Some biochemical properties of the components of Staphylococcus aureus binding to human platelets.
The binding properties of Staphylococcus aureus in relation to human platelets were investigated. Protease digestion (pronase E, proteinase K, trypsin), heat treatment (80 degrees C, 30 min), and sonication for 5 min significantly reduced the binding abilities of the staphylococcal cells to 0% (p < .01), 50 +/- 5% (p < .05), and 38 +/- 9% (p < .05), respectively, while mixed glycosidases did not. Inhibition experiments indicated that protein A and various sugars were ineffective. A binding study using biotinylated cell surface fractions extracted from the whole cells of S. aureus indicated that the proteins having apparent molecular weights of 14400 and 16500 estimated by sodium dodecylsulfate-polyacrylamide gel electrophoresis were involved in the binding between S. aureus and human platelets.
Usui
Y
Y
Department of Microbiology, St. Marianna University, School of Medicine, Kawasaki, Japan.
Ohshima
Y
Y
Ichiman
Y
Y
Ohtomo
T
T
Shimada
J
J
D001422:Bacterial Adhesion / Q000187:drug effects; D001710:Biotin / Q000031:analogs & derivatives; D001792:Blood Platelets / Q000737:chemistry / Q000382:microbiology* / Q000502:physiology; D002241:Carbohydrates / Q000494:pharmacology; D002458:Cell Fractionation; D002462:Cell Membrane / Q000737:chemistry; D010450:Endopeptidases / Q000494:pharmacology; D006358:Hot Temperature; D006801:Humans; D013010:Sonication; D013205:Staphylococcal Protein A / Q000494:pharmacology; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000502:physiology; D013388:Succinimides
D002241:Carbohydrates; D013205:Staphylococcal Protein A; D013388:Succinimides; C053827:biotinyl-N-hydroxysulfosuccinimide ester; D001710:Biotin; D010450:Endopeptidases