Peptidylprolyl cis-trans isomerases of Legionella pneumophila: virulence, moonlighting and novel therapeutic targets

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dc.contributor.authorRasch, Janine
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.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.descriptionUnal, Can/0000-0003-4710-9567en_US
dc.descriptionWOS:000345427100041en_US
dc.descriptionPubMed: 25399597en_US
dc.description.abstractLegionella pneumophila, typically a parasite of free-living protozoa, can also replicate in human alveolar macrophages and lung epithelial cells causing Legionnaires' disease in humans, a severe atypical pneumonia. The pathogen encodes six peptidylprolyl cis-trans isomerases (PPIases), which generally accelerate folding of prolyl peptide bonds, and influence protein folding. PPIases can be divided into three classes, cyclophilins, parvulins and FK506-binding proteins (FKBPs). They contribute to a multitude of cellular functions including bacterial virulence. In the present review, we provide an overview of L. pneumophila PPIases, discussing their known and anticipated functions as well as moonlighting phenomena. By taking the example of the macrophage infectivity potentiator (Mip) of L. pneumophila, we highlight the potential of PPIases as promising drug targets.
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG)German Research Foundation (DFG) [STE 838/8-1]
dc.description.sponsorshipThis work received financial support from the Deutsche Forschungsgemeinschaft (DFG) [grant number STE 838/8-1].
dc.identifier.doi10.1042/BST20140202
dc.identifier.endpage1733en_US
dc.identifier.issn0300-5127
dc.identifier.issn1470-8752
dc.identifier.scopus2-s2.0-84911923740
dc.identifier.scopusqualityQ1
dc.identifier.startpage1728en_US
dc.identifier.urihttp://doi.org/10.1042/BST20140202
dc.identifier.urihttps://hdl.handle.net/20.500.12846/299
dc.identifier.volume42en_US
dc.identifier.wosWOS:000345427100041
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorÜnal, Can Murat
dc.language.isoen
dc.publisherPortland Press Ltd
dc.relation.ispartofBiochemical Society Transactions
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectCyclophilinen_US
dc.subjectFk506-Binding Proteinen_US
dc.subjectLegionella Pneumophilaen_US
dc.subjectMoonlightingen_US
dc.subjectParvulinen_US
dc.subjectPpiaseen_US
dc.titlePeptidylprolyl cis-trans isomerases of Legionella pneumophila: virulence, moonlighting and novel therapeutic targets
dc.typeArticle

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