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dc.date.accessioned2018-10-09T10:10:08Z
dc.date.available2018-10-09T10:10:08Z
dc.date.created2017-01-10T14:55:08Z
dc.date.issued2017
dc.identifier.citationMühlenkamp, Melanie C. Hallstrom, Teresia Autenrieth, Ingo B. Bohn, Erwin Linke, Dirk Rinker, Janina Riesbeck, Kristian Singh, Birendra Leo, Jack Christopher Hammerschmidt, Sven Zipfel, Peter F. Schütz, Monika . Vitronectin binds to a specific stretch within the head region of yersinia adhesin a and thereby modulates yersinia enterocolitica host interaction. Journal of Innate Immunity. 2017, 9(1), 33-51
dc.identifier.urihttp://hdl.handle.net/10852/65094
dc.description.abstractComplement resistance is an important virulence trait of Yersinia enterocolitica (Ye). The predominant virulence factor expressed by Ye is Yersinia adhesin A (YadA), which enables bacterial attachment to host cells and extracellular matrix and additionally allows the acquisition of soluble serum factors. The serum glycoprotein vitronectin (Vn) acts as an inhibitory regulator of the terminal complement complex by inhibiting the lytic pore formation. Here, we show YadA-mediated direct interaction of Ye with Vn and investigated the role of this Vn binding during mouse infection in vivo. Using different Yersinia strains, we identified a short stretch in the YadA head domain of Ye O:9 E40, similar to the ‘uptake region' of Y. pseudotuberculosis YPIII YadA, as crucial for efficient Vn binding. Using recombinant fragments of Vn, we found the C-terminal part of Vn, including heparin-binding domain 3, to be responsible for binding to YadA. Moreover, we found that Vn bound to the bacterial surface is still functionally active and thus inhibits C5b-9 formation. In a mouse infection model, we demonstrate that Vn reduces complement-mediated killing of Ye O:9 E40 and, thus, improved bacterial survival. Taken together, these findings show that YadA-mediated Vn binding influences Ye pathogenesis. © 2017 Karger Publishersen_US
dc.languageEN
dc.titleVitronectin binds to a specific stretch within the head region of yersinia adhesin a and thereby modulates yersinia enterocolitica host interactionen_US
dc.title.alternativeENEngelskEnglishVitronectin binds to a specific stretch within the head region of yersinia adhesin a and thereby modulates yersinia enterocolitica host interaction
dc.typeJournal articleen_US
dc.creator.authorMühlenkamp, Melanie C.
dc.creator.authorHallstrom, Teresia
dc.creator.authorAutenrieth, Ingo B.
dc.creator.authorBohn, Erwin
dc.creator.authorLinke, Dirk
dc.creator.authorRinker, Janina
dc.creator.authorRiesbeck, Kristian
dc.creator.authorSingh, Birendra
dc.creator.authorLeo, Jack Christopher
dc.creator.authorHammerschmidt, Sven
dc.creator.authorZipfel, Peter F.
dc.creator.authorSchütz, Monika
cristin.unitcode185,15,29,0
cristin.unitnameInstitutt for biovitenskap
cristin.ispublishedtrue
cristin.fulltextpreprint
cristin.qualitycode1
dc.identifier.cristin1424350
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal of Innate Immunity&rft.volume=9&rft.spage=33&rft.date=2017
dc.identifier.jtitleJournal of Innate Immunity
dc.identifier.volume9
dc.identifier.issue1
dc.identifier.startpage33
dc.identifier.endpage51
dc.identifier.doihttp://dx.doi.org/10.1159/000449200
dc.identifier.urnURN:NBN:no-67627
dc.type.documentTidsskriftartikkelen_US
dc.source.issn1662-811X
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/65094/1/M%25C3%25BChlenkamp%2Bet%2Bal%2Bsumbission%2BPDF.pdf
dc.type.versionSubmittedVersion
dc.relation.projectNFR/240483


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