Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells.
SourceJournal of Cell Biology, 164, 1, (2004), pp. 145-55
Article / Letter to editor
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Cell Biology (UMC)
Journal of Cell Biology
SubjectUMCN 1.4: Immunotherapy, gene therapy and transplantation; UMCN 5.3: Cellular energy metabolism
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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