Dendritic Cell (DC)-specific Intercellular Adhesion Molecule 3 (ICAM-3)-grabbing Nonintegrin (DC-SIGN, CD209), a C-type Surface Lectin in Human DCs, Is a Receptor for LeishmaniaAmastigotes

Colmenares, Marı́a; Puig‐Kröger, Amaya; Pello, Óscar M.; Corbí, Ángel L.; Rivas, Luís

doi:10.1074/jbc.m205270200

Cited by 153 publications

(126 citation statements)

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“…CFSE-labeled parasites were added onto the cells at a 5:1 ratio, and cells were incubated at 37°C for 1 h. For inhibition experiments, cells were washed with PBS/1 mM EDTA and preincubated for 10 min at room temperature with MR-1 anti-DC-SIGN antibody (1.2 g/ml). Afterward, cells were fixed (1% paraformaldehyde in PBS) for 1 h at room temperature, and cells with and without attached parasites were resolved by flow cytometry in two peaks of low and high fluorescence intensity, using an EPICS-CS (Coulter Científica, Madrid, Spain), as described (8). (Fig.…”

Section: Methodsmentioning

confidence: 99%

“…Therefore, IL-4-up-regulated DC-SIGN on THP-1 cells participates in functionally relevant interactions with T lymphocytes. In addition, to evaluate the pathogen-binding function of DC-SIGN (29) on differentiated THP-1 cells, we measured the ability of bryostatin plus IL-4-treated cells to bind Leishmania amastigotes (8). THP-1 cells differentiated in the presence of IL-4 exhibited higher amastigote binding than the corresponding cells differentiated in the absence of IL-4 ( Fig.…”

Section: Il-4-treated Differentiated Thp-1 Cells Exhibit Dc-sign-depementioning

confidence: 99%

“…THP-1 cells differentiated in the presence of bryostatin and IL-4 were incubated with CFSE-labeled amastigotes at a 1:5 ratio at 37°C for 1 h, either in the presence or in the absence of an anti-DC-SIGN antibody or human polyclonal IgG. Cells were then fixed, and the percentage of cells with bound amastigotes determined by flow cytometry as described (8). D, identification of DC-SIGN isoforms in differentiated THP-1 cells.…”

Section: Fig 5 Dc-sign-dependent Functions Exhibited By Bryostatin mentioning

confidence: 99%

“…Structurally, DC-SIGN contains a carbohydrate-binding lectin domain, a "neck" region with seven 23-amino acid repeats, and a transmembrane region followed by a cytoplasmic tail with recycling and internalization motifs (1,5). DC-SIGN recognizes a large array of pathogens, including HIV (6), Ebola virus (7), Leishmania amastigotes (8), Mycobacterium tuberculosis (9,10), Schistosoma mansoni, Helicobacter pylori (11), and Candida (12) in a mannose or fucose-dependent manner (11,13,14). It is currently accepted that DC-SIGN mediates HIV capture by DC in peripheral tissues and enhances the infection in trans of cells expressing HIV receptors and co-receptors (6,15,16).…”

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confidence: 99%

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Regulated Expression of the Pathogen Receptor Dendritic Cell-specific Intercellular Adhesion Molecule 3 (ICAM-3)-grabbing Nonintegrin in THP-1 Human Leukemic Cells, Monocytes, and Macrophages

Puig‐Kröger

Serrano‐Gómez

Caparrós

et al. 2004

Journal of Biological Chemistry

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107

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Section: Methodsmentioning

confidence: 99%

Section: Il-4-treated Differentiated Thp-1 Cells Exhibit Dc-sign-depementioning

confidence: 99%

Section: Fig 5 Dc-sign-dependent Functions Exhibited By Bryostatin mentioning

confidence: 99%

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confidence: 99%

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Regulated Expression of the Pathogen Receptor Dendritic Cell-specific Intercellular Adhesion Molecule 3 (ICAM-3)-grabbing Nonintegrin in THP-1 Human Leukemic Cells, Monocytes, and Macrophages

Puig‐Kröger

Serrano‐Gómez

Caparrós

et al. 2004

Journal of Biological Chemistry

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107

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“…In addition to HIV, DC-SIGN was recently shown to bind a variety of microorganisms such as CMV [4], Ebola virus [5], Dengue virus [6], hepatitis C virus [7,8], simian immunodeficiency virus [9], Leishmania [10], Candida albicans [11], Mycobacterium [12][13][14] and Schistosoma [15]. Some pathogens subvert DC functions to escape immune surveillance [16].…”

Section: Introductionmentioning

confidence: 99%

Role of DC‐SIGN in the activation of dendritic cells by HPV‐16 L1 virus‐like particle vaccine

et al. 2006

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Dendritic cell-specific intercellular adhesion molecule-grabbing non-integrin (DC-SIGN), a specific C-type lectin expressed on DC, binds and transmits different pathogens to susceptible cells. In the present study, we examined the role of DC-SIGN in the capture of human papillomavirus (HPV) pseudovirions and activation of DC. We demonstrate that HPV virus-like particles (VLP) bind to DC-SIGN expressed on transfected Raji cells and that antibodies against DC-SIGN block this interaction. DC take up VLP, which activate expression of costimulatory markers and cytokines/ chemokines. Although our results indicate that DC-SIGN is not the major receptor for VLP in DC, this interaction contributes to the activation of DC surface antigens (HLA class I) and of various cytokines/chemokines, particularly TNF-a, IL-6, and RANTES. Induction of these markers in DC by VLP was significantly abrogated when binding to DC-SIGN was blocked by anti-DC-SIGN antibodies. These results suggest that DC-SIGN has a functional role in DC activation induced by HPV-16 L1-VLP, and thus highlight new aspects of DC interactions with HPV VLP. IntroductionThe C-type lectin dendritic cell-specific intercellular adhesion molecule-grabbing non-integrin (DC-SIGN; CD209) is a pathogen recognition receptor that interacts with mannose residues of glycoproteins in a calciumdependent manner via its C-terminal carbohydrate recognition domain [1,2]. DC-SIGN acts both as an adhesion molecule and pathogen recognition receptor, facilitating DC binding and internalization of several viruses, including HIV-1 [3].In addition to HIV, DC-SIGN was recently shown to bind a variety of microorganisms such as CMV [4], Ebola virus [5], Dengue virus [6], hepatitis C virus [7,8], simian immunodeficiency virus [9], Leishmania [10], Candida albicans [11], Mycobacterium [12][13][14] and Schistosoma [15]. Some pathogens subvert DC functions to escape immune surveillance [16]. DC-SIGN is abundantly expressed primarily on DC, including those derived from monocytes and those located beneath the genital surface [3].Human papillomavirus (HPV) virus-like particles (VLP) are a promising vaccine candidate for HPV and cervical cancer [17][18][19][20]. Recent clinical trials have shown that VLP afford excellent protection against persistent infection [20,21]. Because of the lack of a suitable cell culture system for in vitro propagation of HPV and the unavailability of virions, HPV VLP have been used as soluble surrogates for native virus particles. The routes of HPV-16 L1-VLP entry in DC and the nature of cellular receptors involved in capture have been studied but remain to be fully characterized. HPV VLP Here, we report that HPV-16 L1-VLP particles bind to DC-SIGN in transfected cell lines, and to a lesser extent in DC, and that this interaction participates in L1-VLPinduced activation of DC. Thus, DC-SIGN is likely involved in DC activation by HPV VLP. Results and discussion HPV L1-VLP bind to DC-SIGN in DC-SIGN-transfected cell linesTo study interactions between L1-VLP and DC-SIGN, we...

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Dendritic Cells in Leishmaniasis: Regulators of Immunity and Tools for New Immune Intervention Strategies

Moll¹

2006

Handbook of Dendritic Cells

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Dendritic Cell (DC)-specific Intercellular Adhesion Molecule 3 (ICAM-3)-grabbing Nonintegrin (DC-SIGN, CD209), a C-type Surface Lectin in Human DCs, Is a Receptor for LeishmaniaAmastigotes

Cited by 153 publications

References 31 publications

Regulated Expression of the Pathogen Receptor Dendritic Cell-specific Intercellular Adhesion Molecule 3 (ICAM-3)-grabbing Nonintegrin in THP-1 Human Leukemic Cells, Monocytes, and Macrophages

Regulated Expression of the Pathogen Receptor Dendritic Cell-specific Intercellular Adhesion Molecule 3 (ICAM-3)-grabbing Nonintegrin in THP-1 Human Leukemic Cells, Monocytes, and Macrophages

Role of DC‐SIGN in the activation of dendritic cells by HPV‐16 L1 virus‐like particle vaccine

Dendritic Cells in Leishmaniasis: Regulators of Immunity and Tools for New Immune Intervention Strategies

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