Purification, characterization, and cDNA cloning of a galactose-specific C-type lectin from Drosophila melanogaster.

We purified a lectin from a pupal extract of Drosophila melanogaster. This lectin agglutinated trypsinized and glutaraldehyde-fixed bovine red blood cells in the presence of calcium or magnesium. The hapten sugar of this lectin was galactose. The molecular mass of the intact lectin was determined to be 41 kDa, and it comprised 14- and 17-kDa subunits. The 17-kDa subunit was shown to be a glycosylated form of the 14-kDa subunit. Analysis of the cDNA for this lectin revealed that the 14-kDa subunit consists of 163 amino acid residues and contains all residues conserved in various C-type lectins. It was suggested that the Drosophila lectin and Sarcophaga lectin share some properties and function similarly in defense and development, but probably they are not structural homologues.