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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Autores principales:	Joost te Riet, Ben Joosten, Inge Reinieren-Beeren, Carl G. Figdor, Alessandra Cambi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2792df3e23b645b498863f907b74dc47
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spelling	oai:doaj.org-article:2792df3e23b645b498863f907b74dc472021-12-02T11:52:20ZN-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy10.1038/s41598-017-07220-w2045-2322https://doaj.org/article/2792df3e23b645b498863f907b74dc472017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07220-whttps://doaj.org/toc/2045-2322Abstract 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.Joost te RietBen JoostenInge Reinieren-BeerenCarl G. FigdorAlessandra CambiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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
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.
format	article
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
title	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_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_sort	n-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/2792df3e23b645b498863f907b74dc47
work_keys_str_mv	AT joostteriet nglycanmediatedadhesionstrengtheningduringpathogenreceptorbindingrevealedbycellcellforcespectroscopy AT benjoosten nglycanmediatedadhesionstrengtheningduringpathogenreceptorbindingrevealedbycellcellforcespectroscopy AT ingereinierenbeeren nglycanmediatedadhesionstrengtheningduringpathogenreceptorbindingrevealedbycellcellforcespectroscopy AT carlgfigdor nglycanmediatedadhesionstrengtheningduringpathogenreceptorbindingrevealedbycellcellforcespectroscopy AT alessandracambi nglycanmediatedadhesionstrengtheningduringpathogenreceptorbindingrevealedbycellcellforcespectroscopy
_version_	1718395092483440640

N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy

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