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Blood, 15 June 2007, Vol. 109, No. 12, pp. 5337-5345. Prepublished online as a Blood First Edition Paper on March 5, 2007; DOI 10.1182/blood-2006-09-048058. This Article Full Text (PDF) All Versions of this Article: blood-2006-09-048058v1 109/12/5337    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Dominguez-Soto, A. Articles by Corbi, A. L Search for Related Content PubMed PubMed Citation Articles by Dominguez-Soto, A. Articles by Corbi, A. L Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted September 21, 2006 Accepted February 23, 2007 The DC-SIGN-related lectin LSECtin mediates antigen capture and pathogen binding by human myeloid cells Angeles Dominguez-Soto, Laura Aragoneses-Fenoll, Enrique Martin-Gayo, Lorena Martinez-Prats, Maria Colmenares, Marisa Naranjo-Gomez, Francesc E Borras, Pilar Munoz, Mercedes Zubiaur, Maria L Toribio, Rafael Delgado, and Angel L Corbi* Centro de Investigaciones Biologicas, CSIC, Madrid, Spain Centro de Biologia Molecular "Severo Ochoa", CSIC, Madrid, Spain Hospital Doce de Octubre, Madrid, Spain Hospital Universitari Germans Trias i Pujol, Badalona, Spain Instituto de Parasitologia y Biomedicina, CSIC, Granada, Spain * Corresponding author; email: acorbi{at}cib.csic.es. LSECtin (CLEC4G) is a C-type lectin encoded within the L-SIGN/DC-SIGN/CD23 gene cluster. LSECtin expression has been previously described as restricted to sinusoidal endothelial cells of liver and lymph node. We now report LSECtin expression in human peripheral blood and thymic dendritic cells isolated ex vivo. LSECtin is also detected in monocyte-derived macrophages and dendritic cells at the RNA and protein level. In vitro, IL-4 induces the expression of three LSECtin alternatively spliced isoforms, including a potentially soluble form (2 isoform) and a shorter version of the prototypic molecule (3/4 isoform). LSECtin functions as a pathogen receptor, as its expression confers Ebola virus-binding capacity to leukemic cells. Sugar binding studies indicate that LSECtin specifically recognizes N-Acetyl-Glucosamine, whereas no LSECtin binding to Mannan- or N-Acetyl-Galactosamine-containing matrices is observed. Antibody- or ligand-mediated engagement triggers a rapid internalization of LSECtin, which is dependent on tyrosine- and diglutamic-containing motifs within the cytoplasmic tail. Therefore, LSECtin is a pathogen-associated molecular pattern receptor in human myeloid cells. In addition, our results suggests that LSECtin participates in antigen uptake and internalization, and might be a suitable target molecule in vaccination strategies. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. K. Azad, J. B. Torrelles, and L. S. Schlesinger Mutation in the DC-SIGN cytoplasmic triacidic cluster motif markedly attenuates receptor activity for phagocytosis and endocytosis of mannose-containing ligands by human myeloid cells J. Leukoc. Biol., December 1, 2008; 84(6): 1594 - 1603. [Abstract] [Full Text] [PDF] K. Elvevold, B. Smedsrod, and I. Martinez The liver sinusoidal endothelial cell: a cell type of controversial and confusing identity Am J Physiol Gastrointest Liver Physiol, February 1, 2008; 294(2): G391 - G400. [Abstract] [Full Text] [PDF] A. S. Powlesland, T. Fisch, M. E. Taylor, D. F. Smith, B. Tissot, A. Dell, S. Pohlmann, and K. Drickamer A Novel Mechanism for LSECtin Binding to Ebola Virus Surface Glycoprotein through Truncated Glycans J. Biol. Chem., January 4, 2008; 283(1): 593 - 602. [Abstract] [Full Text] [PDF]

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