Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells
Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells
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DOI：
10.1073/pnas.071065798
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发表时间：
2001-04-10
影响因子：
11.1
通讯作者：
Blobel, G
中科院分区：
文献类型：
--
作者：
Hoiczyk, E;Blobel, G
许多致病性的革兰氏阴性细菌能够在三种膜上分泌特定的蛋白质：细菌内外膜和真核质膜。在小肠结肠炎耶尔森菌中，分泌蛋白的初级结构以及分泌机制的组成部分，两者都是质粒编码的，是已知的。然而，蛋白质易位的机制在很大程度上是未知的。在这里，我们发现小肠结肠炎杆菌将分泌机制的6 kda蛋白聚合成能够刺穿真核生物质膜的针。这些针形成了一个管道，用于将特定蛋白质从细菌运输到真核细胞质，在那里它们发挥细胞毒性活性。在阴性染色电镜下，分离的针长60-80 nm，宽6-7 nm，中心中空约2 nm。我们的数据表明，正是6-kDa蛋白聚合成这些针，提供了穿透真核质膜的力量。
A number of pathogenic, Cram-negative bacteria are able to secrete specific proteins across three membranes: the inner and outer bacterial membrane and the eukaryotic plasma membrane. In the pathogen Yersinia enterocolitica, the primary structure of the secreted proteins as well as of the components of the secretion machinery, both plasmid-encoded, is known. However, the mechanism of protein translocation is largely unknown. Here we show that Y. enterocolitica polymerizes a 6-kDa protein of the secretion machinery into needles that are able to puncture the eukaryotic plasma membrane. These needles form a conduit for the transport of specific proteins from the bacterial to the eukaryotic cytoplasm, where they exert their cytotoxic activity. In negatively stained electron micrographs, the isolated needles were 60-80 nm long and 6-7 nm wide and contained a hollow center of about 2 nm. Our data indicate that it is the polymerization of the 6-kDa protein into these needles that provides the force to perforate the eukaryotic plasma membrane.