A Dendritic Cell–Specific Intercellular Adhesion Molecule 3–Grabbing Nonintegrin (Dc-Sign)–Related Protein Is Highly Expressed on Human Liver Sinusoidal Endothelial Cells and Promotes HIV-1 Infection

  title={A Dendritic Cell–Specific Intercellular Adhesion Molecule 3–Grabbing Nonintegrin (Dc-Sign)–Related Protein Is Highly Expressed on Human Liver Sinusoidal Endothelial Cells and Promotes HIV-1 Infection},
  author={Arman Bashirova and Teunis B. H. Geijtenbeek and Gerard C F van Duijnhoven and Sandra J. van Vliet and Jeroen B. G. Eilering and Maureen P. Martin and Li Wu and T. D. Martin and Nicola K. Viebig and Percy A. Knolle and Vineet N Kewalramani and Yvette van Kooyk and Mary N. Carrington},
  journal={The Journal of Experimental Medicine},
  pages={671 - 678}
The discovery of dendritic cell (DC)-specific intercellular adhesion molecule (ICAM)-3–grabbing nonintegrin (DC-SIGN) as a DC-specific ICAM-3 binding receptor that enhances HIV-1 infection of T cells in trans has indicated a potentially important role for adhesion molecules in AIDS pathogenesis. A related molecule called DC-SIGNR exhibits 77% amino acid sequence identity with DC-SIGN. The DC-SIGN and DC-SIGNR genes map within a 30-kb region on chromosome 19p13.2-3. Their strong homology and… 

Figures and Tables from this paper

DC-SIGN (dendritic cell-specific ICAM-grabbing non-integrin) and DC-SIGN-related (DC-SIGNR): friend or foe?
The mapping of DC-SIGN and DC-R to chromosome 19p13.3 adjacent to the previously described C-type lectin, CD23 [the low-affinity receptor for immunoglobulin E (FcERII] is described, and the similar genomic organization of these three genes is discussed and consideration is given to the evolutionary duplications that may underlie this arrangement.
HIV-1 Transmission by Dendritic Cell-specific ICAM-3-grabbing Nonintegrin (DC-SIGN) Is Regulated by Determinants in the Carbohydrate Recognition Domain That Are Absent in Liver/Lymph Node-SIGN (L-SIGN)*
Determinants in dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) necessary for human immunodeficiency virus, type 1 (HIV-1), transmission are identified and suggest that DC-SIGN structural elements distinct from the oligosaccharide-binding site are required for HIV-1 glycoprotein selectivity.
Low expression of dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin-related protein in non-Hodgkin lymphoma and significant correlations with lactic acid dehydrogenase and β2-microglobulin.
The results suggest that DC-SIGNR is a biological molecule that may be potentially useful in NHL clinical settings, and there is no statistically significant correlation between serum DC- SIGNR levels and clinical data such as sex, Ann Arbor stage, B symptoms, and histologic subtypes.
Characterization of DC-SIGN/R Interaction with Human Immunodeficiency Virus Type 1 gp120 and ICAM Molecules Favors the Receptor's Role as an Antigen-Capturing Rather than an Adhesion Receptor
The pH dependence in DC-SIGN binding to gp120 showed that the receptor retained high-affinity gp120 binding at neutral pH but lost gp120binding at pH 5, suggesting a release mechanism of HIV in the acidic endosomal compartment by DC-sign.
Functional Evaluation of DC-SIGN Monoclonal Antibodies Reveals DC-SIGN Interactions with ICAM-3 Do Not Promote Human Immunodeficiency Virus Type 1 Transmission
In vitro data indicate that DC-SIGN interactions with ICAM-3 do not promoteDC-SIGN-mediated virus transmission, and the role of intercellular contact in facilitating HIV-1 transmission may not be dependent solely on DC- SIGN.
Leukocyte Reaction Dendritic Cell Stimulation of the Mixed for Human Lymph Node and Is Not Required Abundant on Macrophages in the Normal Molecule 3-Grabbing Nonintegrin/CD209 Is Dendritic Cell-Specific Intercellular Adhesion
Results indicate that DC-SIGN has the potential to contribute to macrophage function in normal human lymph node, and that DCs do not requireDC-SIGN to transmit HIV or to initiate T cell responses.
Overexpression of dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin-related protein in cervical cancer and correlation with squamous cell carcinoma antigen
The results of the present study demonstrate that DC-SIGNR is overexpressed in cervical cancer tissue, and suggest that Washington cell-specific intercellular adhesion molecule-3-grabbing nonintegrin-related protein could serve as a biomarker for the early diagnosis of cervical cancer.
Binding of Human Immunodeficiency Virus Type 1 to Immature Dendritic Cells Can Occur Independently of DC-SIGN and Mannose Binding C-Type Lectin Receptors via a Cholesterol-Dependent Pathway
It is proposed that pathways to HIV-1 attachment and uptake in DC exhibit functional redundancy; that is, they are made up of multiple independent activities that can, at least in part, compensate for one another.


Cutting Edge: DC-SIGN; a Related Gene, DC-SIGNR; and CD23 Form a Cluster on 19p131 2
The genomic organization of DC-SIGN is reported and it is mapped to chromosome 19p13 adjacent to the C-type lectin CD23 (FcεRII) and a novel, closely linked gene, DC-signR, which shows 73% identity to DC- SIGN at the nucleic acid level and a similar genomic organization is reported.
Identification of DC-SIGN, a Novel Dendritic Cell–Specific ICAM-3 Receptor that Supports Primary Immune Responses
DC-SIGN, a Dendritic Cell–Specific HIV-1-Binding Protein that Enhances trans-Infection of T Cells
Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor alpha
Cultured DCs are as efficient as antigen-specific B cells in presenting tetanus toxoid (TT) to specific T cell clones and their efficiency of antigen presentation can be further enhanced by specific antibodies via FcR- mediated antigen uptake.
Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120.
Data demonstrate that the gp120-binding protein is a membrane-associated mannose-binding lectin, which may play an important role in the CD4-independent association of HIV with cells.
Cytoplasmic tails of beta 1, beta 2, and beta 7 integrins differentially regulate LFA-1 function in K562 cells.
Data demonstrate that distinct signaling routes activate beta 1 and beta 2 integrins through the beta-chain and hint at the involvement of lymphocyte-specific signal transduction elements in beta 2 and beta 7 integrin activation that are absent in the nonlymphocytic cell line K562.
The mannose receptor mediates induction of IFN-alpha in peripheral blood dendritic cells by enveloped RNA and DNA viruses.
It is demonstrated that stimulation of IFN-alpha synthesis by HSV is inhibited by a number of monosaccharides, including fucose, N- acetylglucosamine, and N-acetylgalactosamine as well as the yeast polysaccharide mannan, supporting a role for lectin(s) in theIFN- alpha stimulation pathway.
Macrophage recognition of ICAM-3 on apoptotic leukocytes.
Results show that ICAM-3 can function as a phagocytic marker of apoptotic leukocytes on which it acquires altered macrophage receptor-binding activity.
Lectin-carbohydrate interactions and infectivity of human immunodeficiency virus type 1 (HIV-1).
ConA neutralized HIV-1 infectivity for monocytic U937 as well as for lymphoid CEM cells, and behaves like neutralizing antibodies which do not interfere with CD4 binding of gp120 but rather with some later event that leads to virus entry.
High frequency of adhesion defects in B-lineage acute lymphoblastic leukemia.
A new fluorescent beads adhesion assay is developed that facilitates flow cytometric investigation of lymphocyte function-associated antigen 1 (LFA-1)- and very late activation antigen-4 (VLA-4)-mediated functional adhesion in B-lineage acute lymphoblastic leukemia (ALL).