Peptidyl proly cis/trans isomerases (PPIases) are ubiquitous enzymes of prokaryotes and eukaryotes. They catalytically accelerate the interconversion of the energetically favored cis and trans isomers of prolyl bonds and interact with specific substrate proteins. The superfamily of PPIases comprise FK506-binding proteins (FKBPs), cyclophilins, and parvulins and controls a multitude of processes involved in host-pathogen interactions. Eukaryotic PPIases play key roles in cancer, neurodegeneration, psychiatric disorders, bacterial and viral infections, while bacterial PPIases are involved in metabolism, virulence, and multiple stress responses. Since PPIases control many fundamental properties of their target proteins such as bioactivity, localization or stability, specific inhibitors are regarded to be important therapeutics.
PPIases influence physiological and pathophysiological processes in pathogens, hosts, and their interactions. However, although many bacterial cyclophilins, FKBPs and parvulins have been identified, their natural substrates and specific molecular functions often remain elusive. In humans, eighteen cyclophilin and sixteen FKBP isoenzymes and numerous parvulins including Pin1 have been described and the importance of cyclophilin CypA during HIV and HCV infections is well established. Nevertheless there is a lack of information to what extent and how human PPIases exactly influence cell-cell communication, intracellular signaling, and inflammation in the context of infections. Accordingly, this research topic is thought to provide a forum to present new data on pathogen and host PPIases and their inhibitors.
In this Research Topic, we aim to give an overview on PPIases as such and their contributions to virulence. Moreover, we aim to cover the involvement of host PPIases in infectious processes.
In particular, we seek Original Research articles and up-to-date Reviews that cover the following topics:
1.) General properties of bacterial PPIases, enzymatic activities, regulatory and physiological relevance.
2.) Bacterial PPIases in virulence.
3.) Host PPIases implicated in bacterial, parasitic and viral infections.
4.) Host and bacterial PPIases as drug targets.
Peptidyl proly cis/trans isomerases (PPIases) are ubiquitous enzymes of prokaryotes and eukaryotes. They catalytically accelerate the interconversion of the energetically favored cis and trans isomers of prolyl bonds and interact with specific substrate proteins. The superfamily of PPIases comprise FK506-binding proteins (FKBPs), cyclophilins, and parvulins and controls a multitude of processes involved in host-pathogen interactions. Eukaryotic PPIases play key roles in cancer, neurodegeneration, psychiatric disorders, bacterial and viral infections, while bacterial PPIases are involved in metabolism, virulence, and multiple stress responses. Since PPIases control many fundamental properties of their target proteins such as bioactivity, localization or stability, specific inhibitors are regarded to be important therapeutics.
PPIases influence physiological and pathophysiological processes in pathogens, hosts, and their interactions. However, although many bacterial cyclophilins, FKBPs and parvulins have been identified, their natural substrates and specific molecular functions often remain elusive. In humans, eighteen cyclophilin and sixteen FKBP isoenzymes and numerous parvulins including Pin1 have been described and the importance of cyclophilin CypA during HIV and HCV infections is well established. Nevertheless there is a lack of information to what extent and how human PPIases exactly influence cell-cell communication, intracellular signaling, and inflammation in the context of infections. Accordingly, this research topic is thought to provide a forum to present new data on pathogen and host PPIases and their inhibitors.
In this Research Topic, we aim to give an overview on PPIases as such and their contributions to virulence. Moreover, we aim to cover the involvement of host PPIases in infectious processes.
In particular, we seek Original Research articles and up-to-date Reviews that cover the following topics:
1.) General properties of bacterial PPIases, enzymatic activities, regulatory and physiological relevance.
2.) Bacterial PPIases in virulence.
3.) Host PPIases implicated in bacterial, parasitic and viral infections.
4.) Host and bacterial PPIases as drug targets.
