Department of Biosciences & Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India.
Faculty of Pharmacy, Bank Building, Science Road, The University of Sydney, Sydney NSW 2006, Australia.
Future Med Chem. 2016 Jun;8(10):1111-32. doi: 10.4155/fmc-2016-0041. Epub 2016 Jun 10.
Filamenting temperature-sensitive mutant Z (FtsZ), an essential cell division protein in bacteria, has recently emerged as an important and exploitable antibacterial target. Cytokinesis in bacteria is regulated by the assembly dynamics of this protein, which is ubiquitously present in eubacteria. The perturbation of FtsZ assembly has been found to have a deleterious effect on the cytokinetic machinery and, in turn, upon cell survival. FtsZ is highly conserved among prokaryotes, offering the possibility of broad-spectrum antibacterial agents, while its limited sequence homology with tubulin (an essential protein in eukaryotic mitosis) offers the possibility of selective toxicity. This review aims to summarize current knowledge regarding the mechanism of action of FtsZ, and to highlight existing attempts toward the development of clinically useful inhibitors.
丝状温度敏感突变 Z（FtsZ）是细菌中一种必需的细胞分裂蛋白，最近它作为一个重要的、可开发的抗菌靶点而受到关注。细菌的细胞分裂受该蛋白的组装动力学调控，而该蛋白在真细菌中普遍存在。研究发现，FtsZ 组装的扰动会对细胞分裂机制产生有害影响，进而影响细胞存活。FtsZ 在原核生物中高度保守，这为开发广谱抗菌剂提供了可能，而其与微管蛋白（真核有丝分裂中的必需蛋白）的有限序列同源性为选择性毒性提供了可能。本综述旨在总结 FtsZ 的作用机制的现有知识，并强调目前开发临床有用抑制剂的尝试。
