Ünal, Can MuratSteinert, Michael2021-01-082021-01-0820150304-41651872-8006http://doi.org/10.1016/j.bbagen.2014.12.018https://hdl.handle.net/20.500.12846/285Unal, Can/0000-0003-4710-9567WOS:000361263700015PubMed: 25529296Background: FK506-binding proteins (FKBPs) contain a domain with peptidyl-prolyl-cis/trans-isomerase (PPlase) activity and bind the immunosuppressive drugs FK506 and rapamycin. FKBPs belong to the immunophilin family and are found in eukaryotes and bacteria. Scope of review: 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. Major conclusions: 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. General significance: 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. (C) 2014 Elsevier B.V. All rights reserved.eninfo:eu-repo/semantics/closedAccessFk506-Binding ProteinMacrophage Infectivity Potentiator (Mip)BacteriaPathogenInfectionDrug TargetReview Article18501010.1016/j.bbagen.2014.12.01820962102Q1Q1WOS:0003612637000152-s2.0-84940597104