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首页> 外文期刊>Infection and immunity >The C-terminal domain is essential for protective activity of the Bordetella pertussis adenylate cyclase-hemolysin.
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The C-terminal domain is essential for protective activity of the Bordetella pertussis adenylate cyclase-hemolysin.

机译：C末端结构域对于百日咳博德特氏菌腺苷酸环化酶-溶血素的保护活性是必不可少的。

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摘要

The adenylate cyclase-hemolysin of Bordetella pertussis consists of a cell-invasive N-terminal adenylate cyclase domain linked to a C-terminal RTX hemolysin containing extensive glycine-rich repeats. The toxin is an essential virulence factor required in the initial stages of infection. Adenylate cyclase-hemolysin was also shown to be a potent vaccinating antigen inducing protection against B. pertussis colonization of the mouse respiratory tract. This protective activity depends on a posttranslational fatty-acylation modification. We used a set of deletion derivatives of the recombinant adenylate cyclase-hemolysin to localize the protective epitopes on the 1,706-residue toxin. We show that specific anti-adenylate cyclase-hemolysin antibodies present in the sera of B. pertussis-infected mice and humans are directed predominantly against the modification-and-repeat portion of the toxin, contained in the last 800 residues of the adenylate cyclase-hemolysin. These antibodies appear to recognize conformational epitopes present only in a structure formed by the intact C-terminal half of the toxin. There was no correlation between the capacity of the truncated adenylate cyclase-hemolysin derivatives to induce both toxin-neutralizing antibodies upon immunization of mice and protective immunity. However, only the truncated proteins which were recognized by the sera of infected mice and humans and which had their last 800 residues intact had the capacity to induce protection of mice against colonization by B. pertussis. This indicates that the structure of the modification-and-repeat region of adenylate cyclase-hemolysin is critical for its protective activity.
机译：百日咳博德特氏菌的腺苷酸环化酶溶血素由细胞侵入性N末端腺苷酸环化酶结构域与C端RTX溶血素相连，后者含有大量富含甘氨酸的重复序列。毒素是感染初期所需的必需毒力因子。还显示出腺苷酸环化酶-溶血素是一种有效的疫苗抗原，可诱导针对百日咳博德特氏菌定殖的小鼠呼吸道保护作用。这种保护活性取决于翻译后脂肪酰化修饰。我们使用了一组重组腺苷酸环化酶-溶血素的缺失衍生物来定位保护性表位在1,706-残基毒素上。我们显示存在于百日咳博德特氏菌感染的小鼠和人类血清中的特异性抗腺苷酸环化酶溶血素抗体主要针对毒素的修饰和重复部分，该部分包含在腺苷酸环化酶的最后800个残基中。溶血素。这些抗体似乎识别仅在毒素的完整C末端一半形成的结构中存在的构象表位。小鼠免疫后，截短的腺苷酸环化酶-溶血素衍生物诱导毒素中和抗体的能力与保护性免疫之间没有相关性。但是，只有被感染的小鼠和人类的血清识别的并且截短了最后800个残基的截短的蛋白质才具有诱导保护小鼠免受百日咳博德特氏菌定殖的能力。这表明腺苷酸环化酶-溶血素的修饰和重复区的结构对其保护活性至关重要。

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