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dc.contributor.authorÜnal, Can Murat
dc.contributor.authorSteinert, Michael
dc.date.accessioned2021-01-08T21:51:29Z
dc.date.available2021-01-08T21:51:29Z
dc.date.issued2014
dc.identifier.issn1092-2172
dc.identifier.issn1098-5557
dc.identifier.urihttp://doi.org/10.1128/MMBR.00015-14
dc.identifier.urihttps://hdl.handle.net/20.500.12846/301
dc.descriptionUnal, Can/0000-0003-4710-9567en_US
dc.descriptionWOS:000341639400008en_US
dc.descriptionPubMed: 25184565en_US
dc.description.abstractInitially discovered in the context of immunomodulation, peptidyl-prolyl cis/trans isomerases (PPIases) were soon identified as enzymes catalyzing the rate-limiting protein folding step at peptidyl bonds preceding proline residues. Intense searches revealed that PPIases are a superfamily of proteins consisting of three structurally distinguishable families with representatives in every described species of prokaryote and eukaryote and, recently, even in some giant viruses. Despite the clear-cut enzymatic activity and ubiquitous distribution of PPIases, reports on solely PPIase-dependent biological roles remain scarce. Nevertheless, they have been found to be involved in a plethora of biological processes, such as gene expression, signal transduction, protein secretion, development, and tissue regeneration, underscoring their general importance. Hence, it is not surprising that PPIases have also been identified as virulence-associated proteins. The extent of contribution to virulence is highly variable and dependent on the pleiotropic roles of a single PPIase in the respective pathogen. The main objective of this review is to discuss this variety in virulence-related bacterial and protozoan PPIases as well as the involvement of host PPIases in infectious processes. Moreover, a special focus is given to Legionella pneumophila macrophage infectivity potentiator (Mip) and Mip-like PPIases of other pathogens, as the best-characterized virulence-related representatives of this family. Finally, the potential of PPIases as alternative drug targets and first tangible results are highlighted.en_US
dc.description.sponsorshipTUBITAKTurkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) [2219]; State of Lower Saxony, Niedersachsisches Vorab [VWZN2889]; DFGGerman Research Foundation (DFG) [STE838/8-1]en_US
dc.description.sponsorshipCan M. Unal is supported by a 2219 (2012/2 term) grant from TUBITAK and the State of Lower Saxony, Niedersachsisches Vorab (grant VWZN2889), within the joint research project "Epidemiology and systems biology of the bacterial pathogen Clostridium difficile (CDiff)." Michael Steinert is funded by DFG grant STE838/8-1.en_US
dc.language.isoengen_US
dc.publisherAmer Soc Microbiologyen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.titleMicrobial peptidyl-prolyl cis/trans isomerases (ppIases): virulence factors and potential alternative drug targetsen_US
dc.typeReviewen_US
dc.relation.journalMicrobiology And Molecular Biology Reviewsen_US
dc.identifier.volume78en_US
dc.identifier.issue3en_US
dc.relation.publicationcategoryotheren_US
dc.contributor.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.contributor.institutionauthorÜnal, Can Murat
dc.identifier.doi10.1128/MMBR.00015-14
dc.identifier.startpage544en_US
dc.identifier.endpage571en_US


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