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dc.contributor.authorMeissner, Andree
dc.contributor.authorWild, Verena
dc.contributor.authorSimm, Roger
dc.contributor.authorRohde, Manfred
dc.contributor.authorErck, Christian
dc.contributor.authorBredenbruch, Florian
dc.contributor.authorMorr, Michael
dc.contributor.authorRömling, Ute
dc.contributor.authorHäussler, Susanne
dc.date.accessioned2008-05-22T12:45:59Z
dc.date.available2008-05-22T12:45:59Z
dc.date.issued2007-10
dc.identifier.citationPseudomonas aeruginosa cupA-encoded fimbriae expression is regulated by a GGDEF and EAL domain-dependent modulation of the intracellular level of cyclic diguanylate. 2007, 9 (10):2475-85 Environ. Microbiol.en
dc.identifier.issn1462-2912
dc.identifier.pmid17803773
dc.identifier.doi10.1111/j.1462-2920.2007.01366.x
dc.identifier.urihttp://hdl.handle.net/10033/27612
dc.description.abstractCyclic-diguanylate (c-di-GMP) is a widespread bacterial signal molecule that plays a major role in the modulation of cellular surface components, such as exopolysaccharides and fimbriae, and in the establishment of a sessile life style. Here, we report that intracellular c-di-GMP levels influence cupA-encoded fimbriae expression in Pseudomonas aeruginosa. In an autoaggregative P. aeruginosa small colony variant (SCV) CupA fimbriae and the intracellular c-di-GMP concentration were found to be enhanced as compared with the clonal wild-type. The SCV morphology and the expression of CupA fimbriae were dependent on a functional PA1120 and morA gene both encoding a GGDEF domain. Overexpression of the GGDEF domain protein PA1120 complemented the PA1120 and the morA mutant with respect to CupA fimbriae expression. In agreement with these findings, overexpression of the EAL domain containing phenotypic variance regulator (PvrR) in the SCV resulted in a decreased intracellular level of c-di-GMP, a reduced cupA fimbriae expression and a switch to wild-type colony morphology.
dc.language.isoenen
dc.subject.meshCyclic GMPen
dc.subject.meshFimbriae Proteinsen
dc.subject.meshFimbriae, Bacterialen
dc.subject.meshHumansen
dc.subject.meshPhenotypeen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshPseudomonas aeruginosaen
dc.titlePseudomonas aeruginosa cupA-encoded fimbriae expression is regulated by a GGDEF and EAL domain-dependent modulation of the intracellular level of cyclic diguanylate.en
dc.typeArticleen
dc.contributor.departmentDivision of Cell Biology and Immunology, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany.en
dc.identifier.journalEnvironmental microbiologyen
refterms.dateFOA2008-10-05T00:00:00Z
html.description.abstractCyclic-diguanylate (c-di-GMP) is a widespread bacterial signal molecule that plays a major role in the modulation of cellular surface components, such as exopolysaccharides and fimbriae, and in the establishment of a sessile life style. Here, we report that intracellular c-di-GMP levels influence cupA-encoded fimbriae expression in Pseudomonas aeruginosa. In an autoaggregative P. aeruginosa small colony variant (SCV) CupA fimbriae and the intracellular c-di-GMP concentration were found to be enhanced as compared with the clonal wild-type. The SCV morphology and the expression of CupA fimbriae were dependent on a functional PA1120 and morA gene both encoding a GGDEF domain. Overexpression of the GGDEF domain protein PA1120 complemented the PA1120 and the morA mutant with respect to CupA fimbriae expression. In agreement with these findings, overexpression of the EAL domain containing phenotypic variance regulator (PvrR) in the SCV resulted in a decreased intracellular level of c-di-GMP, a reduced cupA fimbriae expression and a switch to wild-type colony morphology.


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