The 32-kDa glycoprotein of Chlamydia trachomatis is an acidic protein that may be involved in the attachment process.
The 32-kDa glycoprotein of Chlamydia trachomatis was shown to have a pI of 6.2 to 6.4 which distinguished this protein from the chlamydial histone-like protein of similar molecular mass that has a pI of > 10. The initial interaction of the glycan of 32 kDa glycoprotein and HeLa cells was also investigated. Glycan was cleaved from the protein backbone by N-glycanase and radiolabeled with tritium by sodium borohydride reduction. Competition assays showed the binding of glycan to HeLa cells was inhibited by galactose, mannose, and N-acetylglucosamine but not by sedoheptulose and fructose. Untreated and UV-treated organisms inhibited the binding, while heat-inactivated organisms did not. Binding was blocked by rabbit antiserum against whole organisms but not by rabbit anti-155-kDa antiserum or monoclonal antibodies against the lipopolysaccharide and major outer membrane protein.
Swanson
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AF
Department of Pathobiology, University of Washington, Seattle 98195.
Kuo
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CC
D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000302:isolation & purification* / Q000378:metabolism; D001667:Binding, Competitive; D002692:Chlamydia trachomatis / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D008562:Membrane Glycoproteins / Q000302:isolation & purification* / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D008562:Membrane Glycoproteins; D011134:Polysaccharides