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.
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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.
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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.
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