Mechanism of adhesion of Alysiella bovis to glass surfaces.
Alysiella bovis adheres to surfaces by means of short, ruthenium red-staining, rod-like fimbriae. The fimbriae remain associated with the cell envelope of A. bovis, even when sonicated or exposed sequentially to toluene, Triton X-100, lysozyme, ribonuclease, and deoxyribonuclease. Adhesion of outer membrane-derived cell wall ghosts of A. bovis to glass was inhibited by IO4-, sodium dodecyl sulfate, urea, pronase, and trypsin. Protease treatment digested the fimbriae from the distal end, and exposure to sodium dodecyl sulfate depolymerized the fimbriae. Exposure of ghosts to 1% sodium dodecyl sulfate preferentially solubilized a 16,500-dalton protein which was subsequently purified by gel filtration and demonstrated to be a glycoprotein (ca. 17% carbohydrate). Antibodies raised against the 16,500-dalton glycoprotein agglutinated whole cells and inhibited adhesion of ghosts to glass.
D002250:Carbon Radioisotopes; D002462:Cell Membrane / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D010861:Fimbriae, Bacterial / Q000648:ultrastructure; D005898:Glass; D006088:Gram-Negative Aerobic Bacteria / Q000166:cytology* / Q000648:ultrastructure; D008565:Membrane Proteins / Q000032:analysis; D008854:Microscopy, Electron; D012430:Ruthenium Red
D002250:Carbon Radioisotopes; D008565:Membrane Proteins; D012430:Ruthenium Red