Ultrastructural investigations on surface structures involved in Coxiella burnetii phase variation.
By using the cytochemical staining procedure with concanavalin A, horseradish peroxidase, and diaminobenzidine, no surface carbohydrates with terminal alpha-glucosyl or sterically closely related residues could be detected on the cell walls of Coxiella burnetii phases I and II. Using a polycationized ferritin derivative as a cytochemical probe, anionic binding sites were visualized in the electron microscope on cell membranes of C. burnetii phase II, but not on phase I organisms. The sites appeared to be masked in phase I particles. Anionic sites could be demonstrated on phase I organisms after treatment with NaIO4 or dimethyl sulfoxide. A number of different biological properties of C. burnetii phases I and II may depend on the presence or absence of a net negative charge on the surface of the cell walls of these organisms.
D000096:Acetone; D003165:Complement System Proteins; D003208:Concanavalin A; D003381:Coxiella / Q000648:ultrastructure*; D004121:Dimethyl Sulfoxide; D014644:Genetic Variation; D006651:Histocytochemistry; D006821:Hyaluronoglucosaminidase; D009113:Muramidase; D010544:Peroxidases; D010636:Phenols; D011402:Pronase; D013305:Streptomyces griseus / Q000201:enzymology; D014238:Trichloroacetic Acid
D010636:Phenols; D003208:Concanavalin A; D000096:Acetone; D014238:Trichloroacetic Acid; D003165:Complement System Proteins; D010544:Peroxidases; D009113:Muramidase; D006821:Hyaluronoglucosaminidase; D011402:Pronase; D004121:Dimethyl Sulfoxide