Johnson Steven, Deane Janet E, Lea Susan M
Laboratory of Molecular Biophysics, Department of Biochemistry, South Parks Road, Oxford OX1 3QU, UK.
Curr Opin Struct Biol. 2005 Dec;15(6):700-7. doi: 10.1016/j.sbi.2005.10.007. Epub 2005 Nov 2.
Many Gram-negative pathogens translocate virulence proteins directly into host cells using a type III secretion system. This complex secretion machinery is composed of approximately 25 different proteins that assemble to span both bacterial membranes, and contact the host cell to form a direct channel between the bacterial and host cell cytoplasms. Assembly of the system and efficient secretion of virulence proteins through this apparatus require specific chaperones. Although the machinery is morphologically conserved among all bacteria, the secreted proteins vary widely and are responsible for the range of diseases caused by bacterial pathogens. Recent structures have given insights into important chaperone and effector proteins, as well as revealing the first atomic structures of portions of the secretion machinery itself.
许多革兰氏阴性病原体利用III型分泌系统将毒力蛋白直接转运到宿主细胞中。这种复杂的分泌机制由大约25种不同的蛋白质组成，这些蛋白质组装起来跨越细菌的两层膜，并与宿主细胞接触，在细菌和宿主细胞的细胞质之间形成一条直接通道。该系统的组装以及通过该装置有效分泌毒力蛋白需要特定的分子伴侣。尽管该机制在所有细菌中形态上是保守的，但分泌的蛋白质差异很大，并且是导致细菌病原体引发各种疾病的原因。最近的结构研究深入了解了重要的分子伴侣和效应蛋白，同时也揭示了分泌机制本身部分结构的首个原子结构。
