Proteome analysis of secreted proteins of the gastric pathogen Helicobacter pylori

Bumann, D. and Aksu, S. and Wendland, M. and Janek, K. and Zimny-Arndt, U. and Sabarth, N. and Meyer, T. F. and Jungblut, P. R.. (2002) Proteome analysis of secreted proteins of the gastric pathogen Helicobacter pylori. Infection and Immunity, 70 (7). pp. 3396-3403.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5259820

Downloads: Statistics Overview


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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Infection Biology > Molecular Microbiology (Bumann)
UniBasel Contributors:Bumann, Dirk
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Microbiology
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:27 Nov 2017 09:24
Deposited On:22 Mar 2012 13:23

Repository Staff Only: item control page