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Characterization of a Novel Galactose-Binding Lectin Homologue from Tenebrio molitor

Authors: JiEun Jeong, Dae-Hyun Seog, Yong Seok Lee, Dong Hyun Kim, Bharat Bhusan Patnaik, Se Won Kang, HeeJu Hwang, Yong Hun Jo, YeonSooHan


An expressed sequence tag (EST) analysis provideus portions of expressed genes. We have constructed cDNA library and determined randomly sequences from cDNA library clones of T. molitor injected with acholeplasma lysate. We identified the homologous to a galectin gene. As the result of cloning and characterization of novel, we found that the protein has an open reading frame (ORF) of 495 bp, with 164 amino acid residues and molecular weight of 18.5 kDa. To characterize the role of novel Tm-galectin in immune system, we quantified the mRNA level of galectin at different times after treatment with immune elicitors. The galectin mRNA was up-regulated about 7-folds within 18 hrs. This suggests that Tm-galectin is a novel member of animal lectins, and has a role in the process of pathogen recognition. Our study would be helpful for the study on immune defense system and signaling cascade.

Keywords: Innate Immunity, Tenebrio molitor, EST, Galectin

Digital Object Identifier (DOI):

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[1] Park, J. W., 2006. A synthetic peptidoglycan fragment as a competitive inhibitor of the melanization cascade. J. Biol. Chem. 281, 7747-55.
[2] Yang, R., Rabinovich, G., Liu, F., 2008. Galectins: Structure, function and therapeutic potential. Expert Reviews in Molecular Medicine 10, 1–24
[3] Liu, F., Patterson, R.J., Wang, J.L., 2002. Intracellular functions of galectins. Biochimica et Biophysica Acta 1572, 263–273.
[4] Liu, F., 2010. "Galectins: Regulators of acute and chronic inflammation". Annals of the New York Academy of Sciences 1183, 158–182.
[5] Yang, R., Rabinovich, G., Liu, F., 2008. "Galectins: Structure, function and therapeutic potential". Expert Reviews in Molecular Medicine 10: 1–24.
[6] Fujita, T., 2002. Evolution of the lectin-complement pathway and its role in innate immunity. Nat. Rev. Immunol. 2, 346-353.
[7] Revillard, J.P., 2002. Innate immunity. Eur. J. Dermatol. 12, 224-227.
[8] Turner, M.W., 1996. Mannose-binding lectin: the pluripotent molecule of the innate immune system. Immunol. Today 17, 532.
[9] Jiang, R., Kim, E.H., Gong, J.H., Kwon, H.M., Kim, C.H., Ryu, K.H. et al. 2009. Three pairs of protease-serpin complexes cooperatively regulate the insect innate immune responses. J. Biol. Chem.284, 35652-35658.
[10] Yu, F., Finley, R.L Jr., Raz, A., Kim, H.R., 2002. Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation. J. Biol. Chem. 277, 15819-15827.