N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy
Abstract Glycan-protein lateral interactions have gained increased attention as important modulators of receptor function, by regulating surface residence time and endocytosis of membrane glycoproteins. The pathogen-recognition receptor DC-SIGN is highly expressed at the membrane of antigen-presenti...
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| Format: | Article |
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Nature Portfolio
2017-07-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-017-07220-w |
| _version_ | 1818431052089131008 |
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| author | Joost te Riet Ben Joosten Inge Reinieren-Beeren Carl G. Figdor Alessandra Cambi |
| author_facet | Joost te Riet Ben Joosten Inge Reinieren-Beeren Carl G. Figdor Alessandra Cambi |
| author_sort | Joost te Riet |
| collection | DOAJ |
| description | Abstract Glycan-protein lateral interactions have gained increased attention as important modulators of receptor function, by regulating surface residence time and endocytosis of membrane glycoproteins. The pathogen-recognition receptor DC-SIGN is highly expressed at the membrane of antigen-presenting dendritic cells, where it is organized in nanoclusters and binds to different viruses, bacteria and fungi. We recently demonstrated that DC-SIGN N-glycans spatially restrict receptor diffusion within the plasma membrane, favoring its internalization through clathrin-coated pits. Here, we investigated the involvement of the N-glycans of DC-SIGN expressing cells on pathogen binding strengthening when interacting with Candida fungal cells by using atomic force microscope (AFM)-assisted single cell-pathogen adhesion measurements. The use of DC-SIGN mutants lacking the N-glycans as well as blocking glycan-mediated lateral interactions strongly impaired cell stiffening during pathogen binding. Our findings demonstrate for the first time the direct involvement of the cell membrane glycans in strengthening cell-pathogen interactions. This study, therefore, puts forward a possible role for the glycocalyx as extracellular cytoskeleton contributing, possibly in connection with the intracellular actin cytoskeleton, to optimize strengthening of cell-pathogen interactions in the presence of mechanical forces. |
| first_indexed | 2024-12-14T15:43:10Z |
| format | Article |
| id | doaj.art-2792df3e23b645b498863f907b74dc47 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-14T15:43:10Z |
| publishDate | 2017-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-2792df3e23b645b498863f907b74dc472022-12-21T22:55:34ZengNature PortfolioScientific Reports2045-23222017-07-017111210.1038/s41598-017-07220-wN-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopyJoost te Riet0Ben Joosten1Inge Reinieren-Beeren2Carl G. Figdor3Alessandra Cambi4Department of Tumor Immunology, Radboud Institute for Medical Life Sciences, Radboud University Medical CenterDepartment of Cell Biology, Radboud Institute for Molecular Life Sciences, Radboud University Medical CenterDepartment of Tumor Immunology, Radboud Institute for Medical Life Sciences, Radboud University Medical CenterDepartment of Tumor Immunology, Radboud Institute for Medical Life Sciences, Radboud University Medical CenterDepartment of Cell Biology, Radboud Institute for Molecular Life Sciences, Radboud University Medical CenterAbstract Glycan-protein lateral interactions have gained increased attention as important modulators of receptor function, by regulating surface residence time and endocytosis of membrane glycoproteins. The pathogen-recognition receptor DC-SIGN is highly expressed at the membrane of antigen-presenting dendritic cells, where it is organized in nanoclusters and binds to different viruses, bacteria and fungi. We recently demonstrated that DC-SIGN N-glycans spatially restrict receptor diffusion within the plasma membrane, favoring its internalization through clathrin-coated pits. Here, we investigated the involvement of the N-glycans of DC-SIGN expressing cells on pathogen binding strengthening when interacting with Candida fungal cells by using atomic force microscope (AFM)-assisted single cell-pathogen adhesion measurements. The use of DC-SIGN mutants lacking the N-glycans as well as blocking glycan-mediated lateral interactions strongly impaired cell stiffening during pathogen binding. Our findings demonstrate for the first time the direct involvement of the cell membrane glycans in strengthening cell-pathogen interactions. This study, therefore, puts forward a possible role for the glycocalyx as extracellular cytoskeleton contributing, possibly in connection with the intracellular actin cytoskeleton, to optimize strengthening of cell-pathogen interactions in the presence of mechanical forces.https://doi.org/10.1038/s41598-017-07220-w |
| spellingShingle | Joost te Riet Ben Joosten Inge Reinieren-Beeren Carl G. Figdor Alessandra Cambi N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy Scientific Reports |
| title | N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy |
| title_full | N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy |
| title_fullStr | N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy |
| title_full_unstemmed | N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy |
| title_short | N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy |
| title_sort | n glycan mediated adhesion strengthening during pathogen receptor binding revealed by cell cell force spectroscopy |
| url | https://doi.org/10.1038/s41598-017-07220-w |
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