A new form of arthropod phenoloxidase is abundant in venom of the parasitoid wasp Pimpla hypochondriaca.

We have recently identified phenoloxidase (PO) activity among several biologically active factors in venom from the parasitoid wasp Pimpla hypochondriaca. We have now isolated three genes, designated POI, POII and POIII, from a cDNA library made from venom-producing glands and found that their products are related to pro-phenoloxidases (PPOs), which are expressed as proenzymes in haemocytes and which mediate immune processes in arthropods. This is the first report of PO as a venom constituent. Amino acid sequence comparisons between the three Pimpla POs and PPOs revealed several notable differences, including the absence of sequences which specify the site of proteolytic activation in insect PPOs and the unprecedented occurrence of signal peptide sequences. NH(2)-terminal amino acid analysis of PO purified from venom yielded a peptide sequence matching the predicted mature NH(2) termini of POI and POII, confirming the authenticity of the signal peptide and indicating that proteolytic processing, other than to remove the signal peptide, does not occur in the wasp. Expression of POI, analysed by Northern hybridization, was approximately uniform from the time of adult emergence to day 6 post-emergence, after which it declined. A novel means of host immune suppression, mediated by the unregulated activity of venom PO in the haemocoel, is proposed.