Immunoanalysis of unique protein in Trichoplusia ni larvae parasitized by the braconid wasp Chelonus near curvimaculatus |
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| Affiliation: | 1. Department of Entomology, University of Kentucky, Lexington, Kentucky, U.S.A.;2. Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky, U.S.A.;1. School of Biology & Basic Medical Science, Soochow University, Suzhou 215123, China;2. National Engineering Laboratory for Modern Silk, Soochow University, Suzhou 215123, China;1. The Graduate School, University of Santo Tomas, España, 1015, Manila, Philippines;2. Department of Biological Sciences, College of Science, University of Santo Tomas, España, 1015, Manila, Philippines;3. Research Center for the Natural and Applied Sciences, Molecular Biology and Biotechnology Laboratory, University of Santo Tomas, España, 1015, Manila, Philippines;1. Central University of Valle (UCEVA), Tuluá, Colombia;2. Colombian Sugarcane Research Center (Cenicaña), Cali, Colombia;3. National University of Colombia – Palmira Campus, Colombia;4. National University of Colombia – Bogotá Campus;5. Department of Entomology, Kansas State University, Agricultural Research Center-Hays, Hays, KS, USA |
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| Abstract: | Parasitization in insects brings about profound biochemical and physiological effects in the host which may include complete overriding of the normal endocrinological program, resulting in precocious metamorphosis and in blockage of pupal development. The subtle effects of parasitization include changes in the expression of hemolymph proteins and the appearance of proteins which are unique to parasitized hosts. One such protein has been identified in the hemolymph of Trichoplusia ni larvae parasitized by the braconid wasp Chelonus near curvimaculatus. In this study, purified preparations of the parasitism-specific protein were used to generate polyconal antibodies against the protein. Results from the immunocharacterization indicate the antibodies obtained are highly specific for the protein and are present in a high titer (1:8000 antiserum dilution yielded strong signals in analysis of the protein in 0.25 μl hemolymph). Subsequently, the expression of the parasitism-specific protein in the hemolymph and tissues was analyzed by immunoblotting during the entire course of development in normal and parasitized insects. The parasitism-specific protein was not detected in normal, unparasitized larvae. In parasitized insects, expression of the parasitism-specific protein appears to be stage-specific in that it is only detected during the last larval stadium of precociously metamorphosing larvae, but is absent from all earlier stages of development. |
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