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C-Terminal Domain of Bacillus cereus Hemolysin II Is Able to Interact with Erythrocytes
Russian Journal of Bioorganic Chemistry ( IF 1 ) Pub Date : 2020-05-01 , DOI: 10.1134/s1068162020030188
N. V. Rudenko , A. P. Karatovskaya , A. V. Zamyatina , A. V. Siunov , Zh. I. Andreeva-Kovalevskaya , A. S. Nagel , F. A. Brovko , A. S. Solonin

Hemolysin II (HlyII) is one of the pathogenic factors of Bacillus cereus. With respect to the prototype of β-barrel toxins, the α-toxin of S. aureus, this pore-forming protein has a C-terminal domain (CTD) of 94 amino acids. The role of CTD in membrane pore formation and cell lysis is not clear, although removal of this portion of the protein is known to significantly reduce hemolytic activity. A representative panel of monoclonal antibodies against recombinant CTD recognizing full-length HlyII was obtained. Using the obtained monoclonal antibodies, CTD was shown to bind to rabbit red blood cells.

中文翻译:

蜡样芽孢杆菌溶血素 II 的 C 端结构域能够与红细胞相互作用

溶血素II(HlyII)是蜡样芽孢杆菌的致病因子之一。关于 β-桶毒素的原型,金黄色葡萄球菌的 α-毒素,这种成孔蛋白具有 94 个氨基酸的 C 端结构域 (CTD)。CTD 在膜孔形成和细胞裂解中的作用尚不清楚,尽管已知去除这部分蛋白质会显着降低溶血活性。获得了一组具有代表性的抗重组 CTD 识别全长 HlyII 的单克隆抗体。使用获得的单克隆抗体,CTD 显示与兔红细胞结合。
更新日期:2020-05-01
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