The surface carbohydrates of the Echinococcus granulosus larva interact selectively with the rodent Kupffer cell receptor
| Autor: | Gerardo Lin, Noriyasu Hada, Po Kai Chuang, Klaus Brehm, Akihiko Koizumi, Shie-Liang Hsieh, Tsui-Ling Hsu, Chi-Huey Wong, Alvaro Díaz |
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| Rok vydání: | 2013 |
| Předmět: |
Antigen presentation
Asialoglycoprotein Receptor Biology Echinococcus multilocularis Host-Parasite Interactions Polysaccharides parasitic diseases medicine Animals Humans Receptors Immunologic Echinococcus granulosus Receptor Molecular Biology Innate immune system Macrophages Cell Membrane Mucin Kupffer cell Mucins biology.organism_classification Immunity Innate medicine.anatomical_structure Echinococcus Biochemistry Larva Carbohydrate Metabolism Parasitology Protein Binding |
| Zdroj: | Molecular and Biochemical Parasitology. 192:55-59 |
| ISSN: | 0166-6851 |
| DOI: | 10.1016/j.molbiopara.2013.12.001 |
| Popis: | The larvae of the cestodes belonging to the genus Echinococcus dwell primarily in mammalian liver. They are protected by the laminated layer (LL), an acellular mucin-based structure. The glycans decorating these mucins constitute the overwhelming majority of molecules exposed by these larvae to their hosts. However, their decoding by host innate immunity has not been studied. Out of 36 mammalian innate receptors with carbohydrate-binding domains, expressed as Fc fusions, only the mouse Kupffer cell receptor (KCR; CLEC4F) bound significantly to the Echinococcus granulosus LL mucins. The receptor also bound the Echinococcus multilocularis LL. Out of several synthetic glycans representing Echinococcus LL structures, the KCR bound strongly in particular to those ending in Galα1-4Galβ1-3 or Galα1-4Galβ1-4GlcNAc, both characteristic LL carbohydrate motifs. LL carbohydrates may be optimized to interact with the KCR, expressed only in liver macrophages, cells known to contribute to the tolerogenic antigen presentation that is characteristic of this organ. |
| Databáze: | OpenAIRE |
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