Differential glycosaminoglycan binding of Chlamydia trachomatis OmcB protein from serovars E and LGV.
We recently showed that OmcB protein from Chlamydia trachomatis serovar LGV1 functions as an adhesin. In this study, we produced Escherichia coli expressing OmcB from serovar E and compared this OmcB to OmcB from serovar LGV1. Infectivity inhibition assays carried out with serovars LGV1 and E of C. trachomatis in the presence of recombinant OmcB showed considerable (approximately 60%) inhibition of infectivity. In the presence of heparan sulphate, there was significant inhibition (68%) of adherence of E. coli expressing OmcB from serovar LGV1 only. In a further experiment, recombinant OmcB from serovar LGV1 showed minimal binding to glycosaminoglycan (GAG)-deficient cells, whilst to the same cells, recombinant OmcB from serovar E showed binding equal to that to the wild-type cells. Our experiments strongly suggest that OmcB from serovar E, in contrast to that from serovar LGV1, is not binding to host cells through a GAG-dependent mechanism.
Fadel
Sanaa
S
Department of Microbiology, Faculty of Pharmacy, Cairo University, Egypt.|Henry Wellcome Laboratories for Medical Research, School of Medicine and Biomedical Sciences, University of Sheffield Medical School, Sheffield S10 2RX, UK.
Eley
Adrian
A
Henry Wellcome Laboratories for Medical Research, School of Medicine and Biomedical Sciences, University of Sheffield Medical School, Sheffield S10 2RX, UK.
D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D045744:Cell Line, Tumor; D002692:Chlamydia trachomatis / Q000145:classification* / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D006025:Glycosaminoglycans / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012703:Serotyping
D001425:Bacterial Outer Membrane Proteins; D006025:Glycosaminoglycans; C436968:OmcB protein, bacteria; D011994:Recombinant Proteins