A C-type lectin from the Tunicate, Styela plicata, that modulates cellular activity

Sham V. Nair, Monika Burandt, Aimee Hutchinson, Robert L. Raison, David A. Raftos

    Research output: Contribution to journalArticlepeer-review

    18 Citations (Scopus)


    Previous studies have identified proteins from tunicates (invertebrate members of the Phylum Chordata) that have physicochemical and functional properties similar to those of the inflammatory cytokine, interleukin 1 (IL-1). Here we characterize one of those proteins from the tunicate, Styela plicata, that can stimulate tunicate and mammalian cell proliferation, activate phagocytosis, increase interleukin 2 (IL-2) secretion by mammalian peripheral blood mononuclear cells and enhance IL-2 receptor (IL-2R) expression by mammalian EL-4.IL-2 cells. Partial amino acid sequence data showed that the S. plicata protein resembles three C-type lectins (TC14, TC14-1 and TC14-2) from a closely related tunicate species, Polyandrocarpa misakiensis. Its similarity to carbohydrate recognition domains (CRDs) from P. misakiensis lectins suggests that the S. plicata protein modulates the activities of mammalian immunocompetent cells by interacting with carbohydrate moieties of glycosylated cell surface receptors.

    Original languageEnglish
    Pages (from-to)11-24
    Number of pages14
    JournalComparative Biochemistry and Physiology - C Toxicology and Pharmacology
    Issue number1
    Publication statusPublished - 2001


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