PMID- 11859097
OWN - NLM
STAT- MEDLINE
DCOM- 20020315
LR  - 20211203
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 168
IP  - 5
DP  - 2002 Mar 1
TI  - The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen for 
      presentation to T cells.
PG  - 2118-26
AB  - Dendritic cells (DCs) capture Ags or viruses in peripheral tissue to transport 
      them to lymphoid organs to induce cellular T cell responses. Recently, a 
      DC-specific C-type lectin was identified, DC-specific ICAM-grabbing non-integrin 
      (DC-SIGN), that functions as cell adhesion receptor mediating both DC migration 
      and T cell activation. DC-SIGN also functions as an HIV-1R that captures HIVgp120 
      and facilitates DC-induced HIV transmission of T cells. Internalization motifs in 
      the cytoplasmic tail of DC-SIGN hint to a function of DC-SIGN as endocytic 
      receptor. In this study we demonstrate that on DCs DC-SIGN is rapidly 
      internalized upon binding of soluble ligand. Mutating a putative internalization 
      motif in the cytoplasmic tail reduces ligand-induced internalization. Detailed 
      analysis using ratio fluorescence imaging and electron microscopy showed that 
      DC-SIGN-ligand complexes are targeted to late endosomes/lysosomes. Moreover, 
      ligands internalized by DC-SIGN are efficiently processed and presented to CD4+ T 
      cells. The distinct pattern of expression of C-type lectins on DCs in situ and 
      their nonoverlapping Ag recognition profile hint to selective functions of these 
      receptors to allow a DC to recognize a wide variety of Ags and to process these 
      to induce T cell activation. These data point to a novel function of the adhesion 
      receptor DC-SIGN as an efficient DC-specific Ag receptor that can be used as a 
      target to induce viral and antitumor immunity.
FAU - Engering, Anneke
AU  - Engering A
AD  - Department of Molecular Cell Biology, Vrye Universiteit Medical Center, van der 
      Boechorststraat 7, 1081 BT Amsterdam, The Netherlands.
FAU - Geijtenbeek, Teunis B H
AU  - Geijtenbeek TB
FAU - van Vliet, Sandra J
AU  - van Vliet SJ
FAU - Wijers, Mietske
AU  - Wijers M
FAU - van Liempt, Ellis
AU  - van Liempt E
FAU - Demaurex, Nicolas
AU  - Demaurex N
FAU - Lanzavecchia, Antonio
AU  - Lanzavecchia A
FAU - Fransen, Jack
AU  - Fransen J
FAU - Figdor, Carl G
AU  - Figdor CG
FAU - Piguet, Vincent
AU  - Piguet V
FAU - van Kooyk, Yvette
AU  - van Kooyk Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (DC-specific ICAM-3 grabbing nonintegrin)
RN  - 0 (Lectins)
RN  - 0 (Lectins, C-Type)
RN  - 0 (Ligands)
RN  - 0 (Mannose Receptor)
RN  - 0 (Mannose-Binding Lectins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, Immunologic)
SB  - IM
MH  - Amino Acid Sequence
MH  - *Antigen Presentation
MH  - CD4-Positive T-Lymphocytes/*immunology
MH  - Cell Adhesion Molecules/metabolism/physiology
MH  - Cells, Cultured
MH  - Clone Cells
MH  - Dendritic Cells/cytology/*immunology/ultrastructure
MH  - Endocytosis
MH  - Endosomes/metabolism/ultrastructure
MH  - Humans
MH  - Lectins/chemistry/*metabolism/*physiology
MH  - Lectins, C-Type
MH  - Ligands
MH  - Lysosomes/metabolism/ultrastructure
MH  - Mannose Receptor
MH  - *Mannose-Binding Lectins
MH  - Microscopy, Fluorescence
MH  - Molecular Sequence Data
MH  - Receptors, Cell Surface/chemistry/*metabolism/*physiology
MH  - Receptors, Immunologic/metabolism/physiology
MH  - Sequence Homology, Amino Acid
EDAT- 2002/02/23 10:00
MHDA- 2002/03/16 10:01
CRDT- 2002/02/23 10:00
PHST- 2002/02/23 10:00 [pubmed]
PHST- 2002/03/16 10:01 [medline]
PHST- 2002/02/23 10:00 [entrez]
AID - 10.4049/jimmunol.168.5.2118 [doi]
PST - ppublish
SO  - J Immunol. 2002 Mar 1;168(5):2118-26. doi: 10.4049/jimmunol.168.5.2118.