Multivalent binding of toxin A from Clostridium difficile to carbohydrate receptors.
A specific monoclonal antibody against toxin A from Clostridium difficile was generated that did not show thermolabile binding. Nonspecific murine monoclonal antibodies bound toxin A at 4 degrees C, but less effectively at 37 degrees C. Nonspecific human monoclonal antibodies did not bind to toxin A at 4 degrees C. Cytotoxic properties of purified toxin A were not inhibited by Bandeiraea simplicifolia lectin. This points to a carbohydrate moiety on the cell surface and a multivalent nonspecific carbohydrate binding ligand on toxin A.
Wolfhagen
M J
MJ
Eijkman-Winkler Laboratory for Medical Microbiology, Ultrecht, The Netherlands.
Torensma
R
R
Fluit
A C
AC
Aarsman
C J
CJ
Jansze
M
M
Verhoef
J
J
D000818:Animals; D000918:Antibody Specificity; D001427:Bacterial Toxins / Q000378:metabolism*; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002478:Cells, Cultured; D002522:Chlorocebus aethiops; D016360:Clostridioides difficile; D004768:Enterotoxins / Q000378:metabolism*; D005260:Female; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D011956:Receptors, Cell Surface / Q000378:metabolism*; D014709:Vero Cells
D001427:Bacterial Toxins; D004768:Enterotoxins; D011956:Receptors, Cell Surface; C041348:tcdA protein, Clostridium difficile