A MnSOD gene was cloned from the fall webworm, H. cunea. The MnSOD cDNAs encode precursor proteins of 215 amino acid residues. The deduced amino acid sequences of the H. cunea MnSOD cDNA showed 76% identity to B. mori MnSOD and 62-56% to MnSOD sequences from other organisms. MnSOD and Cu/ZnSOD in H. cunea is expressed from all tissues. MnSOD expression is changed at a trace level in infected larvae, while Cu/ZnSOD expression is strongly changed against bacteria, and fungi. The expression level of Cu/ZnSOD increased by different artificial photoperiod (24L:0D), UV irradiation (312nm), and starvation condition, while the expression level of MnSOD only increased by starvation condition. Also, expression of MnSOD and Cu/ZnSOD showed no significant change in 0L:24D condition. In addition to expression levels of Cu/ZnSOD in H. cunea significantly increased by temperature stress and injection with paraquat, but reduced by injection with 10% H2O2. The expression level of MnSOD significantly increased by temperature stress and reduced by injection with 10% H2O2 and paraquat.

Reactive oxygen species (ROS) is toxic to living organisms, because its high reactivity causes oxidative damage to proteins, nucleic acids, and lipids. Superoxide dismutase (SOD) is an enzyme facilitating the removal of superoxide anions from living organisms. This study focused on the cloning of MnSOD cDNA from Hyphantria cuneaand its induction upon bacterial infection and various stresses. The open reading frame of MnSOD is composed of 645 bp, encoding 215 amino acid residues. The theoretical molecular mass and pI of putative MnSOD was evaluated to be 24276 Da and 9.14, respectively. The MnSOD from H. cunea is highly similar to human MnSOD (59.5%) as well as Bombyx mori MnSOD (76.2%). MnSOD showed no big induction upon bacterial infection and stresses, compared to that of Cu/ZnSOD.