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J. Biol. Chem., Vol. 277, Issue 15, 13091-13098, April 12, 2002

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Characterization of a Novel Drosophila melanogaster Galectin
EXPRESSION IN DEVELOPING IMMUNE, NEURAL, AND MUSCLE TISSUES^*

Karen E. Pace, Tim Lebestky^§, Thomas Hummel^¶, Pascal Arnoux, Kent Kwan, and Linda G. Baum^§**

From the  Department of Pathology and Laboratory Medicine, ^§ Molecular Biology Institute, ^¶ Howard Hughes Medical Institute, UCLA, Los Angeles, California 90095 and  Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada

We have cloned and characterized the first galectin to be identified in Drosophila melanogaster. The amino acid sequence of Drosophila galectin showed striking sequence similarity to invertebrate and vertebrate galectins and contained amino acids that are crucial for binding -galactoside sugars. Confirming its identity as a galectin family member, the Drosophila galectin bound -galactoside sugars. Structurally, the Drosophila galectin was a tandem repeat galectin containing two carbohydrate recognition domains connected by a unique peptide link. This divalent structure suggests that like mammalian galectins, Drosophila galectin may mediate cell-cell communication or facilitate cross-linking of receptors to trigger signal transduction events. The Drosophila galectin was very abundant in embryonic, larval, and adult Drosophila. During embryogenesis, Drosophila galectin had a unique and specific tissue distribution. Drosophila galectin expression was concentrated in somatic and visceral musculature and in the central nervous system. Similar to other insect lectins, Drosophila galectin may function in both embryogenesis and in host defense. Drosophila galectin was expressed by hemocytes, circulating phagocytic cells, suggesting a role for Drosophila galectin in the innate immune system.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF338142.

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