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A venom metalloproteinase from the parasitic wasp Eulophus pennicornis is toxic towards its host, tomato moth ( Lacanobia oleracae )
Author(s) -
Price D. R. G.,
Bell H. A.,
Hinchliffe G.,
Fitches E.,
Weaver R.,
Gatehouse J. A.
Publication year - 2009
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/j.1365-2583.2009.00864.x
Subject(s) - biology , venom , host (biology) , metalloproteinase , botany , ecology , matrix metalloproteinase , genetics
Three genes encoding clan MB metalloproteinases (EpMP1–3) were identified from venom glands of the ectoparasitic wasp Eulophus pennicornis . The derived amino acid sequences predict mature proteins of approximately 46 kDa, with a novel two‐domain structure comprising a C‐terminal reprolysin domain, and an N‐terminal domain of unknown function. EpMP3 expressed as a recombinant protein in Pichia pastoris had gelatinase activity, which was inhibited by EDTA. Injection of recombinant EpMP3 into fifth instar Lacanobia oleracea (host) larvae resulted in partial insect mortality associated with the moult to sixth instar, with surviving insects showing retarded development and growth. EpMP3 is expressed specifically in venom glands. These results suggest that EpMP3 is a functional component of Eulophus venom, which is able to manipulate host development.