Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis
Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis
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DOI：
10.1016/j.febslet.2008.12.028
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发表时间：
2009-01-22
期刊：
影响因子：
3.5
通讯作者：
Bhakdi, Sucharit
中科院分区：
文献类型：
--
作者：
Husmann, Matthias;Beckmann, Erik;Bhakdi, Sucharit
金黄色葡萄球菌α毒素是细菌成孔毒素的原型，是大多数临床分离的金黄色葡萄球菌分泌的关键毒力因子。金黄色。毒素单体与靶细胞结合并寡聚化以在质膜中形成小的β-桶孔。许多有核细胞能够通过未知的非钙依赖性机制修复有限数量的病变。在这里，我们表明，细胞可以内化α-毒素，摄取是细胞生存所必需的，并且孔复合物不被蛋白水解降解，而是在外泌体样结构的背景下返回到细胞外环境，我们称之为毒体。(C)2008年欧洲生物化学学会联合会。由Elsevier B出版。V.保留所有权利。
Staphylococcus aureus alpha-toxin is the archetype of bacterial pore forming toxins and a key virulence factor secreted by the majority of clinical isolates of S. aureus. Toxin monomers bind to target cells and oligomerize to form small beta-barrel pores in the plasma membrane. Many nucleated cells are able to repair a limited number of lesions by unknown, calcium-independent mechanisms. Here we show that cells can internalize alpha-toxin, that uptake is essential for cellular survival, and that pore-complexes are not proteolytically degraded, but returned to the extracellular milieu in the context of exosome-like structures, which we term toxosomes. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.