Analysis of proteins in Chlamydia trachomatis L2 outer membrane complex, COMC.
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.
Birkelund
Svend
S
Institute of Medical Microbiology and Immunology, University of Aarhus, Denmark. chlam@medmicro.au.dk
Morgan-Fisher
Marie
M
Timmerman
Evy
E
Gevaert
Kris
K
Shaw
Allan C
AC
Christiansen
Gunna
G
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis* / Q000302:isolation & purification; D001483:Base Sequence; D002692:Chlamydia trachomatis / Q000737:chemistry*; D002853:Chromatography, Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D004847:Epithelial Cells / Q000737:chemistry / Q000382:microbiology; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D018272:Porins / Q000032:analysis / Q000302:isolation & purification; D053719:Tandem Mass Spectrometry
D001425:Bacterial Outer Membrane Proteins; D018272:Porins