Molecular Characterization of the EhaG and UpaG Trimeric Autotransporter Proteins from Pathogenic Escherichia coli
Identifieur interne : 001E48 ( Pmc/Checkpoint ); précédent : 001E47; suivant : 001E49Molecular Characterization of the EhaG and UpaG Trimeric Autotransporter Proteins from Pathogenic Escherichia coli
Auteurs : Makrina Totsika [Australie] ; Timothy J. Wells [Australie] ; Christophe Beloin [France] ; Jaione Valle [France] ; Luke P. Allsopp [Australie] ; Nathan P. King [Australie] ; Jean-Marc Ghigo [France] ; Mark A. Schembri [Australie]Source :
- Applied and Environmental Microbiology [ 0099-2240 ] ; 2012.
Abstract
Trimeric autotransporter proteins (TAAs) are important virulence factors of many Gram-negative bacterial pathogens. A common feature of most TAAs is the ability to mediate adherence to eukaryotic cells or extracellular matrix (ECM) proteins via a cell surface-exposed passenger domain. Here we describe the characterization of EhaG, a TAA identified from enterohemorrhagic
Url:
DOI: 10.1128/AEM.06680-11
PubMed: 22286983
PubMed Central: 3302597
Affiliations:
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<front><div type="abstract" xml:lang="en"><p>Trimeric autotransporter proteins (TAAs) are important virulence factors of many Gram-negative bacterial pathogens. A common feature of most TAAs is the ability to mediate adherence to eukaryotic cells or extracellular matrix (ECM) proteins via a cell surface-exposed passenger domain. Here we describe the characterization of EhaG, a TAA identified from enterohemorrhagic <named-content content-type="genus-species">Escherichia coli</named-content>
(EHEC) O157:H7. EhaG is a positional orthologue of the recently characterized UpaG TAA from uropathogenic <named-content content-type="genus-species">E. coli</named-content>
(UPEC). Similarly to UpaG, EhaG localized at the bacterial cell surface and promoted cell aggregation, biofilm formation, and adherence to a range of ECM proteins. However, the two orthologues display differential cellular binding: EhaG mediates specific adhesion to colorectal epithelial cells while UpaG promotes specific binding to bladder epithelial cells. The EhaG and UpaG TAAs contain extensive sequence divergence in their respective passenger domains that could account for these differences. Indeed, sequence analyses of UpaG and EhaG homologues from several <named-content content-type="genus-species">E. coli</named-content>
genomes revealed grouping of the proteins in clades almost exclusively represented by distinct <named-content content-type="genus-species">E. coli</named-content>
pathotypes. The expression of EhaG (in EHEC) and UpaG (in UPEC) was also investigated and shown to be significantly enhanced in an <italic>hns</italic>
isogenic mutant, suggesting that H-NS acts as a negative regulator of both TAAs. Thus, while the EhaG and UpaG TAAs contain some conserved binding and regulatory features, they also possess important differences that correlate with the distinct pathogenic lifestyles of EHEC and UPEC.</p>
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<title-group><article-title>Molecular Characterization of the EhaG and UpaG Trimeric Autotransporter Proteins from Pathogenic <named-content content-type="genus-species">Escherichia coli</named-content>
</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Totsika</surname>
<given-names>Makrina</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wells</surname>
<given-names>Timothy J.</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Beloin</surname>
<given-names>Christophe</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
<xref ref-type="aff" rid="aff3"><sup>c</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Valle</surname>
<given-names>Jaione</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
<xref ref-type="author-notes" rid="FN1">*</xref>
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<contrib contrib-type="author"><name><surname>Allsopp</surname>
<given-names>Luke P.</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>King</surname>
<given-names>Nathan P.</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Ghigo</surname>
<given-names>Jean-Marc</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
<xref ref-type="aff" rid="aff3"><sup>c</sup>
</xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Schembri</surname>
<given-names>Mark A.</given-names>
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<xref ref-type="aff" rid="aff1"><sup>a</sup>
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</contrib>
<aff id="aff1"><label>a</label>
Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, QLD, Australia</aff>
<aff id="aff2"><label>b</label>
Institut Pasteur, Unité de Génétique des Biofilms, Département de Microbiologie, Paris, France</aff>
<aff id="aff3"><label>c</label>
CNRS, URA2172, Paris, France</aff>
</contrib-group>
<author-notes><corresp>Address correspondence to Mark A. Schembri, <email>m.schembri@uq.edu.au</email>
.</corresp>
<fn id="FN1" fn-type="present-address"><label>*</label>
<p>Present address: Laboratory of Microbial Biofilms, Instituto de Agrobiotecnologia, Universidad Pública de Navarra-CSIC-Gobierno de Navarra, Pamplona, Spain.</p>
</fn>
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<pub-date pub-type="ppub"><month>4</month>
<year>2012</year>
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<volume>78</volume>
<issue>7</issue>
<fpage>2179</fpage>
<lpage>2189</lpage>
<history><date date-type="received"><day>30</day>
<month>8</month>
<year>2011</year>
</date>
<date date-type="accepted"><day>17</day>
<month>1</month>
<year>2012</year>
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<abstract><p>Trimeric autotransporter proteins (TAAs) are important virulence factors of many Gram-negative bacterial pathogens. A common feature of most TAAs is the ability to mediate adherence to eukaryotic cells or extracellular matrix (ECM) proteins via a cell surface-exposed passenger domain. Here we describe the characterization of EhaG, a TAA identified from enterohemorrhagic <named-content content-type="genus-species">Escherichia coli</named-content>
(EHEC) O157:H7. EhaG is a positional orthologue of the recently characterized UpaG TAA from uropathogenic <named-content content-type="genus-species">E. coli</named-content>
(UPEC). Similarly to UpaG, EhaG localized at the bacterial cell surface and promoted cell aggregation, biofilm formation, and adherence to a range of ECM proteins. However, the two orthologues display differential cellular binding: EhaG mediates specific adhesion to colorectal epithelial cells while UpaG promotes specific binding to bladder epithelial cells. The EhaG and UpaG TAAs contain extensive sequence divergence in their respective passenger domains that could account for these differences. Indeed, sequence analyses of UpaG and EhaG homologues from several <named-content content-type="genus-species">E. coli</named-content>
genomes revealed grouping of the proteins in clades almost exclusively represented by distinct <named-content content-type="genus-species">E. coli</named-content>
pathotypes. The expression of EhaG (in EHEC) and UpaG (in UPEC) was also investigated and shown to be significantly enhanced in an <italic>hns</italic>
isogenic mutant, suggesting that H-NS acts as a negative regulator of both TAAs. Thus, while the EhaG and UpaG TAAs contain some conserved binding and regulatory features, they also possess important differences that correlate with the distinct pathogenic lifestyles of EHEC and UPEC.</p>
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