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INHIBITORY PROPERTIES OF <i>MICROPLITIS CROCEIPES</i> TERATOCYTE SECRETORY PRODUCTS AND THE RECOMBINANT PROTEIN TSP14 ON PROTEIN SYNTHESIS

Microplitis croceipes is a solitary endoparasitic wasp that oviposits in the hemocoel of Heleothis virescens larvae. Upon parasitization, the host larvaes physiology is altered; resulting in a compromised immune system and a decrease in the production of some vital proteins resulting in a terminal post-wandering prepupal state. Teratocytes, cells derived from the extraembryonic serosa of the parasitic wasp, mimic symptoms of parasitization when injected into host larvae, independent of other factors like polydnavirus and venom. Some of the inhibition of protein synthesis can be attributed to proteins secreted by the teratocytes (teratocyte secretory proteins or TSP). A fraction of TSP between 330 kDa inhibits protein synthesis in vivo, in the in vitro fat body and testes assays, and in the rabbit reticulocyte lysate and wheat germ extract assays. This fraction, however, has no effect on nucleic acid synthesis. Its effect on protein synthesis is dose dependent and exposure time sensitive. A 13.9 kDa protein isolated from TSP and expressed in a baculovirus system seems primarily responsible for the inhibition. Although TSP14 production was low, it did bind to the cell surface, enter the cell, and inhibit protein synthesis as the 330 kDa factor did.

Identiferoai:union.ndltd.org:uky.edu/oai:uknowledge.uky.edu:gradschool_theses-1283
Date01 January 2003
CreatorsDiLuna, Francis Anthony
PublisherUKnowledge
Source SetsUniversity of Kentucky
Detected LanguageEnglish
Typetext
Formatapplication/pdf
SourceUniversity of Kentucky Master's Theses

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