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Inhibition of Melanization by a Parasitoid Serine Protease Homolog Venom Protein Requires Both the Clip and the Non-Catalytic Protease-Like Domains

Author(s): Pune Thomas | Sassan Asgari

Journal: Insects
ISSN 2075-4450

Volume: 2;
Issue: 4;
Start page: 509;
Date: 2011;
Original page

Keywords: Cotesia rubecula | Vn50 | prophenoloxidase | melanization | clip domain | serine protease homolog

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.

Tango Jona
Tangokurs Rapperswil-Jona

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