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Literature summary for 3.4.24.69 extracted from

  • Kukreja, R.; Chang, T.W.; Cai, S.; Lindo, P.; Riding, S.; Zhou, Y.; Ravichandran, E.; Singh, B.R.
    Immunological characterization of the subunits of type A botulinum neurotoxin and different components of its associated proteins (2009), Toxicon, 53, 616-624.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information the presence of neurotoxin associated proteins enhances the oral toxicity of the neurotoxin significantly. Hemagglutinin Hn-33 makes up the largest fraction of neurotoxin associated proteins in BoNT/AC and strongly protects BoNT/A against proteases of the gastrointestinal tract Clostridium botulinum

Application

Application Comment Organism
medicine Hn-33 and other neurotoxin associated proteins can potentially be employed as adjuvants for development of vaccines against botulism and can be a good surrogate for botulinum diagnostics. Medical implications of immunogenicity of different components of BoNT/A complex Clostridium botulinum

Cloned(Commentary)

Cloned (Comment) Organism
BoNT/A, DNA and amino acid sequence determination, BoNT/A is produced along with six neurotoxin associated proteins, including hemagglutinin Hn-33, through polycistronic expression of a clustered group of genes to form a complex, BoNT/AC. Expresssion of His-tagged BoNT/A mutant E224A/E262A in Escherichia coli Clostridium botulinum

Protein Variants

Protein Variants Comment Organism
E224A/E262A the recombinant full length botulinum type A with mutation in its two active site residues is a detoxified BoNT/A mutant since it lacks its endopeptidase activity Clostridium botulinum

Organism

Organism UniProt Comment Textmining
Clostridium botulinum
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serotype BoNT/A
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Clostridium botulinum ATCC 3502
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serotype BoNT/A
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Purification (Commentary)

Purification (Comment) Organism
native BoNT/A free and in complex. Recombinant His-tagged BoNT/A mutant E224A/E262A from Escherichia coli by nickel affinity chromatography, separation of the light and heavy chains Clostridium botulinum

Synonyms

Synonyms Comment Organism
BoNT/A
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Clostridium botulinum
More botulinum neurotoxins, BoNTs, constitute a family of seven structurally similar but antigenically distinct proteins produced by different strains of Clostridium botulinum Clostridium botulinum
type A botulinum neurotoxin
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Clostridium botulinum

General Information

General Information Comment Organism
additional information the presence of neurotoxin associated proteins enhances the oral toxicity of the neurotoxin significantly. The whole neurotoxin complex reacts 60 times better with the complex and 35 times better with Hn-33 and NAPs compared to the purified neurotoxin suggesting stronger immunogenicity of neurotoxin associated proteins over that of purified neurotoxin and a higher potential of BoNT/AC and its associated proteins to induce host immune response. BoNT/A in its purified and complex forms induces equal immunogenic response and a 2.5fold higher immunogenic response compared to BoNT/A light and heavy chains Clostridium botulinum