Fagan, R.P., Lambert, M.A. and Smith, S.G. (2008) The hek outer membrane protein of Escherichia coli strain RS218 binds to proteoglycan and utilizes a single extracellular loop for adherence, invasion, and autoaggregation. Infection and Immunity, 76 (3). 1135 - 1142.
Abstract
Escherichia coli is the principal gram-negative causative agent of sepsis and meningitis in neonates. The pathogenesis of meningitis due to E. coli K1 involves mucosal colonization, transcytosis of epithelial cells, survival in the bloodstream, and eventually invasion of the meninges. The last two aspects have been well characterized at a molecular level. Less is known about the early stages of pathogenesis, i.e., adhesion to and invasion of epithelial cells. We have previously reported that the Hek protein causes autoaggregation and can mediate adherence to and invasion of epithelial cells. Here, we report that Hek-mediated adherence is dependent on binding to glycosoaminoglycan, in particular, heparin. The ability to hemagglutinate, autoaggregate, adhere, and invade is contingent on a putative 25-amino-acid loop that is exposed to the outside of the bacterial cells.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2008 American Society for Microbiology. Reproduced in accordance with the publisher's self-archiving policy. |
Keywords: | Adhesins, Escherichia coli; Animals; Bacterial Adhesion; Cell Line; Chondroitin Sulfates; Cricetinae; Dextran Sulfate; Epithelial Cells; Escherichia coli; Heparin; Heparitin Sulfate; Models, Molecular; Protein Binding; Protein Interaction Mapping; Protein Structure, Tertiary; Sequence Deletion |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 16 Apr 2014 13:39 |
Last Modified: | 27 Mar 2018 03:18 |
Published Version: | http://dx.doi.org/10.1128/IAI.01327-07 |
Status: | Published |
Publisher: | American Society for Microbiology |
Identification Number: | 10.1128/IAI.01327-07 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:78497 |