Sandbox WWC1: Difference between revisions
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94. </ref> <ref> Minton NP. 1995. Molecular genetics of | 94. </ref> <ref> Minton NP. 1995. Molecular genetics of | ||
clostridial neurotoxins. Curr. Top. Microbiol. | clostridial neurotoxins. Curr. Top. Microbiol. | ||
Immunol. 195:161–94 </ref> <ref> Oguma K, Fujinaga Y, Inoue K. 1995.Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 39:161–68 </ref> <ref name="Lacy"> PMID: 3722863 </ref> <ref> Popoff MR, Marvaud J-C. 1999. Structural and genomic features of clostridial neurotoxins. See Ref. 132, pp. 174– | Immunol. 195:161–94 </ref> <ref> Oguma K, Fujinaga Y, Inoue K. 1995.Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 39:161–68 </ref> <ref name="Lacy"> PMID: 3722863</ref> <ref> Popoff MR, Marvaud J-C. 1999. Structural and genomic features of clostridial neurotoxins. See Ref. 132, pp. 174– | ||
201 </ref>). | 201 </ref>). | ||
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== Function == | == Function == | ||
The active form of BTX has three functional domains responsible for binding, translocation, and catalysis <ref>Montecucco and Schiavo 1995 C. Montecucco, G. Schiavo Structure and function of tetanus and botulinum neurotoxins Quart. Rev. Biophys., 28 (1995), pp. 423–472. </ref>. The C terminus of the heavy chain is responsible for binding a ganglioside and protein receptors on the nerve terminal while the N terminus half functions by translocating the protein across the membrane by signaling endocytosis <ref>Dolly et al 1984 J.O. Dolly, J. Black, R.S. Williams, J. Melling Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization Nature, 307 (1984), pp. 457–460 </ref>. Once in a vesicle in the cytosol of a nerve terminal, the light chain dissociates from the heavy chain and cleaves SNARE proteins involved in synaptic vesicle fusion. The cleavage of these SNARE proteins, VAMP, SNAP-25, and syntax, depends on the serotype of BTX where each serotype cuts at a different place. The cut SNAREs inhibit the binding of vesicles containing acetylcholine which effectively stops the signaling from nerves to muscle cells, resulting in paralysis <ref> | The active form of BTX has three functional domains responsible for binding, translocation, and catalysis <ref>Montecucco and Schiavo 1995 C. Montecucco, G. Schiavo Structure and function of tetanus and botulinum neurotoxins Quart. Rev. Biophys., 28 (1995), pp. 423–472. </ref>. The C terminus of the heavy chain is responsible for binding a ganglioside and protein receptors on the nerve terminal while the N terminus half functions by translocating the protein across the membrane by signaling endocytosis <ref>Dolly et al 1984 J.O. Dolly, J. Black, R.S. Williams, J. Melling Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization Nature, 307 (1984), pp. 457–460 </ref>. Once in a vesicle in the cytosol of a nerve terminal, the light chain dissociates from the heavy chain and cleaves SNARE proteins involved in synaptic vesicle fusion. The cleavage of these SNARE proteins, VAMP, SNAP-25, and syntax, depends on the serotype of BTX where each serotype cuts at a different place. The cut SNAREs inhibit the binding of vesicles containing acetylcholine which effectively stops the signaling from nerves to muscle cells, resulting in paralysis <ref name="Lacy" /> | ||
</ref>. | </ref>. | ||
== Disease == | == Disease == | ||
