IAI Accepts, published online ahead of print on 22 June 2009

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Infect. Immun. doi:10.1128/IAI.00364-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Outer membrane protein (OMP) expression profile in Helicobacter pylori clinical isolates

Stefan Odenbreit, Kirstin Swoboda, Iris Barwig, Stefan Ruhl, Thomas Borén, Sibylle Koletzko, and Rainer Haas^*

Max von Pettenkofer-Institute for Hygiene and Medical Microbiology, Ludwig-Maximilians-University Munich, Pettenkoferstr. 9a, D-80336 Munich, Germany; Department of Oral Biology, School of Dental Medicine, State University of New York at Buffalo, Buffalo, NY, USA; Department Medical Biochemistry and Biophysics Umeå University, SE-901 87 Umeå, Sweden; Dr. von Haunersches Kinderspital, Div. Pediatric Gastroenterology, Ludwig-Maximilians-University Munich, Germany

^* To whom correspondence should be addressed. Email: haas{at}mvp.uni-muenchen.de.

The Gram-negative gastric pathogen Helicobacter pylori is equipped with an extraordinarily large set of outer membrane proteins (OMPs), the role of which in the infection process is not well understood. The Hop (Helicobacter outer membrane porins) and the Hor (Hop-related proteins) group constitute a large paralogous family consisting of 33 members. The OMPs AlpA, AlpB, BabA SabA and HopZ have been identified as adhesins or adherence-associated proteins. To better understand the relevance of these and other OMPs during infection, we analysed the expression of eight different omp genes (alpA, alpB, babA, babB, babC, sabA, hopM and oipA) in a set of 200 patient isolates mostly from symptomatic children or young adults. Virtually all clinical isolates produced the AlpA and AlpB proteins, supporting their essential function. All other OMPs were produced in extremely variable rates, ranging between 35% and 73%, indicating a function in close adaptation to the individual host or gastric niche. In 11% of the isolates BabA and in 5% SabA was produced, but the strains failed to bind their cognate substrates. Interleukin-8 (IL-8) expression in gastric cells was strictly dependent on the presence of the cag pathogenicity island (cag-PAI), whereas the presence of OipA clearly enhanced IL-8 production. The presence of the translocated effector protein CagA correlated well with BabA and OipA production. In conclusion, we find an unexpectedly diverse omp expression profile in individual H. pylori strains and hypothesize that this reflects the selective pressure for adhesion, which may differ across different hosts as well as within an individual over time.