Molecular properties of each subcomponent in Clostridium botulinum type B haemagglutinin complex
Molecular properties of each subcomponent in Clostridium botulinum type B haemagglutinin complex
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DOI：
10.1016/j.micpath.2008.04.007
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发表时间：
2008-08-01
影响因子：
3.8
通讯作者：
Oguma, Keiji
中科院分区：
文献类型：
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作者：
Arimitsu, Hideyuki;Sakaguchi, Yoshihiko;Oguma, Keiji
研究了肉毒梭菌血清型B血凝素（HA）的每个亚组分的作用，HA是16 S毒素的一种组分，由4种亚组分（HA 1、2、3a和3 B）组成。为了鉴定有助于神经毒素在胃肠道中稳定性的亚组分，将每种重组HA（rHA）亚组分与胃肠道蛋白酶一起孵育。虽然rHA 1和rHA 3对这些蛋白酶稳定，但特异性切割除外，但rHA 2不稳定。在Western blot和ELISA中，游离抗HA全血清与16S毒素中的rHA 2和HA 2均不反应，而抗rHA 2血清在Western blot中与16S毒素中的rHA 2和HA 2均反应，但在ELISA中与16S毒素不反应。在rHA1和rHA3中发现了对红细胞的结合或血细胞凝集活性，但在rHA2中没有。此外，只有HA1结合到肠部分。这些结果表明，HA（和16S毒素）复合物的组装方式，HA1和HA3（HA3a加HA3b）包住HA2，然后用胰蛋白酶样细菌蛋白酶修饰，导致的结论是，HA1和HA3作为保护因子的神经毒素和作为附着因子的宿主细胞。(c)2008爱思唯尔有限公司保留所有权利。
The role of each subcomponent of Clostridium botulinum serotype B haemagglutinin (HA), which is one component of 16S toxin, and consists of four subcomponents (HA1, 2, 3a, and 3b), was investigated. In order to identify the subcomponent contributing to the stability of a neurotoxin in the gastro-intestinal tract, each recombinant HA (rHA) subcomponent was incubated with gastro-intestinal proteases. Although rHA1 and rHA3 were stable to these proteases except for specific cleavage, rHA2 was not. Anti-free whole HA serum reacted with neither rHA2 nor HA2 in 16S toxin on both Western blot and ELISA, while anti-rHA2 serum reacted with both rHA2 and HA2 in 16S toxin on Western blots, although it did not react with 16S toxin in ELISA. Binding or haemagglutination activity against erythrocytes was found in rHA1 and rHA3, but not in rHA2. In addition, only HA1 bound to the intestinal section. These results indicate that the HA (and 16S toxin) complex is assembled in the way that HA1 and HA3 (HA3a plus HA3b) encase HA2, followed by modification with trypsin-like bacterial protease, leading to the conclusion that HA1 and HA3 act as protective factors for the neurotoxin and as attachment factors to host cells. (c) 2008 Elsevier Ltd. All rights reserved.