Cloning and characterization of a lectin from the octocoral Sinularia lochmodes

Mitsuru Jimbo, Kazuhiko Koike, Ryuichi Sakai, Koji Muramoto, Hisao Kamiya

    Research output: Contribution to journalArticlepeer-review

    24 Citations (Scopus)


    In the present study, the entire amino acid sequence and cDNA structure encoding the d-galactose-binding lectin, SLL-2, isolated from the octocoral Sinularia lochmodes, were determined. SLL-2 regulates the morphology of symbiotic dinoflagellates Symbiodinium spp. through unknown mechanisms. Here, three cDNAs that encode SLL-2 were cloned and characterized. All the SLL-2 cDNAs encoded 142 amino acids with high similarity to each other. The mature subunit of SLL-2 was found to be composed of 94 amino acids and to contain one putative glycosylation site common to all three SLL-2. N-Glycopeptidase F treatment of SLL-2 resulted in a protein band shift from 16.5 to 9.5 kDa in SDS-PAGE, confirming that SLL-2s are glycoproteins. Two-dimensional polyacrylamide gel electrophoresis analysis of the deglycosylated SLL-2 indicated a presence of three polypeptides as encoded in SLL-2 cDNAs. The deduced sequences of SLL-2 cDNAs had a similarity to the C-terminal region of discoidin I, the slime mold Dictyostelium discoideum lectin.

    Original languageEnglish
    Pages (from-to)157-162
    Number of pages6
    JournalBiochemical and biophysical research communications
    Issue number1
    Publication statusPublished - 2005 Apr 29


    • D-Galactose-binding lectin
    • Discoidin
    • Octocoral
    • Sinularia lochmodes
    • Symbiodinium
    • Symbiosis
    • Symbiotic dinoflagellates

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Fingerprint Dive into the research topics of 'Cloning and characterization of a lectin from the octocoral Sinularia lochmodes'. Together they form a unique fingerprint.

    Cite this