Structure and biological activity of botulinum neurotoxin.

Journal de physiologie Pub Date : 1990-01-01
B R DasGupta
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Abstract

Botulinum neurotoxin appears to undergo structural alterations after synthesis and also before it inhibits neurotransmitter release. Discussions and conjectures are presented in this context: 1. At what sites on the 150 kDa neurotoxin does posttranslational proteolytic processing occur? 2. Does neurotransmitter inhibition depend on separation of a segment of the neurotoxin from the rest of the molecule? 3. At what step in the intoxication pathway does activation of neurotoxin (enhanced lethality following limited proteolysis) manifest? 4. Can the receptor binding parameters (based on bovine brain synaptosome and lipid membrane), channel forming property (lipid bilayer membrane) and intracellular inhibitory activity (based on permeabilized chromaffin and PC 12 cells) provide clues to differences in the lethal potency between the neurotoxin serotypes? In addition, the following issues are considered: 5. The spontaneous fragmentation of isolated 50 kDa light chain, after its separation from 100 kDa heavy chain, 6. Effect of specific chemical modification of Arg, His, Lys, Trp, Tyr and Asp/Glu residues of types A, B and E neurotoxins on lethality and antigenicity, and 7. Development of second generation toxoids.

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肉毒杆菌神经毒素的结构与生物活性。
肉毒杆菌神经毒素似乎在合成后和抑制神经递质释放之前经历结构改变。在此背景下提出了讨论和猜想:1。150 kDa神经毒素的翻译后蛋白水解发生在哪些位点?2. 神经递质抑制是否依赖于神经毒素的一部分与分子的其余部分分离?3.在中毒途径的哪一步,神经毒素的激活(有限蛋白水解后的致命性增强)表现出来?4. 受体结合参数(基于牛脑突触体和脂质膜)、通道形成特性(脂质双层膜)和细胞内抑制活性(基于渗透化染色质和pc12细胞)能否为神经毒素血清型之间的致死效力差异提供线索?此外,还审议了下列问题:分离的50 kDa轻链与100 kDa重链分离后的自发断裂,6。6 . A、B、E型神经毒素Arg、His、Lys、Trp、Tyr和Asp/Glu残基特异性化学修饰对致死性和抗原性的影响;第二代类毒素的发展。
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