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ProGlyProt ID
Organism Information
Organism Name
Chlamydia trachomatis serovar L2 (strain 434/Bu)
Family: Chlamydiaceae
Order: Chlamydiales
Class: Chlamydiae
Division or phylum: "Chlamydiae"
Taxonomic ID (NCBI)
Genome Sequence(s)
Gene Information
Gene Name
ompA (CTL0050)
Protein Information
Protein Name
Major outer membrane protein (MOMP, 40 kDa)
UniProtKB/SwissProt ID
UniProtKB Sequence
Sequence length
394 AA
Subcellular Location
Membrane associated
The MOMP (40 kDa protein) is the principal structural protein of the EB (infectious elementary body). Through disulfide-mediated interactions, the MOMP provides the structural integrity to the extracellular infectious form and performs a porin-like function when Chlamydiae are intracellular and metabolically active. The serological specificity of the organism resides in MOMP, and antibodies raised against MOMP neutralize infectivity of Chlamydia.
Glycosylation Status
Glycosylation Type
N(Asn)- linked
Technique(s) used for Glycosylation Detection
Change in SDS-PAGE mobility after periodate oxidation, polysaccharide staining with p-phenylenediamine, rapid migration on SDS-PAGE after PNGaseF treatment, lectin binding (ConA, WGA, DBA), and autoradiography after metabolic labeling with [3H]glucosamine
Glycan Information
Glycan Annotation
Linkage: β-GlcNAc-N-Asn. The major fractions consisted of “high mannose type” oligosaccharides containing 8–9 mannose residues. Bi- and tri-antennary “complex type” oligosaccharides having terminal galactose were detected as minor components. These oligosaccharides were N-linked and contained no sialic acid. A specific high-mannose type oligosaccharide linked to the MOMP of C. trachomatis mediates attachment and infectivity of the organism to HeLa cells. The lectin-binding properties of MOMP and its susceptibility to glycosidase indicate that MOMP glycoprotein contains α-Man and β-GlcNAc at the terminus.
1) Kuo, C., Takahashi, N., Swanson, A.F., Ozeki, Y. and Hakomori, S. (1996) An N-linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells. J Clin Invest, 98, 2813-2818. [PubMed: 8981929]
2) Swanson, A.F. and Kuo, C.C. (1994) Binding of the glycan of the major outer membrane protein of Chlamydia trachomatis to HeLa cells. Infect Immun, 62, 24-28. [PubMed: 8262634]
3) Swanson, A.F. and Kuo, C.C. (1991) Evidence that the major outer membrane protein of Chlamydia trachomatis is glycosylated. Infect Immun, 59, 2120-2125. [PubMed: 1645328]
Year of Identification
Copyright @ 2011 IMTECH
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