Phenoloxidase-like activities and the function of virus-like particles in ovaries of the parthenogenetic parasitoid Venturia canescens.
The ichneumonid endoparasitoid Venturia canescens successfully develops inside the hemocoel of another insect by using maternal protein secretions, including nucleic acid-free virus-like particles (VLPs), to manipulate host physiology. These VLPs consist of four major proteins, which are produced mainly in the calyx tissue and transferred into the host insect together with the egg. One of the protein-coding genes (vlp1), with similarities to phospholipid-hydroperoxide glutathione peroxidases (PHGPx), exists in allelic forms producing two protein variants with different protein properties. Here, we summarise observations indicating that oocytes and eggs are the source of reactive electrons, which potentially damage the lining and membranes of calyx tissues. We discuss the possible role of VLP1 in counteracting the damaging effects of oxidised phospholipids on membranes surrounding VLPs in the calyx lumen.
Schmidt
Otto
O
Department of Applied and Molecular Ecology, Waite Campus, Adelaide University, Glen Osmond, SA 5064, Australia. otto.schmidt@adlaide.edu.au
Li
Dongmei
D
Beck
Markus
M
Kinuthia
Wanja
W
Bellati
Judy
J
Roberts
Harry L S
HL
D000818:Animals; D004583:Electrons; D005260:Female; D005979:Glutathione Peroxidase / Q000235:genetics / Q000378:metabolism*; D006790:Host-Parasite Interactions; D019476:Insect Proteins / Q000378:metabolism / Q000502:physiology*; D018613:Microscopy, Confocal; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D009036:Moths / Q000469:parasitology*; D010053:Ovary / Q000033:anatomy & histology / Q000378:metabolism / Q000502:physiology*; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D013194:Staining and Labeling; D014863:Wasps / Q000821:virology*
D019476:Insect Proteins; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D005979:Glutathione Peroxidase; D014442:Monophenol Monooxygenase