The role of serine- and metalloproteases in Nasonia vitripennis venom in cell death related processes towards a Spodoptera frugiperda Sf21 cell line

- Venom of Nasonia vitripennis induces apoptosis in Sf21 cells.
- Both serine and metalloproteases are cytotoxic venom compounds.
- The activity of venom metalloproteases differs between adherent and suspension cells.
- Serine proteases in the venom are able to induce apoptosis.

Proteases are predominant venom components of the ectoparasitoid Nasonia vitripennis. Two protease families, serine proteases and metalloproteases were examined for their possible cytotoxic functions in the Spodoptera frugiperda (Sf21) cell line using protease inhibitors that inactivate one or both protease families. Viability assays on adherent cells indicated that both protease families are among the main cytotoxic compounds of N. vitripennis venom. However, viability assays and flow cytometry performed on suspension cells 24 h after envenomation revealed that inactivation of metalloproteases did not improve cell survival. These results indicate that both protease families may have tissue specific functions. Time course experiments indicate that serine proteases of N. vitripennis venom are responsible for inducing apoptosis in the Sf21 cell line. However, other venom compounds could also be involved in this process and different cell death pathways may take over when a specific type of cell death is inhibited. During parasitation of their natural hosts, both protease families may possibly function in immune related processes and tissue destruction, enabling venom distribution. Overall, this study provides important insights into the functions of serine and metalloproteases in the venom of N. vitripennis.