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dc.contributor.authorOh, Yoo Jin
dc.contributor.authorSekot, Gerhard
dc.contributor.authorDuman, Memed
dc.contributor.authorChtcheglova, Lilia
dc.contributor.authorMessner, Paul
dc.contributor.authorPeterlik, Herwig
dc.contributor.authorSchaeffer, Christina
dc.contributor.authorHinterdorfer, Peter
dc.date.accessioned2019-12-16T09:57:19Z
dc.date.available2019-12-16T09:57:19Z
dc.date.issued2013
dc.identifier.issn0952-3499
dc.identifier.urihttps://doi.org/10.1002/jmr.2298
dc.identifier.urihttp://hdl.handle.net/11655/19864
dc.description.abstractTannerella forsythia is among the most potent triggers of periodontal diseases, and approaches to understand underlying mechanisms are currently intensively pursued. A similar to 22-nm-thick, 2D crystalline surface (S-) layer that completely covers Tannerella forsythia cells is crucially involved in the bacterium-host cross-talk. The S-layer is composed of two intercalating glycoproteins (TfsA-GP, TfsB-GP) that are aligned into a periodic lattice. To characterize this unique S-layer structure at the nanometer scale directly on intact T. forsythia cells, three complementary methods, i.e., small-angle X-ray scattering (SAXS), atomic force microscopy (AFM), and single-molecular force spectroscopy (SMFS), were applied. SAXS served as a difference method using signals from wild-type and S-layer-deficient cells for data evaluation, revealing two possible models for the assembly of the glycoproteins. Direct high-resolution imaging of the outer surface of T. forsythia wild-type cells by AFM revealed a p4 structure with a lattice constant of similar to 9.0 nm. In contrast, on mutant cells, no periodic lattice could be visualized. Additionally, SMFS was used to probe specific interaction forces between an anti-TfsA antibody coupled to the AFM tip and the S-layer as present on T. forsythia wild-type and mutant cells, displaying TfsA-GP alone. Unbinding forces between the antibody and wild-type cells were greater than with mutant cells. This indicated that the TfsA-GP is not so strongly attached to the mutant cell surface when the co-assembling TfsB-GP is missing. Altogether, the data gained from SAXS, AFM, and SMFS confirm the current model of the S-layer architecture with two intercalating S-layer glycoproteins and TfsA-GP being mainly outwardly oriented. Copyright (c) 2013 John Wiley & Sons, Ltd.
dc.language.isoen
dc.publisherWiley-Blackwell
dc.relation.isversionof10.1002/jmr.2298
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.titleCharacterizing The S-Layer Structure And Anti-S-Layer Antibody Recognition On Intact Tannerella Forsythia Cells By Scanning Probe Microscopy And Small Angle X-Ray Scattering
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/publishedVersion
dc.relation.journalJournal Of Molecular Recognition
dc.contributor.departmentNanoteknoloji ve Nanotıp
dc.identifier.volume26
dc.identifier.issue11
dc.identifier.startpage542
dc.identifier.endpage549
dc.description.indexWoS


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