title: Early presence of an enolase in the oviposition injecta of the aphid parasitoid Aphidius ervi analyzed with chitosan beads as artificial hosts.
abstract: Maternal factors of female wasps that are injected into hosts with their eggs at oviposition play a major role in strategies used by insect parasitoids to overcome host immunity, and to regulate host physiology during early stages of parasitism. Here, we attempted to precisely determine and compare the protein patterns injected by the endoparasitoid Aphidius ervi into two different host systems. Chitosan beads of aphid size designed as artificial and physiologically inert hosts were used as oviposition medium, to be compared with the natural aphid host as young nymphs of Macrosiphum euphorbiae. Proteins that the A. ervi wasp injects into hosts at oviposition were separated by SDS-PAGE, complemented with proteomic techniques. Analyses confirm the identification of A. ervi γ-glutamyl transpeptidase (γ-GT) as a key component in the venom of the endoparasitoid. Using proteomic techniques, the quantity of γ-GT injected by the A. ervi wasp into aphids along with the egg was estimated as approximately 4ng per oviposition strike. We suggest that similar quantities suffice to explain natural parasitization success in A. ervi, which do not rely on polydnavirus to establish into hosts. Moreover, an enolase that showed a high level of sequence identity with teratocyte A. ervi enolase was detected both in chitosan beads extracts, and in extracts of mature eggs excised from the A. ervi ovaries, but not in its venom glands extracts. Detecting enolase shortly after oviposition in the artificial inert hosts at a stage of parasitism when the A. ervi egg is still in the primary chorionated undifferentiated stage suggests the enolase as a chorionic protein of the mature egg. The possible functions of this enolase enzyme for the establishment and early development of A. ervi in aphid hosts are discussed.
authors.affiliation: Institut de Biologie Intégrative et des Systèmes, Université Laval, Quebec, Canada G1V 0A6. thi-thuy-an.nguyen.1@ulaval.ca
authors.forename: Thi Thuy An
authors.initials: TT
authors.lastname: Nguyen
authors.forename: Isabelle
authors.initials: I
authors.lastname: Magnoli
authors.forename: Conrad
authors.initials: C
authors.lastname: Cloutier
authors.forename: Dominique
authors.initials: D
authors.lastname: Michaud
authors.forename: Frédéric
authors.initials: F
authors.lastname: Muratori
authors.forename: Thierry
authors.initials: T
authors.lastname: Hance
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001042:Aphids / Q000254:growth & development / Q000469:parasitology*; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D006790:Host-Parasite Interactions; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D010058:Oviposition; D010063:Ovum / Q000737:chemistry / Q000201:enzymology; D010751:Phosphopyruvate Hydratase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D040901:Proteomics / Q000295:instrumentation / Q000379:methods*; D014863:Wasps / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000502:physiology*; D005723:gamma-Glutamyltransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D019476:Insect Proteins; D005723:gamma-Glutamyltransferase; D010751:Phosphopyruvate Hydratase