Basit öğe kaydını göster

dc.contributor.authorÜnal, Can Murat
dc.contributor.authorBerges, Mareike
dc.contributor.authorSmit, Nathiana
dc.contributor.authorSchiene-Fischer, Cordelia
dc.contributor.authorPriebe, Christina
dc.contributor.authorStrowig, Till
dc.contributor.authorSteinert, Michael
dc.date.accessioned2021-01-08T21:51:23Z
dc.date.available2021-01-08T21:51:23Z
dc.date.issued2018
dc.identifier.issn1664-302X
dc.identifier.urihttp://doi.org/10.3389/fmicb.2018.02913
dc.identifier.urihttps://hdl.handle.net/20.500.12846/213
dc.descriptionUnal, Can/0000-0003-4710-9567en_US
dc.descriptionWOS:000452028000001en_US
dc.descriptionPubMed: 30564207en_US
dc.description.abstractClostridioides difficile is the main cause for nosocomial antibiotic associated diarrhea and has become a major burden for the health care systems of industrial countries. Its main virulence factors, the small GTPase glycosylating toxins TcdA and TcdB, are extensively studied. In contrast, the contribution of other factors to development and progression of C. difficile infection (CDI) are only insufficiently understood. Many bacterial peptidyl-prolyl-cis/trans-isomerases (PPlases) have been described in the context of virulence. Among them are the parvulin-type PrsA-like PPlases of Gram-positive bacteria. On this basis, we identified CD630_35000 as the PrsA2 homolog in C. difficile and conducted its enzymatic and phenotypic characterization in order to assess its involvement during C. difficile infection. For this purpose, wild type CdPrsA2 and mutant variants carrying amino acid exchanges mainly in the PPlase domain were recombinantly produced. Recombinant CdPrsA2 showed PPlase activity toward the substrate peptide Ala-Xaa-Pro-Phe with a preference for positively charged amino acids preceding the proline residue. Mutation of conserved residues in its active site pocket impaired the enzymatic activity. A PrsA2 deficient mutant was generated in the C. difficile 6300erm background using the ClosTron technology. Inactivation of prsA2 resulted in a reduced germination rate in response to taurocholic acid, and in a slight increase in resistance to the secondary bile acids LCA and DCA. Interestingly, in the absence of PrsA2 colonization of mice by C. difficile 630 was significantly reduced. We concluded that CdPrsA2 is an active PPlase that acts as a virulence modulator by influencing crucial processes like sporulation, germination and bile acid resistance resulting in attenuated mice colonization.en_US
dc.description.sponsorshipFederal State of Lower Saxony, Niedersachsisches Vorab [VWZN2889]; Max Planck SocietyMax Planck Societyen_US
dc.description.sponsorshipThis work was supported by the Federal State of Lower Saxony, Niedersachsisches Vorab (VWZN2889) and by the Max Planck Society.en_US
dc.language.isoengen_US
dc.publisherFrontiers Media Saen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectClostridioides Difficileen_US
dc.subjectPrsa2en_US
dc.subjectPeptidyl-Prolyl-Cis/Trans-Isomeraseen_US
dc.subjectResistanceen_US
dc.subjectGerminationen_US
dc.subjectColonizationen_US
dc.titlePrsA2 (CD630_35000) of clostridioides difficile Is an Active Parvulin-Type PPlase and a virulence modulatoren_US
dc.typearticleen_US
dc.relation.journalFrontiers In Microbiologyen_US
dc.identifier.volume9en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.contributor.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.contributor.institutionauthorÜnal, Can Murat
dc.identifier.doi10.3389/fmicb.2018.02913
dc.identifier.wosqualityQ1en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.wosWOS:000452028000001en_US


Bu öğenin dosyaları:

Thumbnail

Bu öğe aşağıdaki koleksiyon(lar)da görünmektedir.

Basit öğe kaydını göster