Protein Domain Analysis of C. botulinum Type A Neurotoxin and Its Relationship with Other Botulinum Serotypes
Autor: | Hem D. Shukla, Uma Basavanna, Shashi Sharma |
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Rok vydání: | 2009 |
Předmět: |
Botulinum Toxins
Synaptosomal-Associated Protein 25 Synaptobrevin Health Toxicology and Mutagenesis Protein domain Serogroup Toxicology medicine.disease_cause Cleavage (embryo) Article Microbiology Clostridium botulinum medicine Neurotoxin Syntaxin Botulinum Toxins Type A Phylogeny biology protein domain neurotoxin Botulinum toxin Protein Structure Tertiary BoNT serotypes coiled-coil domain nervous system Biochemistry biology.protein phylogenetic Antibody medicine.drug |
Zdroj: | Toxins Volume 2 Issue 1 Pages 1-9 |
ISSN: | 2072-6651 |
Popis: | Botulinum neurotoxins (BoNTs) are highly potent poisons produced by seven serotypes of Clostridium botulinum. The mechanism of neurotoxin action is a multistep process which leads to the cleavage of one of three different SNARE proteins essential for synaptic vesicle fusion and transmission of the nerve signals to muscles: synaptobrevin, syntaxin, or SNAP-25. In order to understand the precise mechanism of neurotoxin in a host, the domain structure of the neurotoxin was analyzed among different serotypes of C. botulinum. The results indicate that neurotoxins type A, C, D, E and F contain a coiled-coil domain while types B and type G neurotoxin do not. Interestingly, phylogenetic analysis based on neurotoxin sequences has further confirmed that serotypes B and G are closely related. These results suggest that neurotoxin has multi-domain structure, and coiled-coil domain plays an important role in oligomerisation of the neurotoxin. Domain analysis may help to identify effective antibodies to treat Botulinum toxin intoxication. |
Databáze: | OpenAIRE |
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