Entomopathogenic nematode Steinernema carpocapsae secreted protease role on host immune suppression Natesan Bala subramanian, Duarte Toubarro and Nelson Simes CIRN and Department of Biology, University of Azores , 9500-801 Ponta Delgada , Portugal . Steinernema carpocapsae is an entomopathogenic nematode symbiotically associated with the bacterium Xenorhabdus nematophila . This nematode secrete proteases on there secrete products. Proteases are well known catabolic functions and many tasks imposed by a parasitic life cycle. Serine proteases are the most extensively studied enzymes on host parasite interaction. Host defence mechanism including cellular and humoral reactions against invading organisms. In humoral system phenoloxidase is a key enzyme and c onsidering the parasite survival it may inhibit prophenoloxidase system, could be a key to successful parasitism. In order to study host immune suppression, the in fective third-stage (L3) S. carpocapsae nematodes were grown on 1% Galleria mellonella insect homogenate and then collect secretory products (SP). From the SP trypsin (Sc-TRYP) and chymo trypsin (Sc-CHYM) -like serine protease were identified, purified and characterized. I n vitro, 52.6 % and 63.7% prophenoloxidase suppression was observed for Sc-TRYP and Sc-CHYM respectively. Sc-TRYP could affect G. mellonella insect haemocyte causing cells to become spherical or round shape and actin filaments were detected with Phalloidintetramethylrhodamine showed some of them were disorganised in haemocytes. Sc-chym gene expression was analysed with induced and non induced insect homogenate for 6
to72 h. In vivo , purified Sc-CHYM imbibed beads showed, it could prevent haemocytes encapsulation and melanization by 12 and 24 h, respectively. The role of these proteases in host immune suppression will be discussed.