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Cotesia vestalis parasitization suppresses expression of a Plutella xylostella thioredoxin
- Shi, M., Zhao, S., Wang, Z‐H., Stanley, D., Chen, X.‐X.
- Insect molecular biology 2016 v.25 no.6 pp. 679-688
- Bracovirus, Cotesia, Malpighian tubules, Plutella xylostella, amino acids, cell proliferation, complementary DNA, fat body, genes, hemostasis, humans, insulin, isoelectric point, kidneys, larvae, molecular weight, open reading frames, parasitism, parasitoids, proteins, reactive oxygen species, supercoiled DNA, thioredoxins, toxicity, viruses
- Thioredoxins (Trxs) are a family of small, highly conserved and ubiquitous proteins involved in protecting organisms against toxic reactive oxygen species. In this study, a typical thioredoxin gene, PxTrx, was isolated from Plutella xylostella. The full‐length cDNA sequence is composed of 959 bp containing a 321 bp open reading frame that encodes a predicted protein of 106 amino acids, a predicted molecular weight of 11.7 kDa and an isoelectric point of 5.03. PxTrx was mainly expressed in larval Malpighian tubules and the fat body. An enriched recombinant PxTrx had insulin disulphide reductase activity and stimulated Human Embryonic Kidney 293 (HEK293) cell proliferation. It also protected supercoiled DNA and living HEK293 cells from H₂O₂‐induced damage. Parasitization by Cotesia vestalis and injections of 0.05 and 0.01 equivalents of C. vestalis Bracovirus (CvBv), the symbiotic virus carried by the parasitoid, led to down‐regulation of PxTrx expression in host fat body. Taken together, our results indicate that PxTrx contributes to the maintenance of P. xylostella cellular haemostasis. Host fat body expression of PxTrx is strongly attenuated by parasitization and by injections of CvBv.