Publication year
2004Source
Journal of Cell Biology, 164, 1, (2004), pp. 145-55ISSN
Publication type
Article / Letter to editor

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Organization
Tumorimmunology
Cell Biology (UMC)
Biochemistry (UMC)
Journal title
Journal of Cell Biology
Volume
vol. 164
Issue
iss. 1
Page start
p. 145
Page end
p. 55
Subject
UMCN 1.4: Immunotherapy, gene therapy and transplantation; UMCN 5.3: Cellular energy metabolismAbstract
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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- Faculty of Medical Sciences [86157]
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