Abstract
A set of neurotoxic proteins synthesized by certain strains of Clostridium botulinum, C. butyricum, C. tetani and presumably also by C. barati, are nearly identical in macro structure. Some aspects of their fine structures and pharmacological action are strikingly similar. These proteins, one called tetanus neurotoxin and the rest botulinum neurotoxins (NT), produce in their target nerve cells similar intracellular biochemical lesions; blockage of normal release of neurotransmitters, albeit inhibitory and excitatory. Diversity in the primary, secondary and tertiary structures among these proteins makes them antigenically distinguishable and endows them with the specificity to recognize and bind to the “acceptors/receptors” present on the susceptible nerve cells. This article considers the structural aspects of this generalized theme. The structural features of botulinum NT are presented first. The temptation to keep tetanus NT in the same focus as botulinum NT could not be overcome even twelve years after pointing out for the first time the similarities between botulinum and tetanus neurotoxins.11
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© 1990 Plenum Press, New York
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DasGupta, B.R. (1990). Primary Structure and Conformation of Clostridium Botulinum Neurotoxin. In: Pohland, A.E., et al. Microbial Toxins in Foods and Feeds. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0663-4_7
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DOI: https://doi.org/10.1007/978-1-4613-0663-4_7
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