Hemagglutinin‐33 of type A botulinum neurotoxin complex binds with synaptotagmin II

Botulinum neurotoxin type A (BoNT/A), the most toxic substance known to mankind, is produced by Clostridium botulinum type A as a complex with a group of neurotoxin‐associated proteins (NAPs) through polycistronic expression of a clustered group of genes. NAPs are known to protect BoNT against adver...

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Bibliographic Details
Published in:The FEBS journal 2005-06, Vol.272 (11), p.2717-2726
Main Authors: Zhou, Yu, Foss, Sean, Lindo, Paul, Sarkar, Hemanta, Singh, Bal Ram
Format: Article
Language:English
Subjects:
Bacterial Proteins - metabolism
Binding sites
Biochemistry
botulinum neurotoxin
Botulinum Toxins
Botulinum Toxins, Type A - metabolism
Botulism
Chromatography, Affinity
Clostridium
Clostridium botulinum
Clostridium botulinum - metabolism
hemagglutinin
Hemagglutinins - metabolism
Nerve Tissue Proteins - metabolism
Pharmacology
Proteins
synaptosomes
synaptotagmin
Synaptotagmin II
Toxicity
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Summary:Botulinum neurotoxin type A (BoNT/A), the most toxic substance known to mankind, is produced by Clostridium botulinum type A as a complex with a group of neurotoxin‐associated proteins (NAPs) through polycistronic expression of a clustered group of genes. NAPs are known to protect BoNT against adverse environmental conditions and proteolytic digestion. Hemagglutinin‐33 (Hn‐33) is a 33 kDa subcomponent of NAPs that is resistant to protease digestion, a feature likely to be involved in the protection of the botulinum neurotoxin from proteolysis. However, it is not known whether Hn‐33 plays any role other than the protection of BoNT. Using immunoaffinity column chromatography and pull‐down assays, we have now discovered that Hn‐33 binds to synaptotagmin II, the putative receptor of botulinum neurotoxin. This finding provides important information relevant to the design of novel antibotulism therapeutic agents targeted to block the entry of botulinum neurotoxin into nerve cells.
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2005.04688.x