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Outer membrane protein expression profile in Helicobacter pylori clinical isolates
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2009 (English)In: Infection and Immunity, ISSN 0019-9567, E-ISSN 1098-5522, Vol. 77, no 9, 3782-3790 p.Article in journal (Refereed) Published
Abstract [en]

The gram-negative gastric pathogen Helicobacter pylori is equipped with an extraordinarily large set of outer membrane proteins (OMPs), whose role in the infection process is not well understood. The Hop (Helicobacter outer membrane porins) and Hor (Hop-related proteins) groups 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 analyzed 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 at extremely variable rates, ranging from 35% to 73%, indicating a function in close adaptation to the individual host or gastric niche. In 11% of the isolates, BabA was produced, and SabA was produced in 5% of the isolates, 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, 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 found unexpectedly diverse omp expression profiles 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.

Place, publisher, year, edition, pages
2009. Vol. 77, no 9, 3782-3790 p.
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Cell and Molecular Biology
URN: urn:nbn:se:umu:diva-36421DOI: 10.1128/IAI.00364-09ISI: 000269947200028PubMedID: 19546190OAI: diva2:354134
Available from: 2010-09-30 Created: 2010-09-30 Last updated: 2012-07-04Bibliographically approved

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Borén, Thomas
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Department of Medical Biochemistry and Biophysics
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