By Karen K. Hill, Theresa J. Smith (auth.), Andreas Rummel, Thomas Binz (eds.)
The super effective substance botulinum neurotoxin (BoNT) has attracted a lot curiosity in different fields. initially pointed out as reason for the infrequent yet lethal disorder botulism, army and terrorist meant to misuse this subtle molecule as organic weapon. This brought on its class as pick out agent type A by way of the facilities for ailments regulate and Prevention and the directory within the organic and Toxin guns conference. Later, the civilian use of BoNT as lengthy performing peripheral muscle relaxant has became this molecule into an critical pharmaceutical worldwide with annual sales >$1.5 billion. additionally easy scientists price the botulinum neurotoxin as molecular device for dissecting mechanisms of exocytosis. This e-book will disguise the latest molecular info of botulinum neurotoxin, its mechanism of motion in addition to its detection and application.
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Extra info for Botulinum Neurotoxins
Trends Biochem Sci 11:314–317 Montecucco C, Rossetto O, Schiavo G (2004) Presynaptic receptor arrays for clostridial neurotoxins. Trends Microbiol 12:442–446 Montecucco C, Schiavo G (1995) Structure and function of tetanus and botulinum neurotoxins. Q Rev Biophys 28:423–472 Mueller DS, Kampmann T, Yennamalli R, Young PR, Kobe B, Mark AE (2008) Histidine protonation and the activation of viral fusion proteins. Biochem Soc Trans 36:43–45 Mukherjee J, Tremblay JM, Leysath CE, Ofori K, Baldwin K, Feng X, Bedenice D, Webb RP, Wright PM, Smith LA, Tzipori S, Shoemaker CB (2012) A novel strategy for development of recombinant antitoxin therapeutics tested in a mouse botulism model.
However, there is a large gap in our understanding of the critical events that precede the BoNT–neuron interaction, the most important of which is how the inherently fragile BoNTs survive the harsh environment (low pH, protease-rich) of the gastrointestinal (GI) tract and cross the intestinal epithelial barrier to enter the bloodstream. The mechanism by which this is accomplished involves the secret weapons of BoNTs; the progenitor toxin complexes (PTCs). PTCs are high molecular weight (up to *900 kDa) multiprotein complexes produced by C.
9, respectively. Protonation of these residues has been reported to be involved in low pH-sensing in the pH-gated urea channel, chloride channel, histidine kinases, and viral membrane fusion proteins (Mueller et al. 2008; Perez and Groisman 2007; Stroffekova et al. 1998; Weeks and Sachs 2001). Using structure-based mutagenesis and in vitro binding assays, Glu982 and Asp1037 of BoNT/A were identified as two key residues that mediate the pHdependent binding between BoNT/A and NTNHA-A. A surface electrostatic potential analysis showed that Glu982 and Asp1037 are located in a generally positively charged surface in HC, whereas the opposing NTNHA surface is negatively charged.