Mega assemblages of oligomeric aerolysin-like toxins stabilized by toxin-associating membrane proteins.
Mega assemblages of oligomeric aerolysin-like toxins stabilized by toxin-associating membrane proteins.
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由毒素相关膜蛋白稳定的寡聚气溶素样毒素的巨型组合。
DOI：
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
S. Kitada
中科院分区：
文献类型：
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作者：
H. Shimada;S. Kitada
大多数β致孔毒素需要通过受体寡聚才能形成膜孔。尽管寡聚毒素经常形成耐十二烷基硫酸钠的寡聚体，但耐十二烷基硫酸钠的寡聚体是否反映了天然的功能毒素复合体是值得怀疑的。为了阐明细胞杀灭组合的本质，对溶气素样毒素的寡聚体、溶气素、副孢子素-2和埃西隆毒素进行了检测。在Blue Native PAGE上，用温和的去污剂从靶细胞中溶解的每一种毒素都是一个比典型的耐十二烷基硫酸钠的寡聚体(∼200 kDa)大得多的复合体(近1mda)。大小排斥层析证实了巨型毒素复合体的存在。虽然部分巨大的复合体对蛋白酶敏感，但耐十二烷基硫酸钠的低聚物阻止了蛋白质的降解。据推测，核心毒素复合体保持完好，而细胞蛋白被降解。此外，在较低的温度下可以检测到中间络合物，其中不包括耐十二烷基硫酸钠的低聚物。这项研究为β致孔毒素的巨大功能复合体提供了证据，并强调了它们在组成上的潜在差异。
Most β pore-forming toxins need to be oligomerized via receptors in order to form membrane pores. Though oligomerizing toxins frequently form SDS-resistant oligomers, it was questionable whether SDS-resistant oligomers reflected native functional toxin complexes. In order to elucidate the essence of the cytocidal assemblages, oligomers of aerolysin-like toxins, aerolysin, parasporin-2 and epsilon toxin, were examined with or without SDS. On Blue Native PAGE, each toxin, which had been solubilized from target cells with mild detergent, was a much larger complex (nearly 1 MDa) than the typical SDS-resistant oligomers (∼200 kDa). Size exclusion chromatography confirmed the huge toxin complexes. While a portion of the huge complexes were sensitive to proteases, SDS-resistant oligomers resist the proteolysis. Presumably the core toxin complexes remained intact while the cellular proteins were degraded. Moreover, intermediate complexes, which included no SDS-resistant oligomers, could be detected at lower temperatures. This study provides evidence for huge functional complexes of β pore-forming toxins and emphasizes their potential variance in composition.
影响因子：
2.9
作者：
Miller, CJ;Elliott, JL;Collier, RJ
通讯作者：
Collier, RJ
影响因子：
56.9
作者：
DiFiglia, M;Sapp, E;Aronin, N
通讯作者：
Aronin, N