Analysis of proteins in Chlamydia trachomatis L2 outer membrane complex, COMC

Svend Birkelund; Marie Morgan-Fisher; Evy Timmerman; Kris Gevaert; Allan C Shaw; Gunna Christiansen

doi:10.1111/j.1574-695X.2009.00522.x

Analysis of proteins in Chlamydia trachomatis L2 outer membrane complex, COMC

Svend Birkelund, Marie Morgan-Fisher, Evy Timmerman, Kris Gevaert, Allan C Shaw, Gunna Christiansen

Nutritional Immunology

20 Citations (Scopus)

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.

Original language	English
Journal	FEMS Immunology and Medical Microbiology
Volume	55
Issue number	2
Pages (from-to)	187-95
Number of pages	8
ISSN	0928-8244
DOIs	https://doi.org/10.1111/j.1574-695X.2009.00522.x
Publication status	Published - 2009

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10.1111/j.1574-695X.2009.00522.x

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title = "Analysis of proteins in Chlamydia trachomatis L2 outer membrane complex, COMC",

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.",

author = "Svend Birkelund and Marie Morgan-Fisher and Evy Timmerman and Kris Gevaert and Shaw, {Allan C} and Gunna Christiansen",

note = "Keywords: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Base Sequence; Chlamydia trachomatis; Chromatography, Liquid; Electrophoresis, Gel, Two-Dimensional; Epithelial Cells; Hela Cells; Humans; Molecular Sequence Data; Porins; Tandem Mass Spectrometry",

year = "2009",

doi = "10.1111/j.1574-695X.2009.00522.x",

language = "English",

volume = "55",

pages = "187--95",

journal = "Pathogens and Disease",

issn = "2049-632X",

publisher = "Wiley-Blackwell",

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TY - JOUR

T1 - Analysis of proteins in Chlamydia trachomatis L2 outer membrane complex, COMC

AU - Birkelund, Svend

AU - Morgan-Fisher, Marie

AU - Timmerman, Evy

AU - Gevaert, Kris

AU - Shaw, Allan C

AU - Christiansen, Gunna

N1 - Keywords: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Base Sequence; Chlamydia trachomatis; Chromatography, Liquid; Electrophoresis, Gel, Two-Dimensional; Epithelial Cells; Hela Cells; Humans; Molecular Sequence Data; Porins; Tandem Mass Spectrometry

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

U2 - 10.1111/j.1574-695X.2009.00522.x

DO - 10.1111/j.1574-695X.2009.00522.x

M3 - Journal article

C2 - 19187221

SN - 2049-632X

VL - 55

SP - 187

EP - 195

JO - Pathogens and Disease

JF - Pathogens and Disease

IS - 2

ER -

Analysis of proteins in Chlamydia trachomatis L2 outer membrane complex, COMC

Abstract

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