Epitope regions in the heavy chain of Clostridium botulinum type E neurotoxin recognized by monoclonal antibodies
Article Abstract:
Seventeen monoclonal antibodies (MAbs) that react with the botulinum type E neurotoxin heavy chain have been established. Five MAbs had toxin-neutralizing activity in mice. Two of the five MAbs recognized the regions at amino acid positions 731 to 787 and 811 to 897, respectively. One of the remaining three antibodies reacted with the amino acid sequence VIKAIN, at amino acid positions 663 to 668, closed by the ion channel-forming domain. The ion channel-forming domain may therefore also be associated with the blocking of acetylcholine release. The neutralizing capability of LE15-5 antibody may be due to its ability to block the binding of neurotoxin to the receptor of target cells.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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Molecular cloning of the gene encoding the mosaic neurotoxin, composed of parts of botulinum neurotoxin types C1 and D, and PCR detection of this gene from Clostridium botulinum type C organisms
Article Abstract:
The amino acid sequence of the Clostridium botulinum type C strain 6813 gene encoding the BN/C6813 neurotoxin is similar to that of the genes encoding the C1 and D neurotoxins. The gene is present on a bacteriophage DNA. The core sequence is conserved in all three neurotoxins. The C-terminal portion of BN/C6813 is 95% similar to BN/D while the rest is 95% similar to BN/C1 suggesting that BN/C6813 is a mosaic neurotoxin made up of parts of the BN/C1 and BN/D neurotoxins. It contains 1,280 amino acids and has a molecular mass of 147,817.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin
Article Abstract:
A study was conducted on the binding of the haemagglutinin of type C 16S toxin to epithelial cells of the upper small intestine of guinea pigs. The findings indicate that haemogglutinin of type C 16S toxin plays an essential role in the binding and absorption of botulinum toxin in the small intestine. Further studies are recommended on the detailed absorption mechanism of the 12S toxins.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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