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Analysis of proteins in Chlamydia trachomatis L2 outer membrane complex, COMC
Author(s) -
Birkelund Svend,
MorganFisher Marie,
Timmerman Evy,
Gevaert Kris,
Shaw Allan C.,
Christiansen Gunna
Publication year - 2009
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.2009.00522.x
Subject(s) - bacterial outer membrane , porin , biology , chlamydia trachomatis , membrane protein , biochemistry , peptide sequence , affinity chromatography , microbiology and biotechnology , membrane , escherichia coli , virology , gene , enzyme
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.

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