The gene vlp1 encodes a protein member of the phospholipid hydroperoxide glutathione peroxidases (PHGPx) family, but the active domain lacks an important cysteine and the protein has no enzymatic activity ( Hellers et al., 1996, Li et al., 2003). The genes encoding the 40-kDa protein, vlp1, the 52-kDa protein, vlp2, immunogically related to the 60-kDa protein, and vlp3 coding for a 80–94-kDa protein, have been cloned and characterized ( Asgari et al., 2002 Theopold et al., 1994 Hellers et al., 1996). VcVLPs have been isolated and analyzed, allowing identification of four major (35-, 40-, 52- and 60-kDa) and two minor proteins (80–94 kDa) ( Schmidt and Schuchmann-Feddersen, 1989). They are found together with VcVLPs in the lumen of the calyx region, and they are injected with the egg into the host larvae where they enter host hemocytes, suggesting a potential immune suppressive function ( Reineke and Asgari, 2005). The iflavirus particles form crystalline arrays composed of uniform non-enveloped particles of about 36 nm ( Fig. canescens were also reported to produce small RNA-containing virus particles (VcSRV), most likely belonging to the iflavirus family ( Reineke and Asgari, 2005). They are assembled within the nuclei of calyx gland cells ( Schmidt and Schuchmann-Feddersen, 1989) but they are devoid of nucleic acids ( Bedwin, 1979 Feddersen et al., 1986). canescens VLPs (VcVLPs) are 100–150-nm electron-dense particles surrounded by a membranous envelope, that morphologically resemble ichnoviruses ( Feddersen et al., 1986) ( Fig. The ovarian calyx region produces a viscous fluid containing proteins and virus-like particles that stick to the egg at oviposition ( Feddersen et al., 1986 Kinuthia et al., 1999). Venturia canescens (also named Nemeritis canescens) is an endoparasitoid wasp that deposits its eggs inside the larvae of pyralid moths such as Ephestia kuehniella (Lepidoptera: Phycitidae). Marylène Poirié, in Parasitoid Viruses, 2012 VLPs in Venturia canescens (Hymenoptera: Ichneumonidae)

Calyx point 10.2