protein domain analysis of c. botulinum type a neurotoxin and its relationship with other botulinum serotypes肉毒蛋白质域分析c型肉毒神经毒素及其关系与其他血清型.pdfVIP

Toxins 2010, 2, 1-9; doi:10.3390/toxins2010001 OPEN ACCESS toxins ISSN 2072-6651 /journal/toxins Article Protein Domain Analysis of C. botulinum Type A Neurotoxin and Its Relationship with Other Botulinum Serotypes Shashi K. Sharma 1,*, Uma Basavanna 1 and Hem D. Shukla 2 1 Center for Food Safety and Applied Nutrition, Food and Drug Administration, College Park, MD 20740, USA; E-Mail: uma.basavanna@ 2 Department of Biology, Johns Hopkins University, 3400 North Charles Street Baltimore, MD 21218, USA; E-Mail: hshukla2@ * Author to whom correspondence should be addressed; E-Mail: shashi.sharma@; Tel.: +1 301 436 1570; Fax: +1 301 436 2632. Received: 2 December 2009; in revised form: 23 December 2009 / Accepted: 23 December 2009 / Published: 24 December 2009 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