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Proteome Analysis of Secreted Proteins of the Gastric Pathogen Helicobacter pylori

Department of Molecular Biology,¹ Central Core Facility for Protein Analysis, Max-Planck-Institute for Infection Biology,² Charité, Institute for Biochemistry, Berlin, Germany³

Received 5 December 2001/ Returned for modification 14 January 2002/ Accepted 21 March 2002

Secreted proteins (the secretome) of the human pathogen Helicobacter pylori may mediate important pathogen-host interactions, but such proteins are technically difficult to analyze. Here, we report on a comprehensive secretome analysis that uses protein-free culture conditions to minimize autolysis, an efficient recovery method for extracellular proteins, and two-dimensional gel electrophoresis followed by peptide mass fingerprinting for protein resolution and identification. Twenty-six of the 33 separated secreted proteins were identified. Among them were six putative oxidoreductases that may be involved in the modification of protein-disulfide bonds, three flagellar proteins, three defined fragments of the vacuolating toxin VacA, the serine protease HtrA, and eight proteins of unknown function. A cleavage site for the amino-terminal passenger domain of VacA between amino acids 991 and 992 was determined by collision-induced dissociation mass spectrometry. Several of the secreted proteins are interesting targets for antimicrobial chemotherapy and vaccine development.

Editor: E. I. Tuomanen

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