Differential recognition of lipid domains by two Gb3-binding lectins
Abstract: The two lectins LecA from Pseudomonas aeruginosa and the B-subunit of Shiga toxin from Shigella dysenteriae (StxB) share the glycosphingolipid globotriaosylceramide (Gb3) as receptor. Counterintuitively, we found that LecA and StxB segregated into different domains after recognizing Gb3 at the plasma membrane of cells. We hypothesized that the orientation of the carbohydrate head group of Gb3 embedded in the lipid bilayer differentially influences LecA and StxB binding. To test this hypothesis, we reconstituted lectin-Gb3 interaction using giant unilamellar vesicles and were indeed able to rebuild LecA and StxB segregation. Both, the Gb3 fatty acyl chain structure and the local membrane environment, modulated Gb3 recognition by LecA and StxB. Specifically, StxB preferred more ordered membranes compared to LecA. Based on our findings, we propose comparing staining patterns of LecA and StxB as an alternative method to assess membrane order in cells. To verify this approach, we re-established that the apical plasma membrane of epithelial cells is more ordered than the basolateral plasma membrane. Additionally, we found that StxB recognized Gb3 at the primary cilium and the periciliary membrane, whereas LecA only bound periciliary Gb3. This suggests that the ciliary membrane is of higher order than the surrounding periciliary membrane
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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Scientific reports. - 10 (2020) , 9752, ISSN: 2045-2322
- Classification
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Psychologie
- Event
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Veröffentlichung
- (where)
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Freiburg
- (who)
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Universität
- (when)
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2020
- Creator
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Schubert, Thomas
Sych, Taras
Madl, Josef
Xu, Maokai
Omidvar, Ramin
Patalg, Lukas J.
Ries, Annika
Kettelhoit, Katharina
Brandel, Annette
Mély, Yves
Steinem, Claudia
Werz, Daniel B.
Thünauer, Roland
Römer, Winfried
- DOI
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10.1038/s41598-020-66522-8
- URN
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urn:nbn:de:bsz:25-freidok-1663415
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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25.03.2025, 1:53 PM CET
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Schubert, Thomas
- Sych, Taras
- Madl, Josef
- Xu, Maokai
- Omidvar, Ramin
- Patalg, Lukas J.
- Ries, Annika
- Kettelhoit, Katharina
- Brandel, Annette
- Mély, Yves
- Steinem, Claudia
- Werz, Daniel B.
- Thünauer, Roland
- Römer, Winfried
- Universität
Time of origin
- 2020
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On binding domains
GYF domains : a class of proline rich ligand binding adaptor domains
Ubiquitin-binding domains in polyubiquitin chain synthesis
Protein lipid interactions : from membrane domains to cellular networks
Lipid and image analysis tools for studying lipid-protein binding dynamics in living cells
Binding Proteins and Receptor Binding Domains as Sensor Elements for Biological and Artificial Nanopores
Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
Specificity profiles of protien recognition domains in the molecular medicine
Non-oscillation domains of differential equations with two parameters
Translational and rotational diffusion of micrometer-sized solid domains in lipid membranes
Micro-domains as site for storage lipid biosynthesis in seeds and algae
Beta-Peptide Helices As Transmembrane Domains: Aggregation, Recognition and Lipid-Peptide Interaction
On binding domains
GYF domains : a class of proline rich ligand binding adaptor domains
Ubiquitin-binding domains in polyubiquitin chain synthesis
Protein lipid interactions : from membrane domains to cellular networks
Lipid and image analysis tools for studying lipid-protein binding dynamics in living cells
Binding Proteins and Receptor Binding Domains as Sensor Elements for Biological and Artificial Nanopores
Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
Specificity profiles of protien recognition domains in the molecular medicine
Non-oscillation domains of differential equations with two parameters
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