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Host regulation by the aphid parasitoid Aphidius ervi : the role of teratocytes
Author(s) -
Falabella Patrizia,
Tremblay Ermenegildo,
Pennacchio Francesco
Publication year - 2000
Publication title -
entomologia experimentalis et applicata
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.765
H-Index - 83
eISSN - 1570-7458
pISSN - 0013-8703
DOI - 10.1046/j.1570-7458.2000.00710.x
Subject(s) - parasitoid , biology , aphid , braconidae , host (biology) , aphididae , zoology , homoptera , pest analysis , ecology , botany
Abstract The biochemical profile and metabolism of Acyrthosiphon pisum (Harris) (Homoptera, Aphididae) are markedly altered and redirected in response to parasitization by the endophagous braconid Aphidius ervi Haliday (Hymenoptera, Braconidae). In the present study, the role played in the host regulation process by teratocytes, cells deriving from the dissociation of the embryonic membrane of the parasitoid, is taken into consideration. The protein synthesis activity of these cells of embryonic origin is analysed in vitro and an essential characterization of those proteins de novo synthesized and released in the incubation medium is provided. Teratocytes, obtained by dissecting parasitized host aphids, 3, 4 and 5 days after parasitoid oviposition, were incubated in vitro and, at the end of the incubation period, were separated from the medium for SDS‐PAGE analysis of both cellular and secreted proteins. Various cellular proteins were more abundant as the time between parasitization and teratocyte collection increased. Furthermore, two proteins, showing an approximate molecular mass of 15 kD (p15) and 45 kD (p45) respectively, were abundantly secreted in the incubation medium by 5 day‐old teratocytes. Incubations in presence of 35 S radiolabelled amino acids indicated that p15 and p45 are both synthesized by A. ervi teratocytes. The amino acid composition of these two proteins was similar to that reported for other insect proteins with a demonstrated nutritional function. The p45 protein was found to be glycosylated. A tentative physiological model describing the host regulation role played by different parasitoid‐derived factors is proposed.