A cDNA of novel immulectin homologue (BmIML), a C-type lectin, was cloned from the silkworm, Bombyx mori. The immulectin cDNA is an open reading frame of 921 bp encoding 307 amino acid residues. The deduced amino acid sequence from the BmIML cDNA contains two C-type carbohydrate recognition domains (CRDs). The BmIML was most similar (61 % protein sequence identity) to the M. sexta immulectin-1, whereas BmIML showed relatively lower identity to the B. mori lipopolysaccharide-binding protein (25% protein sequence identity). These features of BmIML indicate that BmIML is a novel member of C-type lectin superfamily. Northern blot analysis revealed that the BmIML is specifically expressed in the fat body of B. moli larvae.