The 32-kDa glycoprotein of Chlamydia trachomatis is an acidic protein that may be involved in the attachment process |
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Authors: | Albertina F Swanson Cho-chou Kuo |
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Institution: | Department of Pathobiology, SC-38, University of Washington, Seattle, Washington 98195, USA |
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Abstract: | Abstract The 32-kDa glycoprotein of Chlamydia trachomatis was shown to have a p I of 6.2 to 6.4 which distinguished this protein from the chlamydial histone-like protein of similar molecular mass that has a p I 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. |
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Keywords: | Chlamydia trachomatis 32-kDa Protein Glycoprotein Glycan Binding ligand |
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