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Infect. Immun. doi:10.1128/IAI.01327-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The Hek outer membrane protein of Escherichia coli strain RS218 binds to proteoglycan and utilizes a single extracellular loop for adherence, invasion and autoaggregation

Department of Clinical Microbiology, Trinity College Dublin, St James's Hospital, Dublin 8, Ireland; Department of Microbiology, Moyne Institute, Trinity College Dublin, Dublin 2, Ireland; Institute for Molecular Medicine, Trinity Centre, Trinity College Dublin, St James's Hospital, Dublin 8, Ireland

^* To whom correspondence should be addressed. Email: sgsmith{at}tcd.ie.

	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 blood stream and eventually invasion of the meninges. The later 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 auto-aggregation 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 haemagglutinate, autoaggregate, adhere and invade is contingent on a putative 25 amino acid loop which is exposed to the outside of the bacterial cells.