The Escherichia coli O157:H7 EhaB autotransporter protein binds to laminin and collagen I and induces a serum IgA response in O157:H7 challenged cattle

Wells, Timothy J., McNeilly, Tom N., Totsika, Makrina, Mahajan, Arvind, Gally, David L. and Schembri, Mark A. (2009) The Escherichia coli O157:H7 EhaB autotransporter protein binds to laminin and collagen I and induces a serum IgA response in O157:H7 challenged cattle. Environmental Microbiology, 11 7: 1803-1814. doi:10.1111/j.1462-2920.2009.01905.x


Author Wells, Timothy J.
McNeilly, Tom N.
Totsika, Makrina
Mahajan, Arvind
Gally, David L.
Schembri, Mark A.
Title The Escherichia coli O157:H7 EhaB autotransporter protein binds to laminin and collagen I and induces a serum IgA response in O157:H7 challenged cattle
Formatted title
The Escherichia coli O157:H7 EhaB autotransporter protein binds a laminin and collagen I and induces a serum IgA response in O157:H7 challenged cattle
Journal name Environmental Microbiology   Check publisher's open access policy
ISSN 1462-2912
1462-2920
Publication date 2009-03-31
Year available 2009
Sub-type Article (original research)
DOI 10.1111/j.1462-2920.2009.01905.x
Open Access Status DOI
Volume 11
Issue 7
Start page 1803
End page 1814
Total pages 12
Editor David A Stahl
Kenneth N Timmis
Place of publication United Kingdom
Publisher Wiley-Blackwell Publishing
Language eng
Subject C1
110801 Medical Bacteriology
920109 Infectious Diseases
Abstract P>Enterohaemorrhagic Escherichia coli (EHEC) are a subgroup of Shiga toxin-producing E. coli that cause gastrointestinal disease with the potential for life-threatening sequelae. Cattle serve as the natural reservoir for EHEC and outbreaks occur sporadically as a result of contaminated beef and other farming products. While certain EHEC virulence mechanisms have been extensively studied, the factors that mediate host colonization are poorly defined. Previously, we identified four proteins (EhaA,B,C,D) from the prototypic EHEC strain EDL933 that belong to the autotransporter (AT) family. Here we characterize the EhaB AT protein. EhaB was shown to be located at the cell surface and overexpression in E. coli K-12 resulted in significant biofilm formation under continuous flow conditions. Overexpression of EhaB in E. coli K12 and EDL933 backgrounds also promoted adhesion to the extracellular matrix proteins collagen I and laminin. An EhaB-specific antibody revealed that EhaB is expressed in E. coli EDL933 following in vitro growth. EhaB also cross-reacted with serum IgA from cattle challenged with E. coli O157:H7, indicating that EhaB is expressed in vivo and elicits a host IgA immune response.
Keyword Human Epithelial-Cells
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID DP0557615
LK0666
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
School of Chemistry and Molecular Biosciences
 
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Created: Thu, 03 Sep 2009, 17:54:05 EST by Mr Andrew Martlew on behalf of School of Chemistry & Molecular Biosciences