Immuno-crossreactivity between botulinum neurotoxin type C1 or D and exoenzyme C3

• Published in: FEBS letters 1989, Vol.252 (1), p.83-87
• Main Authors: Toratani, Satoshi, Yokosawa, Noriko, Yokosawa, Hideyoshi, Ishii, Shin-ichi, Oguma, Keiji
• Format: Article
• Language: English
• Subjects: Adenosine Diphosphate Ribose - metabolism; ADP Ribose Transferases - immunology; ADP-ribosylation; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Antibodies, Monoclonal; Biological and medical sciences; Blotting, Western; Botulinum neurotoxin; Botulinum Toxins - immunology; Botulinum Toxins - isolation & purification; Clostridium botulinum - enzymology; Clostridium botulinum - metabolism; Cross Reactions; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Epitopes - immunology; Exoenzyme C3; Fundamental and applied biological sciences. Psychology; Miscellaneous; Molecular Sequence Data; Monoclonal antibody; Proteins
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(89)80893-2

Botulinum neurotoxin type D and exoenzyme C3 have been separately purified from Clostridium botulinum strain D-1873 to apparent homogeneity. Both ADP-ribosylated a rat liver cytosolic protein of 24 kDa. The N-terminal amino acid sequence of C3 was determined and showed a low degree of homology with those of the light and heavy chains of neurotoxins of various types which have been reported previously. However, a polyclonal antibody raised against C3 cross-reacted with the light chains, but not with the heavy chains, of type C1 and D neurotoxins. Furthermore, a monoclonal antibody recognizing the light chains of type C1 and D neurotoxins interacted with C3. These results suggest that the light chain of type C1 or D neurotoxin and exoenzyme C3 share at least one epitope in common with each other.