Open AccessThe 32‐kDa glycoprotein of Chlamydia trachomatis is an acidic protein that may be involved in the attachment process
Author(s) -
Swanson Albertina F.,
Kuo Chochou
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07209.x
Subject(s) - glycoprotein , glycan , chlamydia trachomatis , antiserum , biochemistry , mannose , biology , bacterial outer membrane , monoclonal antibody , galactose , microbiology and biotechnology , chemistry , antibody , escherichia coli , virology , gene , immunology
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.