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The Hek Outer Membrane Protein of Escherichia coli Strain RS218 Binds to Proteoglycan and Utilizes a Single Extracellular Loop for Adherence, Invasion, and Autoaggregation

Robert P. Fagan,^2, Matthew A. Lambert,^1,2 and Stephen G. J. Smith^1,2,3*

Department of Clinical Microbiology, Trinity College Dublin, St James's Hospital, Dublin 8, Ireland,¹ Department of Microbiology, Moyne Institute, Trinity College Dublin, Dublin 2, Ireland,² Institute for Molecular Medicine, Trinity Centre, Trinity College Dublin, St James's Hospital, Dublin 8, Ireland³

Received 3 October 2007/ Returned for modification 1 November 2007/ Accepted 17 December 2007

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.

Published ahead of print on 26 December 2007.

Editor: B. A. McCormick

Present address: Centre for Molecular Microbiology and Infection, Imperial College London, London SW7 2AZ, United Kingdom.