cDNA cloning and expression of bacteria-induced Hdd11 gene from eri-silkworm, Samia cynthia ricini.
A cDNA clone encoding Hdd11 protein, a bacteria-induced protein of unknown function, was isolated from fat body of immunized Samia cynthia ricini larvae based on suppression subtractive hybridization. The cDNA encodes a 167 amino acid residue open reading frame with an 18 residue predicted signal peptide. The deduced amino acid sequence showed 54% and 55% identity with Hdd11 proteins from Hyphantria cunea and Manduca sexta, respectively. Expression of the gene was undetectable in naive larvae when measured by Northern blot hybridization, but strongly induced in fat body after injecting bacterial cells or peptidoglycan into the larvae. The mRNA expression in the fat body was detected as early as 3 h post injection, reached peak levels at 12 h and continued for further 60 h at significant levels. The transcript was detected at very low levels in midgut, hemocytes and malpighian tubules.