Insects 2011, 2(4), 509-514; https://doi.org/10.3390/insects2040509
Inhibition of Melanization by a Parasitoid Serine Protease Homolog Venom Protein Requires Both the Clip and the Non-Catalytic Protease-Like Domains
School of Biological Sciences, The University of Queensland, St. Lucia QLD 4072, Australia
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Received: 18 October 2011 / Revised: 10 November 2011 / Accepted: 15 November 2011 / Published: 25 November 2011
(This article belongs to the Special Issue Symbiosis: A Source of Evolutionary Innovation in Insects)
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Abstract
Endoparasitoid wasps inject a variety of components into their host hemocoel at oviposition to facilitate successful development of their progeny. Among these are venom proteins which have been shown to play crucial roles in host regulation. A serine protease homolog (SPH)-like venom protein from Cotesia rubecula was previously shown to inhibit melanization in the host hemolymph by blocking activation of prophenoloxidase to phenoloxidase, a key enzyme in melanin formation. Similar to other SPHs, Vn50 consists of a clip and a protease-like (SPL) domain. Protein modeling demonstrated that Vn50 has a very similar structure to known SPHs and functional analysis of Vn50 domains expressed in insect cells indicated that neither of the domains on its own has an inhibitory effect on melanization. View Full-TextKeywords:
Cotesia rubecula; Vn50; prophenoloxidase; melanization; clip domain; serine protease homolog
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Thomas, P.; Asgari, S. Inhibition of Melanization by a Parasitoid Serine Protease Homolog Venom Protein Requires Both the Clip and the Non-Catalytic Protease-Like Domains. Insects 2011, 2, 509-514.