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dc.date.accessioned2017-04-27T10:27:05Z
dc.date.available2018-02-27T23:30:52Z
dc.date.created2017-03-20T12:29:52Z
dc.date.issued2017
dc.identifier.citationHatlem, Daniel Heggelund, Julie Elisabeth Burschowsky, Daniel Krengel, Ute Kristiansen, Per Eugen . 1H, 13C, 15N backbone assignment of the human heat-labile enterotoxin B-pentamer and chemical shift mapping of neolactotetraose binding. Biomolecular NMR Assignments. 2017, 11, 99-104
dc.identifier.urihttp://hdl.handle.net/10852/55283
dc.description.abstractThe major virulence factor of enterotoxigenic Escherichia coli is the heat-labile enterotoxin (LT), an AB5 toxin closely related to the cholera toxin. LT consists of six subunits, the catalytically active A-subunit and five B-subunits arranged as a pentameric ring (LTB), which enable the toxin to bind to the epithelial cells in the intestinal lumen. LTB has two recognized binding sites; the primary binding site is responsible for anchoring the toxin to its main receptor, the GM1-ganglioside, while the secondary binding site recognizes blood group antigens. Herein, we report the 1H, 13C, 15N main chain assignment of LTB from human isolates (hLTB; 103 a.a. per subunit, with a total molecular mass of 58.5 kDa). The secondary structure was predicted based on 13C′, 13Cα, 13Cβ, 1HN and 15N chemical shifts and compared to a published crystal structure of LTB. Neolactotetraose (NEO) was titrated to hLTB and chemical shift perturbations were measured. The chemical shift perturbations were mapped onto the crystal structure, confirming that NEO binds to the primary binding site of hLTB and competes with GM1-binding. Our new data further lend support to the hypothesis that binding at the primary binding site is transmitted to the secondary binding site of the toxin, where it may influence the binding to blood group antigens. This research was first published in Biomolecular NMR Assignments. © Springer Verlag.en_US
dc.languageEN
dc.title1H, 13C, 15N backbone assignment of the human heat-labile enterotoxin B-pentamer and chemical shift mapping of neolactotetraose bindingen_US
dc.typeJournal articleen_US
dc.creator.authorHatlem, Daniel
dc.creator.authorHeggelund, Julie Elisabeth
dc.creator.authorBurschowsky, Daniel
dc.creator.authorKrengel, Ute
dc.creator.authorKristiansen, Per Eugen
cristin.unitcode185,15,29,60
cristin.unitnameSeksjon for genetikk og evolusjonsbiologi
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1
dc.identifier.cristin1459608
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biomolecular NMR Assignments&rft.volume=11&rft.spage=99&rft.date=2017
dc.identifier.jtitleBiomolecular NMR Assignments
dc.identifier.volume11
dc.identifier.startpage99
dc.identifier.endpage104
dc.identifier.doi10.1007/s12104-017-9728-9
dc.identifier.urnURN:NBN:no-58090
dc.type.documentTidsskriftartikkelen_US
dc.type.peerreviewedPeer reviewed
dc.source.issn1874-2718
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/55283/4/hLTB_publication_20170112.pdf
dc.type.versionAcceptedVersion


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