Ünal Can M, Steinert Michael
Türk-Alman Üniversitesi, Fen Fakültesi, Istanbul, Turkey; Technische Universität Braunschweig, Institut für Mikrobiologie, Braunschweig, Germany.
Technische Universität Braunschweig, Institut für Mikrobiologie, Braunschweig, Germany; Helmholtz Centre for Infection Research, Braunschweig, Germany.
Biochim Biophys Acta. 2015 Oct;1850(10):2096-102. doi: 10.1016/j.bbagen.2014.12.018. Epub 2014 Dec 19.
FK506-binding proteins (FKBPs) contain a domain with peptidyl-prolyl-cis/trans-isomerase (PPIase) activity and bind the immunosuppressive drugs FK506 and rapamycin. FKBPs belong to the immunophilin family and are found in eukaryotes and bacteria.
In this review we describe two major groups of bacterial virulence-associated FKBPs, the trigger factor and Mip-like PPIases. Moreover, we discuss the contribution of host FKBPs in bacterial infection processes.
Since PPIases are regarded as alternative antiinfective drug targets we highlight current research strategies utilizing pipecolinic acid and cycloheximide derivatives as well as substrate based inhibitors.
The current research strategies suggest a beneficial synergism of drug development and basic research. This article is part of a Special Issue entitled Proline-directed Foldases: Cell Signaling Catalysts and Drug Targets.
FK506结合蛋白（FKBPs）含有一个具有肽基脯氨酰顺/反异构酶（PPIase）活性的结构域，并能结合免疫抑制药物FK506和雷帕霉素。FKBPs属于亲免素家族，存在于真核生物和细菌中。
在本综述中，我们描述了两大类与细菌毒力相关的FKBPs，触发因子和Mip样PPIases。此外，我们还讨论了宿主FKBPs在细菌感染过程中的作用。
由于PPIases被视为替代抗感染药物靶点，我们重点介绍了目前利用哌啶酸和环己酰亚胺衍生物以及基于底物的抑制剂的研究策略。
目前的研究策略表明药物开发与基础研究具有有益的协同作用。本文是名为“脯氨酸导向的折叠酶：细胞信号催化剂和药物靶点”的特刊的一部分。
