Analysis of automatically generated peptide mass fingerprints of cellular proteins and antigens from Helicobacter pylori 26695 separated by two-dimensional electrophoresis

doi:10.1074/mcp.M300077-MCP200

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Submitted on August 14, 2003
Revised on September 29, 2003
Accepted on September 29, 2003

Analysis of automatically generated peptide mass fingerprints of cellular proteins and antigens from Helicobacter pylori 26695 separated by two-dimensional electrophoresis

Alexander Krah, Frank Schmidt, Dorte Bechner, Monika Schmid, Dirk Albrecht, Axel Rack, Knut Buttner, and Peter R. Jungblut

Campus Charite Mitte, Max Planck Institute for Infection Biology, Berlin, Berlin 10117

Corresponding Author: krah{at}mpiib-berlin.mpg.de

Helicobacter pylori is a causative agent of severe diseases of the gastric tract ranging from chronic gastritis to gastric cancer. Cellular proteins of H. pylori were separated by high-resolution two-dimensional gel electrophoresis. A data set of 384 spots was automatically picked, digested, spotted and analyzed by MALDI-MS peptide mass fingerprint in triple replicates. This procedure resulted in 960 evaluable MS spectra. Using a new version of our data analysis software MS-Screener we improved identification and tested reliability of automatically generated data by comparing with manually produced data. Antigenic proteins from H. pylori are candidates for vaccines and diagnostic tests. Previous immunoproteomics studies of our group revealed antigen candidates and 24 of them were now closely analyzed using the MS-Screener software. Only in three spots minor components were found that may have influenced their antigenicities. These findings affirm the value of immunoproteomics as hypothesis-free approach. Additionally, the protein species distribution of the known antigen GroEL was investigated, dimers of the protein alkyl hydroperoxide reductase were found, and the fragmentation of gamma-glutamyltranspeptidase was demonstrated

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