Construction of a Francisella tularensis two-dimensional electrophoresis protein database
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Electrophoresis, Gel, Two-Dimensional MeSH
- Bacterial Proteins chemistry genetics isolation & purification MeSH
- Databases, Protein * MeSH
- Francisella tularensis chemistry genetics pathogenicity MeSH
- Peptide Mapping MeSH
- Proteome chemistry genetics isolation & purification MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- In Vitro Techniques MeSH
- Virulence MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Proteome MeSH
We have started the construction of a two-dimensional database of the proteome of Francisella tularensis, a bacterium that is responsible for the highly pathogenic disease tularemia. The genome of this intracellular pathogen is not completely sequenced yet and, currently, information about only 66 proteins is available from NCBI database. We have analyzed the F. tularensis live vaccine strain by two-dimensional gel electrophoresis with immobilized pH 3-10 gradient in the first dimension and 9-16% gradient or tricine SDS-PAGE in the second dimension. In both cases about 2000 spots were detected. Furthermore, we compared the protein pattern of the nonvirulent F. tularensis live vaccine strain with protein profiles of two wild type clinical isolates and more than 50 differentially expressed proteins were counted. The separated proteins are going to be identified by peptide mass fingerprinting. However, due to the lack of complete genome sequence data only eight proteins were unambiguously identified. Among them, acid phosphatase and the most basic isoform of a hypothetical 23 kDa protein are characteristic only for virulent strains.
References provided by Crossref.org
Tularemia induces different biochemical responses in BALB/c mice and common voles
