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Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells

The C-type lectin dendritic cell (DC)–specific intercellular adhesion molecule grabbing non-integrin (DC-SIGN; CD209) facilitates binding and internalization of several viruses, including HIV-1, on DCs, but the underlying mechanism for being such an efficient phagocytic pathogen-recognition receptor...

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Autores principales: Cambi, Alessandra, de Lange, Frank, van Maarseveen, Noortje M., Nijhuis, Monique, Joosten, Ben, van Dijk, Erik M.H.P., de Bakker, Bärbel I., Fransen, Jack A.M., Bovee-Geurts, Petra H.M., van Leeuwen, Frank N., Van Hulst, Niek F., Figdor, Carl G.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2004
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171967/
https://www.ncbi.nlm.nih.gov/pubmed/14709546
http://dx.doi.org/10.1083/jcb.200306112
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author Cambi, Alessandra
de Lange, Frank
van Maarseveen, Noortje M.
Nijhuis, Monique
Joosten, Ben
van Dijk, Erik M.H.P.
de Bakker, Bärbel I.
Fransen, Jack A.M.
Bovee-Geurts, Petra H.M.
van Leeuwen, Frank N.
Van Hulst, Niek F.
Figdor, Carl G.
author_facet Cambi, Alessandra
de Lange, Frank
van Maarseveen, Noortje M.
Nijhuis, Monique
Joosten, Ben
van Dijk, Erik M.H.P.
de Bakker, Bärbel I.
Fransen, Jack A.M.
Bovee-Geurts, Petra H.M.
van Leeuwen, Frank N.
Van Hulst, Niek F.
Figdor, Carl G.
author_sort Cambi, Alessandra
collection PubMed
description The C-type lectin dendritic cell (DC)–specific intercellular adhesion molecule grabbing non-integrin (DC-SIGN; CD209) facilitates binding and internalization of several viruses, including HIV-1, on DCs, but the underlying mechanism for being such an efficient phagocytic pathogen-recognition receptor is poorly understood. By high resolution electron microscopy, we demonstrate a direct relation between DC-SIGN function as viral receptor and its microlocalization on the plasma membrane. During development of human monocyte-derived DCs, DC-SIGN becomes organized in well-defined microdomains, with an average diameter of 200 nm. Biochemical experiments and confocal microscopy indicate that DC-SIGN microdomains reside within lipid rafts. Finally, we show that the organization of DC-SIGN in microdomains on the plasma membrane is important for binding and internalization of virus particles, suggesting that these multimolecular assemblies of DC-SIGN act as a docking site for pathogens like HIV-1 to invade the host.
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spelling pubmed-21719672008-03-05 Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells Cambi, Alessandra de Lange, Frank van Maarseveen, Noortje M. Nijhuis, Monique Joosten, Ben van Dijk, Erik M.H.P. de Bakker, Bärbel I. Fransen, Jack A.M. Bovee-Geurts, Petra H.M. van Leeuwen, Frank N. Van Hulst, Niek F. Figdor, Carl G. J Cell Biol Article The C-type lectin dendritic cell (DC)–specific intercellular adhesion molecule grabbing non-integrin (DC-SIGN; CD209) facilitates binding and internalization of several viruses, including HIV-1, on DCs, but the underlying mechanism for being such an efficient phagocytic pathogen-recognition receptor is poorly understood. By high resolution electron microscopy, we demonstrate a direct relation between DC-SIGN function as viral receptor and its microlocalization on the plasma membrane. During development of human monocyte-derived DCs, DC-SIGN becomes organized in well-defined microdomains, with an average diameter of 200 nm. Biochemical experiments and confocal microscopy indicate that DC-SIGN microdomains reside within lipid rafts. Finally, we show that the organization of DC-SIGN in microdomains on the plasma membrane is important for binding and internalization of virus particles, suggesting that these multimolecular assemblies of DC-SIGN act as a docking site for pathogens like HIV-1 to invade the host. The Rockefeller University Press 2004-01-05 /pmc/articles/PMC2171967/ /pubmed/14709546 http://dx.doi.org/10.1083/jcb.200306112 Text en Copyright © 2004, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Cambi, Alessandra
de Lange, Frank
van Maarseveen, Noortje M.
Nijhuis, Monique
Joosten, Ben
van Dijk, Erik M.H.P.
de Bakker, Bärbel I.
Fransen, Jack A.M.
Bovee-Geurts, Petra H.M.
van Leeuwen, Frank N.
Van Hulst, Niek F.
Figdor, Carl G.
Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
title Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
title_full Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
title_fullStr Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
title_full_unstemmed Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
title_short Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
title_sort microdomains of the c-type lectin dc-sign are portals for virus entry into dendritic cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171967/
https://www.ncbi.nlm.nih.gov/pubmed/14709546
http://dx.doi.org/10.1083/jcb.200306112
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