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Botulinum ADP‐ribosyltransferase C3 but not botulinum neurotoxins C1 and D ADP‐ribosylates low molecular mass GTP‐binding proteins
Author(s) -
Rösener S.,
Chhatwal G.S.,
Aktories K.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80418-0
Subject(s) - adp ribosylation , neurotoxin , gtp' , clostridium botulinum , biochemistry , botulinum neurotoxin , chemistry , g protein , gtp binding protein regulators , toxin , biology , enzyme , receptor , nad+ kinase
Botulinum ADP‐ribosyltransferase C3 modified 21‐24 kDa proteins in a guanine nucleotide‐dependent manner similar to that described for botulinum neurotoxin C1 and D. Whereas GTP and GTPγS stimulated C3‐catalyzed ADP‐ribosylation in the absence of Mg 2+ , in the presence of added Mg 2+ ADP‐ribosylation was impaired by GTPγS. C3 was about 1000‐fold more potent than botulinum C1 neurotoxin in ADP‐ribosylation of the 21–24 kDa protein(s) in human platelet membranes. Antibodies raised against C3 blocked ADP‐ribosylation of the 21–24 kDa protein by C3 and neurotoxin C1 but neither cross reacted with neurotoxin C1 immunoblots nor neutralized the toxicity of neurotoxin C1 in mice. The data indicate that the ADP‐ribosylation of low molecular mass GTP‐binding proteins in various eukaryotic cells is not caused by botulinum neurotoxins but is due to the action of botulinum ADP‐ribosyltransferase C3. The weak enzymatic activities described for botulinum neurotoxins appear to be due to the contamination of C1 and D preparations with ADP‐ribosyltransferase C3.