Mapping nano-landscape of pathogen recognition receptor DC-SIGN and lipid rafts on dendritic cells

T. van Zanten, J. Zambrano, M. Koopman, A. Cambi, B. Joosten, C.G. Figdor, M.F. Garcia Parajo

Research output: Contribution to journalMeeting AbstractOther research output

Abstract

The dendritic cell (DC) specific pathogen-recognition receptor DCSIGN binds and internalizes antigens for degradation. The organization of DC-SIGN in microdomains is crucial for the binding and the internalization of virus particles, suggesting that these multimolecular assemblies act as docking site for pathogens like HIV-1 to invade the host. We have recently shown that DC-SIGN potentially associates with lipid rafts [1] and clathrin coated pits [2]. Nevertheless, the nano-scale organization of DC-SIGN with respect to these lipid domains remains largely unresolved. To map the nanolandscape distribution of DC-SIGN on DC cell membranes we are exploiting state-of-the-art microscopic imaging techniques. Single fluorescent molecule detection together with multicolor labeling offers the possibility to elucidate organization and co-localization at <100 nm spatial resolution. Currently we are investigating the potential association of DC-SIGN with lipid rafts using a near-field optical microscope working under physiological conditions. Additionally we are planning a three color experiment to resolve the nano-landscape of DC-SIGN, lipid rafts and clathrin coated pits before and during endocytosis. The possible change in organization and association of DC-SIGN is essential for the understanding of the antigen uptake mechanism(s) from the membrane of DCs. [1] A. Cambi, et al., Journal of Cell Biology, 164, 145 (2004). [2] A. Cambi, et al., Nanoletters, In Press.

Original languageEnglish
Article numberP-500
Pages (from-to)S181-S181
JournalEuropean biophysics journal
Volume36
Issue number1
DOIs
Publication statusPublished - 2007
Event6th European Biophysics Congress, EBSA 2007 - London, United Kingdom
Duration: 14 Jul 200719 Jul 2007
Conference number: 6

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Dendritic Cells
Lipids
Clathrin
Antigens
Endocytosis
Virion
Cell Biology
HIV-1
Color
Cell Membrane
Membranes

Cite this

van Zanten, T., Zambrano, J., Koopman, M., Cambi, A., Joosten, B., Figdor, C. G., & Garcia Parajo, M. F. (2007). Mapping nano-landscape of pathogen recognition receptor DC-SIGN and lipid rafts on dendritic cells. European biophysics journal, 36(1), S181-S181. [P-500]. https://doi.org/10.1007/s00249-007-0178-7
van Zanten, T. ; Zambrano, J. ; Koopman, M. ; Cambi, A. ; Joosten, B. ; Figdor, C.G. ; Garcia Parajo, M.F. / Mapping nano-landscape of pathogen recognition receptor DC-SIGN and lipid rafts on dendritic cells. In: European biophysics journal. 2007 ; Vol. 36, No. 1. pp. S181-S181.
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abstract = "The dendritic cell (DC) specific pathogen-recognition receptor DCSIGN binds and internalizes antigens for degradation. The organization of DC-SIGN in microdomains is crucial for the binding and the internalization of virus particles, suggesting that these multimolecular assemblies act as docking site for pathogens like HIV-1 to invade the host. We have recently shown that DC-SIGN potentially associates with lipid rafts [1] and clathrin coated pits [2]. Nevertheless, the nano-scale organization of DC-SIGN with respect to these lipid domains remains largely unresolved. To map the nanolandscape distribution of DC-SIGN on DC cell membranes we are exploiting state-of-the-art microscopic imaging techniques. Single fluorescent molecule detection together with multicolor labeling offers the possibility to elucidate organization and co-localization at <100 nm spatial resolution. Currently we are investigating the potential association of DC-SIGN with lipid rafts using a near-field optical microscope working under physiological conditions. Additionally we are planning a three color experiment to resolve the nano-landscape of DC-SIGN, lipid rafts and clathrin coated pits before and during endocytosis. The possible change in organization and association of DC-SIGN is essential for the understanding of the antigen uptake mechanism(s) from the membrane of DCs. [1] A. Cambi, et al., Journal of Cell Biology, 164, 145 (2004). [2] A. Cambi, et al., Nanoletters, In Press.",
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van Zanten, T, Zambrano, J, Koopman, M, Cambi, A, Joosten, B, Figdor, CG & Garcia Parajo, MF 2007, 'Mapping nano-landscape of pathogen recognition receptor DC-SIGN and lipid rafts on dendritic cells' European biophysics journal, vol. 36, no. 1, P-500, pp. S181-S181. https://doi.org/10.1007/s00249-007-0178-7

Mapping nano-landscape of pathogen recognition receptor DC-SIGN and lipid rafts on dendritic cells. / van Zanten, T.; Zambrano, J.; Koopman, M.; Cambi, A.; Joosten, B.; Figdor, C.G.; Garcia Parajo, M.F.

In: European biophysics journal, Vol. 36, No. 1, P-500, 2007, p. S181-S181.

Research output: Contribution to journalMeeting AbstractOther research output

TY - JOUR

T1 - Mapping nano-landscape of pathogen recognition receptor DC-SIGN and lipid rafts on dendritic cells

AU - van Zanten, T.

AU - Zambrano, J.

AU - Koopman, M.

AU - Cambi, A.

AU - Joosten, B.

AU - Figdor, C.G.

AU - Garcia Parajo, M.F.

PY - 2007

Y1 - 2007

N2 - The dendritic cell (DC) specific pathogen-recognition receptor DCSIGN binds and internalizes antigens for degradation. The organization of DC-SIGN in microdomains is crucial for the binding and the internalization of virus particles, suggesting that these multimolecular assemblies act as docking site for pathogens like HIV-1 to invade the host. We have recently shown that DC-SIGN potentially associates with lipid rafts [1] and clathrin coated pits [2]. Nevertheless, the nano-scale organization of DC-SIGN with respect to these lipid domains remains largely unresolved. To map the nanolandscape distribution of DC-SIGN on DC cell membranes we are exploiting state-of-the-art microscopic imaging techniques. Single fluorescent molecule detection together with multicolor labeling offers the possibility to elucidate organization and co-localization at <100 nm spatial resolution. Currently we are investigating the potential association of DC-SIGN with lipid rafts using a near-field optical microscope working under physiological conditions. Additionally we are planning a three color experiment to resolve the nano-landscape of DC-SIGN, lipid rafts and clathrin coated pits before and during endocytosis. The possible change in organization and association of DC-SIGN is essential for the understanding of the antigen uptake mechanism(s) from the membrane of DCs. [1] A. Cambi, et al., Journal of Cell Biology, 164, 145 (2004). [2] A. Cambi, et al., Nanoletters, In Press.

AB - The dendritic cell (DC) specific pathogen-recognition receptor DCSIGN binds and internalizes antigens for degradation. The organization of DC-SIGN in microdomains is crucial for the binding and the internalization of virus particles, suggesting that these multimolecular assemblies act as docking site for pathogens like HIV-1 to invade the host. We have recently shown that DC-SIGN potentially associates with lipid rafts [1] and clathrin coated pits [2]. Nevertheless, the nano-scale organization of DC-SIGN with respect to these lipid domains remains largely unresolved. To map the nanolandscape distribution of DC-SIGN on DC cell membranes we are exploiting state-of-the-art microscopic imaging techniques. Single fluorescent molecule detection together with multicolor labeling offers the possibility to elucidate organization and co-localization at <100 nm spatial resolution. Currently we are investigating the potential association of DC-SIGN with lipid rafts using a near-field optical microscope working under physiological conditions. Additionally we are planning a three color experiment to resolve the nano-landscape of DC-SIGN, lipid rafts and clathrin coated pits before and during endocytosis. The possible change in organization and association of DC-SIGN is essential for the understanding of the antigen uptake mechanism(s) from the membrane of DCs. [1] A. Cambi, et al., Journal of Cell Biology, 164, 145 (2004). [2] A. Cambi, et al., Nanoletters, In Press.

U2 - 10.1007/s00249-007-0178-7

DO - 10.1007/s00249-007-0178-7

M3 - Meeting Abstract

VL - 36

SP - S181-S181

JO - European biophysics journal

JF - European biophysics journal

SN - 0175-7571

IS - 1

M1 - P-500

ER -