Superoxide dismutase from venom of the ectoparasitoid Scleroderma guani inhibits melanization of hemolymph

Superoxide dismutase (SOD) known as an important antioxidative stress protein has been recently found in venoms of several parasitoid wasps. However, its functions and characteristics as a virulent factor remain scarcely described. Here, we report the characterization of two venomous SOD genes (SguaSOD1 and SguaSOD3) from the ectoparasitoid, Scleroderma guani. The metal binding sites, cysteine amino acid positions and signature sequences of the SOD family were conserved within SguaSOD1 and SguaSOD3. Relatively high levels of their transcripts were observed in pupae followed a decrease in early adults, after which they had the highest transcriptions, indicating that their productions would be regulated in venom apparatus. Although the two genes showed lower expression in venom apparatus compared to head and thorax, the enzymatic assay revealed that SOD indeed had activity in venom. Further, we showed that recombinant SguaSOD3 suppressed melanization of host hemolymph, implying that this protein used as a virulent factor uniquely impacts the prophenoloxidase cascade. The functions and characteristics of superoxide dismutase (SOD) as a venom component of parasitoids remain scarcely described. Two venomous SOD genes (SguaSOD1 and SguaSOD3) were cloned from the ectoparasitoid, Scleroderma guani. The SOD enzymatic activity was detected in the venom of this parasitoid. Recombinant SguaSOD3 displayed the ability to inhibit the melanization of host hemolymph.