The C Type Lectins DC-SIGN and L-SIGN: Receptors for Viral Glycoproteins

Lozach, Pierre‐Yves; Burleigh, Laura; Staropoli, Isabelle; Amara, Ali

doi:10.1385/1-59745-393-5:51

Cited by 19 publications

(24 citation statements)

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“…In this study, we have, for the first time, cloned and characterized the complete cDNA as well as the gene of pDC-SIGN, characterized its tissue and cellular distribution, showed cross-interactions between pDC-SIGN and human ICAM-3 and between pDC-SIGN and human ICAM-2, and demonstrated the enhancement of PRRSV transmission to target cells in trans by pDC-SIGN. Human DC-SIGN and related homologues have become attractive targets for their important roles in various immune responses including mediating DCs adhesion, migration, inflammation, activating primary T cell, and for their interactions with various pathogens as well as involvement in immune escape of the pathogens [5][6][7]13,14,26,32]. To establish a small animal model for DC-SIGN research, mouse DC-SIGN homologues, from SIGNR1 to SIGNR8, were screened from the available mouse genome or expressed sequence tag (EST) databases and subsequently cloned by RT-PCR [19,22].…”

Section: Discussionmentioning

confidence: 99%

“…Since their identifications, DC-SIGN and L-SIGN have generated considerable interests for their ability to bind and uptake pathogens including viruses, bacteria (Mycobacterium), fungi and parasites in vitro [13]. A broad spectrum of enveloped viruses including Retroviridae (human immunodeficiency virus, simian immunodeficiency virus and feline immunodeficiency virus), Flaviviridae (Dengue virus, West Nile virus and hepatitis C virus), Filoviridae (Ebola and Marburg virus), Coronaviridae (SARS-CoV), Togaviridae (Sindbis virus) and Herpesviridae (human cytomegalovirus), has been reported to use DC-SIGN and/or L-SIGN as recognition and adhesion receptor for enhanced infection in vitro [14]. DC-SIGN/L-SIGN contain C-type-lectin-specific carbohydrate recognition domain (CRD) that tightly binds asparagines-linked high mannose glycans in viral enveloped glycoproteins in a calcium (Ca 2+ )-dependent manner [15].…”

Section: Introductionmentioning

confidence: 99%

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Porcine DC-SIGN: Molecular cloning, gene structure, tissue distribution and binding characteristics

Huang

Dryman

Wen

et al. 2009

Developmental & Comparative Immunology

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DC-SIGN, a human C-type lectin, is involved in the transmission of many enveloped viruses. Here we report the cloning and characterization of the cDNA and gene encoding porcine DC-SIGN (pDC-SIGN). The full-length pDC-SIGN cDNA encodes a type II transmembrane protein of 240 amino acids. Phylogenetic analysis revealed that pDC-SIGN, together with bovine, canis and equine DC-SIGN, are more closely related to mouse SIGNR7 and SIGNR8 than to human DC-SIGN. pDC-SIGN has the same gene structure as bovine, canis DC-SIGN and mouse SIGNR8 with eight exons. pDC-SIGN mRNA expression was detected in pig spleen, thymus, lymph node, lung, bone marrow and muscles. pDC-SIGN protein was found to express on the surface of monocyte-derived macrophages and dendritic cells, alveolar macrophages, lymph node sinusoidal macrophage-like, dendritic-like and endothelial cells but not of monocytes, peripheral blood lymphocytes or lymph node lymphocytes. A BHK cell line stably expressing pDC-SIGN binds to human ICAM-3 and ICAM-2 immunoadhesins in a calcium-dependent manner, and enhances the transmission of porcine reproductive and respiratory syndrome virus (PRRSV) to target cells in trans. The results will help better understand the biological role(s) of DC-SIGN family in innate immunity during the evolutionary process.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Porcine DC-SIGN: Molecular cloning, gene structure, tissue distribution and binding characteristics

Huang

Dryman

Wen

et al. 2009

Developmental & Comparative Immunology

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“…Both soluble DC-SIGN and anti-DC-SIGN antibodies inhibit infection [64,65]. However, recent studies suggest that DC-SIGN is not the actual receptor and may be acting as an attachment molecule [63]. Cryo-EM reconstruction of DC-SIGN in complex with DEN-2 E protein propose Asn 67 as to the primary site for interaction with the DEN-2 E protein [69].…”

Section: Current Targetsmentioning

confidence: 99%

Focus on Flaviviruses: Current and Future Drug Targets

et al. 2009

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Background Infection by mosquito-borne flaviviruses (family Flaviviridae) is increasing in prevalence worldwide. The vast global, social and economic impact due to the morbidity and mortality associated with the diseases caused by these viruses necessitates therapeutic intervention. There is currently no effective clinical treatment for any flaviviral infection. Therefore, there is a great need for the identification of novel inhibitors to target the virus lifecycle. Discussion In this article, we discuss structural and nonstructural viral proteins that are the focus of current target validation and drug discovery efforts. Both inhibition of essential enzymatic activities and disruption of necessary protein–protein interactions are considered. In addition, we address promising new targets for future research. Conclusion As our molecular and biochemical understanding of the flavivirus life cycle increases, the number of targets for antiviral therapeutic discovery grows and the possibility for novel drug discovery continues to strengthen.

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“…DC-SIGN has been focused for its ability to bind a variety of pathogens. Several viruses including human immunodeficiency virus type-1, measles virus, and West Nile virus are shown to bind to DC-SIGN through the envelope glycoproteins [4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Activation of p38 MAPK Pathway by Hepatitis C Virus E2 in Cells Transiently Expressing DC-SIGN

Chen

Zhu

Bian

et al. 2009

Cell Biochem Biophys

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Dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) is a cellular receptor for hepatitis C virus for the binding of viral envelope glycoprotein E2. Interaction of DC-SIGN with the E2 may evoke cellular signal transduction implicated in viral pathogenesis. We developed a cell model with DC-SIGN transient transfection to study p38 mitogen-activated protein kinase (MAPK) signaling pathway in response to the E2 treatment. HEK293T and HeLa were DC-SIGN-deficient cell lines. DC-SIGN was detectable at the surface of HEK293T and HeLa transfected with DC-SIGN, and the levels of DC-SIGN were high in transfected-HEK293T as compared with HeLa. The transfected-HEK293T displayed ability for the E2 binding. In the transfected-HEK293T, level of p38 MAPK phosphorylation was increased upon the E2 treatment and reduced following blockage of DC-SIGN with an antibody against DC-SIGN. Phosphorylation of downstream transcription factor activating transcription factor (ATF)-2 was also up-regulated by the E2 via DC-SIGN. Similar results were obtained with NIH3T3 cells stably expressing DC-SIGN and Huh7 cells. Our results indicate that DC-SIGN transient expression in HEK293T is a useful cell model for investigating p38 MAPK pathway triggered by the E2, which may provide information for understanding cellular receptors-mediated signaling events and the viral pathogenesis.

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The C Type Lectins DC-SIGN and L-SIGN: Receptors for Viral Glycoproteins

Cited by 19 publications

References 0 publications

Porcine DC-SIGN: Molecular cloning, gene structure, tissue distribution and binding characteristics

Porcine DC-SIGN: Molecular cloning, gene structure, tissue distribution and binding characteristics

Focus on Flaviviruses: Current and Future Drug Targets

Activation of p38 MAPK Pathway by Hepatitis C Virus E2 in Cells Transiently Expressing DC-SIGN

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