Molecular characterization of the EhaG and UpaG trimeric autotransporter proteins from pathogenic Escherichia coli

Totsika, Makrina, Wells, Timothy J., Beloin, Christophe, Valle, Jaione, Allsopp, Luke P., King, Nathan P., Ghigo, Jean-Marc and Schembri, Mark A. (2012) Molecular characterization of the EhaG and UpaG trimeric autotransporter proteins from pathogenic Escherichia coli. Applied and Environmental Microbiology, 78 7: 2179-2189. doi:10.1128/AEM.06680-11

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Author Totsika, Makrina
Wells, Timothy J.
Beloin, Christophe
Valle, Jaione
Allsopp, Luke P.
King, Nathan P.
Ghigo, Jean-Marc
Schembri, Mark A.
Title Molecular characterization of the EhaG and UpaG trimeric autotransporter proteins from pathogenic Escherichia coli
Formatted title
Molecular characterization of the EhaG and UpaG trimeric autotransporter proteins from pathogenic Escherichia coli
Journal name Applied and Environmental Microbiology   Check publisher's open access policy
ISSN 0099-2240
1098-5336
Publication date 2012-04
Sub-type Article (original research)
DOI 10.1128/AEM.06680-11
Open Access Status File (Publisher version)
Volume 78
Issue 7
Start page 2179
End page 2189
Total pages 11
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2013
Language eng
Formatted abstract
Trimeric autotransporter proteins (TAAs) are important virulence factors of many Gram
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 Escherichia coli (EHEC) O157:H7. EhaG is a positional orthologue of the recently characterized UpaG TAA from uropathogenic E. coli (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 E. coli genomes revealed grouping of the proteins in clades almost exclusively represented by distinct E. coli pathotypes. The expression of EhaG (in EHEC) and UpaG (in UPEC) was also investigated and shown to be significantly enhanced in an hns 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.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Supplemental material (read only) - http://aem.asm.org/content/78/7/2179/suppl/DC1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Thu, 02 Feb 2012, 10:45:25 EST by Lucy O'Brien on behalf of School of Chemistry & Molecular Biosciences