Please use this identifier to cite or link to this item: https://oar.tib.eu/jspui/handle/123456789/3687
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dc.rights.licenseCC BY 4.0 Unportedger
dc.contributor.authorThein, Marcus
dc.contributor.authorBonde, Mari
dc.contributor.authorBunikis, Ignas
dc.contributor.authorDenker, Katrin
dc.contributor.authorSickmann, Albert
dc.contributor.authorBergström, Sven
dc.contributor.authorBenz, Roland
dc.date.accessioned2018-02-20T22:04:50Z
dc.date.available2019-06-28T08:33:10Z
dc.date.issued2012
dc.identifier.urihttps://oar.tib.eu/jspui/handle/123456789/3687
dc.identifier.urihttp://dx.doi.org/10.34657/1726-
dc.description.abstractLyme disease Borreliae are highly dependent on the uptake of nutrients provided by their hosts. Our study describes the identification of a 36 kDa protein that functions as putative dicarboxylate-specific porin in the outer membrane of Lyme disease Borrelia. The protein was purified by hydroxyapatite chromatography from Borrelia burgdorferi B31 and designated as DipA, for dicarboxylate-specific porin A. DipA was partially sequenced, and corresponding genes were identified in the genomes of B. burgdorferi B31, Borrelia garinii PBi and Borrelia afzelii PKo. DipA exhibits high homology to the Oms38 porins of relapsing fever Borreliae. B. burgdorferi DipA was characterized using the black lipid bilayer assay. The protein has a singlechannel conductance of 50 pS in 1 M KCl, is slightly selective for anions with a permeability ratio for cations over anions of 0.57 in KCl and is not voltage-dependent. The channel could be partly blocked by different di- and tricarboxylic anions. Particular high stability constants up to about 28,000 l/mol (in 0.1 M KCl) were obtained among the 11 tested anions for oxaloacetate, 2-oxoglutarate and citrate. The results imply that DipA forms a porin specific for dicarboxylates which may play an important role for the uptake of specific nutrients in different Borrelia species.
dc.formatapplication/pdf
dc.languageeng
dc.publisherSan Francisco, CA : Public Library of Science
dc.relation.ispartofseriesPLoS ONE, Volume 7, Issue 5-
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/ger
dc.subjectAnimals
dc.subjectBacterial Outer Membrane Proteins
dc.subjectBorrelia
dc.subjectCell Membrane Permeability
dc.subjectDicarboxylic Acid Transporters
dc.subjectHumans
dc.subjectLyme Disease
dc.subjectRabbits
dc.subjectSequence Homology
dc.subjectAmino Acid
dc.subjectSubstrate Specificity
dc.subject.ddc610
dc.titleDipA, a pore-forming protein in the outer membrane of lyme disease spirochetes exhibits specificity for the permeation of dicarboxylate
dc.typearticle-
dc.typeText-
dc.description.versionpublishedVersioneng
local.accessRightsopenAccess-
wgl.contributorISASger
wgl.subjectMedizin, Gesundheitger
wgl.typeZeitschriftenartikelger
dc.relation.doihttps://doi.org/10.1371/journal.pone.0036523
dcterms.bibliographicCitation.journalTitlePLOS ONE-
local.identifier.doihttp://dx.doi.org/10.34657/1726-
Appears in Collections:Medizin

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