Department of Microbiology and Immunobiology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Science. 2012 Aug 17;337(6096):815. doi: 10.1126/science.1222901. Epub 2012 Jul 5.
The bacterial type 6 secretion system (T6SS) functions as a virulence factor capable of attacking both eukaryotic and prokaryotic target cells by a process that involves protein transport through a contractile bacteriophage tail-like structure. The T6SS apparatus is composed, in part, of an exterior sheath wrapped around an interior tube. Here, we report that in living cells the cytoplasmic adenosine triphosphatase called ClpV specifically recognizes the contracted T6SS sheath structure, causing its disassembly within seconds. ClpV imaging allowed spatial and temporal documentation of cell-cell interactions (termed T6SS dueling) that likely mark the location of repeated T6SS-mediated protein translocation events between bacterial cells.
细菌的 6 型分泌系统(T6SS)是一种毒力因子,能够通过一个涉及通过收缩噬菌体尾状结构进行蛋白质运输的过程攻击真核和原核靶细胞。T6SS 装置部分由包裹在内管周围的外部鞘组成。在这里,我们报告说,在活细胞中,称为 ClpV 的细胞质三磷酸腺苷酶特异性识别收缩的 T6SS 鞘结构,导致其在几秒钟内解体。ClpV 成像允许对细胞-细胞相互作用(称为 T6SS 决斗)进行空间和时间记录,这可能标志着细菌细胞之间重复的 T6SS 介导的蛋白质转运事件的位置。