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This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M700554-MCP200v1 7/8/1460    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 Google Scholar Articles by Wolff, S. Articles by Becher, D. PubMed PubMed Citation Articles by Wolff, S. Articles by Becher, D. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 7:1460-1468, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Complementary Analysis of the Vegetative Membrane Proteome of the Human Pathogen Staphylococcus aureus^*,S

Susanne Wolff, Hannes Hahne, Michael Hecker and Dörte Becher

From the Institute for Microbiology, Ernst Moritz Arndt University, D-17489 Greifswald, Germany

The Gram-positive bacterium Staphylococcus aureus is a serious human pathogen causing a wide variety of diseases, and its increasing resistance toward all available antibiotics makes its further investigation absolutely essential. We examined the membrane proteome of exponentially growing cells of S. aureus COL because this subproteome plays a major role in the virulence of the bacterium in its host. In general, an analysis of membrane proteins is impeded by their hydrophobic nature as well as by a high abundance of many cytosolic proteins. The implementation of three different technologies, one-dimensional gel-LC, two-dimensional LC, and a membrane shaving approach combined with MS/MS analyses, enabled an identification of 271 integral and 86 peripheral membrane proteins from exponentially growing cells. In particular, the latter approach that combined membrane shaving with a subsequent chymotrypsin digest of integral membrane domains of proteins greatly facilitated the detection of hydrophobic peptides derived from membrane-spanning segments (713 peptides, 60% of all peptides) and therefore yielded almost exclusively highly hydrophobic integral membrane proteins (96.7%). A comparison of the various methods disclosed the one-dimensional gel-LC and the shaving approach to be highly complementary techniques. A combination of them will reveal a most comprehensive view on membrane proteomes.

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