1. Analysis of proteins in Chlamydia trachomatis L2 outer membrane complex, COMC.
- Author
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Birkelund S, Morgan-Fisher M, Timmerman E, Gevaert K, Shaw AC, and Christiansen G
- Subjects
- Amino Acid Sequence, Bacterial Outer Membrane Proteins isolation & purification, Base Sequence, Chromatography, Liquid, Electrophoresis, Gel, Two-Dimensional, Epithelial Cells chemistry, Epithelial Cells microbiology, HeLa Cells, Humans, Molecular Sequence Data, Porins analysis, Porins isolation & purification, Tandem Mass Spectrometry, Bacterial Outer Membrane Proteins analysis, Chlamydia trachomatis chemistry
- Abstract
The protein composition and N-terminal sequences of proteins in the outer membrane of Chlamydia trachomatis L2 were analysed following isolation of N-terminal peptides using combined fractional diagonal chromatography and identification by liquid chromatography tandem MS. Acetylation of primary amino groups of in vivo generated proteolytic cleavage sites facilitated identification of such sites in known outer membrane proteins (MOMPs). Our results further support a proposed prediction of the topology of the MOMPs. Furthermore, a previously unknown MOMP, CTL0626 (Ct372), was assigned as an MOMP with a carbohydrate-selective porin (OprB) family motif, and the presence of CTL0626 was confirmed using antibodies raised against the protein.
- Published
- 2009
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