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Immuno‐crossreactivity between botulinum neurotoxin type C1 or D and exoenzyme C3
Author(s) -
Toratani Satoshi,
Yokosawa Noriko,
Yokosawa Hideyoshi,
Ishii Shin-ichi,
Oguma Keiji
Publication year - 1989
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(89)80893-2
Subject(s) - exoenzyme , neurotoxin , clostridium botulinum , immunoglobulin light chain , monoclonal antibody , polyclonal antibodies , biochemistry , epitope , peptide sequence , chemistry , toxin , biology , antibody , microbiology and biotechnology , enzyme , genetics , gene
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.