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Toxins 2010, 2(1), 1-9; doi:10.3390/toxins2010001
Article

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

1,* , 1
 and
2
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.
Keywords: protein domain; neurotoxin; BoNT serotypes; coiled-coil domain; phylogenetic protein domain; neurotoxin; BoNT serotypes; coiled-coil domain; phylogenetic
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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