Effects of the interaction between a clip domain serine protease and a white spot syndrome virus protein on phenoloxidase activity

Clip domain serine proteinases participate in invertebrate innate immunity by acting as crucial enzymes in the signaling cascade involved in shrimp immunity. To functionally characterize its role in Fenneropenaeus mer-guiensis, FmclipSP cDNA was cloned and characterized. The FmclipSP gene comprised 1353 bp with an open reading frame of 1110 bp and encoded 369 amino acids. The protein contained clip and serine protease domains. FmClipSP mRNA is highly expressed in hemocytes, and its expression was significantly upregulated by bacterial or viral pathogen challenge. Furthermore, FmClipSP recombinant protein (rFmClipSP) was produced and possessed protease activity, stimulating prophenoloxidase activity. Additionally, rFmClipSP exhibited antibac-terial activity against pathogens and nonpathogens. ELISA results demonstrated the binding ability of rFmClipSP to a recombinant protein of VP28 (rVP28). Interestingly, the binding significantly inhibited prophenoloxidase activity. Altogether, we partially characterized the function of FmclipSP and demonstrated its association with VP28. This study indicates the importance of clipSP as a component of F. merguiensis innate immunity. However, the role of clipSP in crustaceans remains unclear and requires further investigation.

Automated summary

This study partially characterized the function of FmclipSP and demonstrated its association with VP28. The results indicate the importance of FmclipSP in the innate immunity of F. merguiensis.