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Isolation and characterization of a novel venom protein from an endoparasitoid, Cotesia rubecula (Hym: Braconidae)
Author(s) -
Asgari Sassan,
Zareie Reza,
Zhang Guangmei,
Schmidt Otto
Publication year - 2003
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.10088
Subject(s) - braconidae , biology , hemolymph , prophenoloxidase , venom , immune system , host (biology) , microbiology and biotechnology , innate immune system , botany , immunology , genetics , biochemistry , parasitoid
Insects are important vectors of diseases with remarkable immune defense capabilities. Hymenopteran endoparasitoids are adapted to overcome the host defense system and, therefore, are useful sources of immune‐suppressing proteins. Not much is known about venom proteins in endoparasitoids, especially those that have a functional relationship with polydnaviruses (PDVs). Here, we describe the isolation and characterization of a small venom protein (Vn4.6) from an endoparasitoid, Cotesia rubecula , which interferes with the activation of the host hemolymph prophenoloxidase. The coding region for Vn4.6 is located upstream in the opposite direction of a gene coding for a C. rubecula PDV‐protein (Crp32). Arch. Insect Biochem. Physiol. 53:92–100, 2003. © 2003 Wiley‐Liss, Inc.