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All subtypes of the cytotoxin VacA adsorb to the surface of Helicobacter pylori post-secretion

Nicola Fitchen¹, Darren P Letley^1,2, Paul O'Shea³, John C Atherton^1,2, Paul Williams¹ and Kim R Hardie¹

¹Institute of Infection, Immunity, and Inflammation, University of Nottingham, Centre for Biomolecular Sciences, University Park, Nottingham NG7 2RH, UK ²Wolfson Digestive Diseases Centre, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK ³School of Biomedical Sciences, Queen's Medical School, Nottingham NG7 2UH, UK

Correspondence Kim R. Hardie kim.hardie{at}nottingham.ac.uk

Received November 1, 2004
Accepted March 17, 2005

The major secreted virulence factor of Helicobacter pylori, the vacuolating cytotoxin VacA, is known to insert into eukaryotic membranes and has been observed in association with the surface of H. pylori cells that are actively producing it. Here, it is demonstrated that VacA is capable of interacting with the surface of H. pylori and Escherichia coli after secretion. It is shown that this interaction is resistant to disruption of electrostatic and hydrophobic forces, and that it appears to occur despite truncation of LPS and the removal of trypsin-accessible surface proteins. Adsorption to bacterial cell surfaces was independent of the VacA subtype, suggesting that it is not mediated through recognition of a known receptor by the VacA p58 subunit. Similarly, adsorption to bacterial cell surfaces is unlikely to be instigated by the extreme N-terminus of VacA, since a hydrophilic extension at this location that is known to disrupt VacA-induced vacuolation did not interfere with adsorption to H. pylori cells.

Abbreviations: FPE, fluorescein phosphatidylethanolamine; RPTP, receptor-like protein tyrosine phosphatases.

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