| Scleroderma sichuanensis Xiao(Hymenoptera:Bethylidae) is an idiobiont ectoparasitoids, which has Significant value in controlling wood-boring insects such as longhorn beetle. It doesn’t have calyx region and its venom sac accounting for a large proportion in female genital system, so venom may play important roles in parasitism. This paper does the research on Scleroderma sichuanensis Xiao-Tenebrio molitor L, be aimed at pilot studying effects of paralysis, nutrition regulation and bacteriostasis in venom. Pilot study of Physicochemical properties and isolation of paralyzed factors of venom also have been done. The results were summarized as follows:1Effects of venom on Tenebrio molitor L pupae paralyzed and ecdysis inhibitedParalysis degree had a postive correlation with content of venom injection. Tenebrio molitor L pupae showed slight and reversible paralysis as it was injected0.01VRE (venom reservoir equivalent) venom artificially. It wasn’t completely paralyzed and could move, make insensitive and inhibited respond to stimulation. It could get rid of paralysis and show the same as control after24h. The host appeared nonreversible and complete paralysis when the concentration of venom was risen to0.2VRE from0.03VRE. There were no differences in paralysis from0.05VRE to0.3VRE(P>0.05). When Tenebrio molitor L pupae was envenomed by Scleroderma sichuanensis Xiao, the ones recover from paralysis cloud Continued to develop and fail to molting, to become a monster of pupa-imago transition,whereas the others couldn’t recover from paralysis may keep paralytic until dead.2Effects of nutrition regulation of Tenebrio molitor L pupae envenomed and parasitizedIt had a notable decrease of lipid level in the haemolymph of Tenebrio molitor L pupae at3th day(P<0.05), and it decreased78.24%compared with the control. The contents of glycogen, trehalose,reducing sugar,protein in haemolymph, protein and lipid in fat body were not significantly different between venom injected and control(P>0.05).It had a notable decrease of glycogen and trehalose level at1～3day(P<0.05), whereas protein in the haemolymph of Tenebrio molitor L pupae level at2～5day(P<0.05). The contents of reducing sugar had increased significantly at3～6day. The contents of protein and lipid in fat body were not significantly different compared with the control(P>0.05).Result of SDS-PAGE showed that components in haemolymph of Tenebrio molitor L pupae didn’t have been distinctly changed after envenomed and parasitism. Scleroderma sichuanensis Xiao didn’t have an addiction in any of protein of in the haemolymph of Tenebrio molitor L pupae. There wasn’t any specific-peptide which had been reported before,either.3Bacteriostasis of venom from Scleroderma sichuanensis XiaoResults of injection of blend of venom and bacteria showed that venom could postpone humoral melanization in Tenebrio molitor L pupae because the infection from bacteria. It had a great difference between blend contain venom and bacteria and bacteria alone injected in48h(P<0.05).Results of bacteriostatic ring research showed that0.5VRE venom could inhibit developments of Escherichia coli and Staphylococcus aureus. It had a stronger restraining effect to Staphylococcus aureus than to Escherichia coli(P<0.05).4Physicochemical properties and isolation of paralyzed factors of venom from Scleroderma sichuanensis XiaoResults of research showed that the paralyzed factors is one of the proteins of venom, and it never lose activity under the condition:30～50℃, pH4.94～9.18,0.2～1.2M salting strength, normal hexane mixed. However its activity was eliminated when above60℃and trichloromethane-ethylalcohol putting in. The restraining effect to Staphylococcus aureus may disappear when above80℃whereas the restraining effect to Escherichia coli was still maintained at60～100℃. The inhibitor to Staphylococcus aureus may not be the same thing as that to Escherichia coli.Three high absorption zones of ultravilet (Vn.1,Vn.2, Vn.3)appeared after gel filtration chromatography (Sephadex G-75). There were factors cause paralysis in Vn.2and Vn.3,but because of similar physicochemical properties, proteins in Vn.2and Vn.3were difficult to isolate and purify. |
PDF Full Text Request