Binding of Chlamydia trachomatis serovar L2 to collagen types I and IV, fibronectin, heparan sulphate, laminin and vitronectin.
Chlamydia trachomatis serovar L2 elementary bodies were tested for binding to 125I-labelled components of the extracellular matrix. C. trachomatis bound high levels of collagen type I and heparan sulphate, whereas the binding to collagen type IV, fibronectin, laminin and vitronectin was substantially less. Preliminary characterization showed that chlamydial surface proteins are essential for binding to occur. Our results suggest that a selective affinity for C. trachomatis to a limited number of components of the extracellular matrix may have important implications mediating attachment to host cell surfaces and localization of chlamydiae in other tissues, such as joints.
D001422:Bacterial Adhesion; D002692:Chlamydia trachomatis / Q000378:metabolism*; D003094:Collagen / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D006497:Heparan Sulfate / Q000378:metabolism; D007797:Laminin / Q000378:metabolism; D019096:Vitronectin
D003094:Collagen; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D006023:Glycoproteins; D006497:Heparan Sulfate; D007797:Laminin; D019096:Vitronectin