Botulinum Hemagglutinin: Critical Protein for Adhesion and Absorption of Neurotoxin Complex in Host Intestine
Botulinum Hemagglutinin: Critical Protein for Adhesion and Absorption of Neurotoxin Complex in Host Intestine
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DOI：
10.1007/978-1-0716-0430-4_19
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发表时间：
2020-01-01
期刊：
影响因子：
--
通讯作者：
Fujinaga, Yukako
中科院分区：
文献类型：
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作者：
Amatsu, Sho;Fujinaga, Yukako
肉毒杆菌血凝素（HA）是肉毒杆菌神经毒素（BoNT）复合物的辅助蛋白组分之一，是已知最致命的毒素。HA通过至少两种机制促进BoNT的肠吸收，导致高口服毒性。其机制之一是HA的碳水化合物结合活性使大前体毒素复合物（L-PTC）附着于肠上皮细胞表面。另一种是HA的E-钙粘蛋白结合活性破坏上皮屏障。HA的碳水化合物结合活性还促进附着于基底外侧细胞表面，这增加了HA和E-钙粘蛋白之间的接触频率。总之，HA的碳水化合物结合活性对于BoNT的肠吸收至关重要。HA的三聚体三骨架状结构赋予其与配体的多价结合并增加HA的致病生物活性。
Botulinum hemagglutinin (HA) is one of the auxiliary protein components of the botulinum neurotoxin (BoNT) complex, the most lethal toxin known. HA promotes the intestinal absorption of BoNT by at least two mechanisms, resulting in high oral toxicity. One of the mechanisms is the attachment of large progenitor toxin complexes (L-PTCs) to the cell surface of the intestinal epithelium by the carbohydratebinding activity of HA. The other is epithelial barrier disruption by the E-cadherin-binding activity of HA. The carbohydrate-binding activity of HA also promotes attachment to the basolateral cell surface, which increases the frequency of contact between HA and E-cadherin. Together, the carbohydrate-binding activity of HA is critical for the intestinal absorption of BoNTs. The trimeric triskelion-shaped structure of HA confers the multivalent binding to its ligands and increases the pathogenic biological activities of HA.