HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: M600363-MCP200v1 6/2/193    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pyndiah, S. Articles by Bonneu, M. Search for Related Content PubMed PubMed Citation Articles by Pyndiah, S. Articles by Bonneu, M. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 6:193-206, 2007.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Two-dimensional Blue Native/SDS Gel Electrophoresis of Multiprotein Complexes from Helicobacter pylori^*

Slovénie Pyndiah^,,¶, Jean Paul Lasserre^||, Armelle Ménard^,, Stéphane Claverol^||, Valérie Prouzet-Mauléon^,, Francis Mégraud^,,**, Frank Zerbib^, and Marc Bonneu^||

From INSERM, U853, Bordeaux, F 33076 France and the Laboratoire de Bactériologie and ^|| Pôle Protéomique, Plateforme Génomique Fonctionnelle Bordeaux, Université Victor Segalen Bordeaux 2, Bordeaux, F 33076 France

The study of protein interactions constitutes an important domain to understand the physiology and pathogenesis of microorganisms. The two-dimensional blue native/SDS-PAGE was initially reported to analyze membrane protein complexes. In this study, both cytoplasmic and membrane complexes of a bacterium, the strain J99 of the gastric pathogen Helicobacter pylori, were analyzed by this method. It was possible to identify 34 different proteins grouped in 13 multiprotein complexes, 11 from the cytoplasm and two from the membrane, either previously reported partially or totally in the literature. Besides complexes involved in H. pylori physiology, this method allowed the description of interactions involving known pathogenic factors such as (i) urease with the heat shock protein GroEL or with the putative ketol-acid reductoisomerase IlvC and (ii) the cag pathogenicity island CagA protein with the DNA gyrase GyrA as well as insight on the partners of TsaA, a peroxide reductase/stress-dependent molecular chaperone. The two-dimensional blue native/SDS-PAGE combined with mass spectrometry is a potential tool to study the differences in complexes isolated in various situations and also to study the interactions between bacterial and eucaryotic cell proteins.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				A. L. Menon, F. L. Poole II, A. Cvetkovic, S. A. Trauger, E. Kalisiak, J. W. Scott, S. Shanmukh, J. Praissman, F. E. Jenney Jr., W. R. Wikoff, et al. Novel Multiprotein Complexes Identified in the Hyperthermophilic Archaeon Pyrococcus furiosus by Non-denaturing Fractionation of the Native Proteome Mol. Cell. Proteomics, April 1, 2009; 8(4): 735 - 751. [Abstract] [Full Text] [PDF]

				K. Stingl, K. Schauer, C. Ecobichon, A. Labigne, P. Lenormand, J.-C. Rousselle, A. Namane, and H. de Reuse In Vivo Interactome of Helicobacter pylori Urease Revealed by Tandem Affinity Purification Mol. Cell. Proteomics, December 1, 2008; 7(12): 2429 - 2441. [Abstract] [Full Text] [PDF]

				C. Mendoza-Palomares, N. Biteau, C. Giroud, V. Coustou, T. Coetzer, E. Authie, A. Boulange, and T. Baltz Molecular and Biochemical Characterization of a Cathepsin B-Like Protease Family Unique to Trypanosoma congolense Eukaryot. Cell, April 1, 2008; 7(4): 684 - 697. [Abstract] [Full Text] [PDF]