Literature summary for 2.4.1.B62 extracted from

Roberts, A.; Shone, C.
Modification of surface histidine residues abolishes the cytotoxic activity of Clostridium difficile toxin A (2000), Toxicon, 39, 325-333.

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Protein Variants

Protein Variants	Comment	Organism
additional information	modification of toxin A with diethyl dicarbonate leads to concentration dependent labelling of histidine residues and abolishes both its cytotoxic activity and the ability of the toxin to bind Zn-Sepharose gel. Histidine modification has no effect on the glucosyl transferase enzyme activity of toxin A. However, modification abolishes the binding of toxin to bovine thyroglobulin in an ELISA and reduces ligand binding activity in a rabbit erythrocyte haemagglutination assay. The data suggest that the histidine residues may be crucial to the receptor-binding activity of toxin A	Clostridioides difficile

Organism

Organism	UniProt	Comment	Textmining
Clostridioides difficile	-	-	-
Clostridioides difficile VPI 10463	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Clostridioides difficile

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Release 2023.1 (January 2023)