament and bulb, and therefore, we designate it FaaA (flagella-associated autotransporter A). In comparison to a wild-type H. pylori strain, an isogenic faaA mutant strain exhibits decreased motility, decreased flagellar stability, and an increased proportion of flagella in a nonpolar site. The flagellar localization of FaaA differs markedly from the localization of other known autotransporters, and the current results reveal an important role of FaaA in flagellar localization and motility. IMPORTANCE The pathogenesis of most bacterial infections is dependent on the actions of secreted proteins, and proteins secreted by the autotransporter pathway constitute the largest family of secreted proteins in pathogenic Gram-negative bacteria. In this study, we analyzed three autotransporter proteins (VacA-like proteins) produced by Helicobacter pylori, a Gram-negative bacterium that colonizes the human stomach and contributes to the pathogenesis of gastric cancer and peptic ulcer disease. We demonstrate that these three proteins each enhance the capacity of H. pylori to colonize the stomach. Unexpectedly, one of these proteins (FaaA) is localized to a sheath that overlies H. pylori flagella. The absence of FaaA results in decreased H. pylori motility as well as a reduction in flagellar stability and a change in flagellar localization. The atypical localization of FaaA reflects a specialized function of this autotransporter designed to optimize H. pylori colonization of the gastric niche.
format	article
author	Jana N. Radin Jennifer A. Gaddy Christian González-Rivera John T. Loh Holly M. Scott Algood Timothy L. Cover
author_facet	Jana N. Radin Jennifer A. Gaddy Christian González-Rivera John T. Loh Holly M. Scott Algood Timothy L. Cover
author_sort	Jana N. Radin
title	Flagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein
title_short	Flagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein
title_full	Flagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein
title_fullStr	Flagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein
title_full_unstemmed	Flagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein
title_sort	flagellar localization of a <named-content content-type="genus-species">helicobacter pylori</named-content> autotransporter protein
publisher	American Society for Microbiology
publishDate	2013
url	https://doaj.org/article/c7f90886bfff46c68cfcad99ce886041
work_keys_str_mv	AT jananradin flagellarlocalizationofanamedcontentcontenttypegenusspecieshelicobacterpylorinamedcontentautotransporterprotein AT jenniferagaddy flagellarlocalizationofanamedcontentcontenttypegenusspecieshelicobacterpylorinamedcontentautotransporterprotein AT christiangonzalezrivera flagellarlocalizationofanamedcontentcontenttypegenusspecieshelicobacterpylorinamedcontentautotransporterprotein AT johntloh flagellarlocalizationofanamedcontentcontenttypegenusspecieshelicobacterpylorinamedcontentautotransporterprotein AT hollymscottalgood flagellarlocalizationofanamedcontentcontenttypegenusspecieshelicobacterpylorinamedcontentautotransporterprotein AT timothylcover flagellarlocalizationofanamedcontentcontenttypegenusspecieshelicobacterpylorinamedcontentautotransporterprotein
_version_	1718427728737206272

Flagellar Localization of a <named-content content-type="genus-species">Helicobacter pylori</named-content> Autotransporter Protein

Ejemplares similares