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Originally published In Press as doi:10.1074/jbc.M204473200 on May 22, 2002

J. Biol. Chem., Vol. 277, Issue 31, 27896-27902, August 2, 2002
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Identification of Surface Proteins of Helicobacter pylori by Selective Biotinylation, Affinity Purification, and Two-dimensional Gel Electrophoresis*

Nicolas Sabarth, Stefanie Lamer, Ursula Zimny-Arndt, Peter R. Jungblut, Thomas F. MeyerDagger , and Dirk Bumann

From the Max-Planck-Institut für Infektionsbiologie, Abteilung Molekulare Biologie, Schumannstrabeta e 21/22, D-10117 Berlin, Germany

Helicobacter pylori is a widespread human pathogen that can cause gastric ulcers and cancer. To identify surface proteins that may play a role in pathogen-host interactions and represent potential targets for the control of this infection, we selectively biotinylated intact H. pylori with the hydrophilic reagent sulfosuccinimidyl-6-(biotinamido)-hexanoate and purified the labeled proteins by membrane isolation, solubilization, and affinity chromatography. After separation of 82 biotinylated proteins on two-dimensional gels, 18 were identified with comparison to proteome data and peptide mass fingerprinting. Among the identified proteins, 9 have previously been shown to be surface-exposed, 7 are associated with virulence, and 11 are highly immunogenic in infected patients. In conclusion, this generally applicable combined proteome approach facilitates the rapid identification of promising targets for the control of H. pylori and might be applicable to numerous other human pathogens although larger biotinylation reagents might be required in some cases to prevent permeation of porin channels in the outer membrane.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 49-30-28460402; Fax: 49-03-28460401; E-mail: meyer@mpiib-berlin-mpg.de.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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