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首页> 外文期刊>Journal of natural toxins >Hemagglutinin binding mediated protection of botulinum neurotoxin from proteolysis.
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Hemagglutinin binding mediated protection of botulinum neurotoxin from proteolysis.

机译：血凝素结合介导的肉毒杆菌神经毒素免受蛋白水解的保护。

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摘要

Type A Clostridium botulinum, the causative agent of the food poisoning botulism disease, secretes botulinum neurotoxins along with seven neurotoxin associated proteins (NAPs). The function of NAPs has been shown to protect the neurotoxin from acidity, heat, and proteolytic attack in the environmental and gastrointestinal tract during the toxicogenesis of the botulism disease. One of the NAPs, purified from type A botulinum neurotoxin complex, showed hemagglutination activity. A direct interaction has been demonstrated between purified NAP, a 33-kDa hemagglutinin or Hn-33, and the neurotoxin by using Sephadex G-200 column chromatography. Furthermore, Hn-33 has complete resistance against proteolytic attack at pH 2.0 as well as at normal physiological pH. We have investigated digestion of the neurotoxin in the presence and absence of Hn-33. The neurotoxin alone has been found to be more susceptible to the enzymatic digestion than neurotoxin with Hn-33. The presence of Hn-33 changes the proteolytic fragmentation pattern of the neurotoxin. It seems that Hn-33 protects the neurotoxin from proteolysis either by structural modification of the neurotoxin or by blocking the protease accessible sites of the neurotoxin.
机译：食物中毒肉毒中毒的病原体A型肉毒梭菌会分泌肉毒杆菌神经毒素以及7种神经毒素相关蛋白（NAP）。 NAPs的功能已被证明可以在肉毒杆菌中毒的过程中保护神经毒素免受环境，胃肠道中的酸，热和蛋白水解攻击。从A型肉毒杆菌神经毒素复合物中纯化得到的NAP之一显示出血凝活性。通过使用Sephadex G-200柱色谱法，已证明纯化的NAP，33 kDa血凝素或Hn-33与神经毒素之间存在直接的相互作用。此外，Hn-33在pH 2.0和正常生理pH下具有完全的抗蛋白水解攻击能力。我们研究了在Hn-33存在和不存在的情况下神经毒素的消化情况。已经发现单独的神经毒素比具有Hn-33的神经毒素对酶消化更敏感。 Hn-33的存在改变了神经毒素的蛋白水解片段化模式。似乎Hn-33可以通过神经毒素的结构修饰或通过阻断神经毒素的蛋白酶可及位来保护神经毒素免于蛋白水解。

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