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Toxins 2010, 2(1), 1-9; https://doi.org/10.3390/toxins2010001

Protein Domain Analysis of C. botulinum Type A Neurotoxin and Its Relationship with Other Botulinum Serotypes

1
Center for Food Safety and Applied Nutrition, Food and Drug Administration, College Park, MD 20740, USA
2
Department of Biology, Johns Hopkins University, 3400 North Charles Street Baltimore, MD 21218, USA
*
Author to whom correspondence should be addressed.
Received: 2 December 2009 / Revised: 23 December 2009 / Accepted: 23 December 2009 / Published: 24 December 2009
(This article belongs to the Special Issue Neurotoxins of Biological Origin)
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Abstract

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. View Full-Text
Keywords: protein domain; neurotoxin; BoNT serotypes; coiled-coil domain; phylogenetic protein domain; neurotoxin; BoNT serotypes; coiled-coil domain; phylogenetic
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Sharma, S.K.; Basavanna, U.; Shukla, H.D. Protein Domain Analysis of C. botulinum Type A Neurotoxin and Its Relationship with Other Botulinum Serotypes. Toxins 2010, 2, 1-9.

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