Penaeus monodonThioredoxin Restores the DNA Binding Activity of Oxidized White Spot Syndrome Virus IE1
| العنوان: | Penaeus monodonThioredoxin Restores the DNA Binding Activity of Oxidized White Spot Syndrome Virus IE1 |
|---|---|
| المؤلفون: | Jiann Horng Leu, Geen-Dong Chang, Jiun Yan Huang, Guang Hsiung Kou, Han Ching Wang, Der-Yen Lee, Chu Fang Lo, Wang-Jing Liu, Shih-Ting Kang, Mong-Hsun Tsai, Hao-Ching Wang, I-Tung Chen |
| المصدر: | Antioxidants & Redox Signaling. 17:914-926 |
| بيانات النشر: | Mary Ann Liebert Inc, 2012. |
| سنة النشر: | 2012 |
| مصطلحات موضوعية: | animal structures, Physiology, viruses, Clinical Biochemistry, Mutant, Electrophoretic Mobility Shift Assay, Biochemistry, Cell Line, Penaeus monodon, law.invention, chemistry.chemical_compound, Thioredoxins, White spot syndrome virus 1, Penaeidae, law, Animals, Immunoprecipitation, Electrophoretic mobility shift assay, Molecular Biology, General Environmental Science, biology, virus diseases, Cell Biology, Glutathione, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, Molecular biology, Original Research Communications, chemistry, DNA, Viral, Recombinant DNA, General Earth and Planetary Sciences, Thioredoxin, DNA, Protein Binding, Cysteine |
| الوصف: | Aims: In this study we identified viral gene targets of the important redox regulator thioredoxin (Trx), and explored in depth how Trx interacts with the immediate early gene #1 (IE1) of the white spot syndrome virus (WSSV). Results: In a pull-down assay, we found that recombinant Trx bound to IE1 under oxidizing conditions, and a coimmunoprecipitation assay showed that Trx bound to WSSV IE1 when the transfected cells were subjected to oxidative stress. A pull-down assay with Trx mutants showed that no IE1 binding occurred when cysteine 62 was replaced by serine. Electrophoretic mobility shift assay (EMSA) showed that the DNA binding activity of WSSV IE1 was downregulated under oxidative conditions, and that Penaeus monodon Trx (PmTrx) restored the DNA binding activity of the inactivated, oxidized WSSV IE1. Another EMSA experiment showed that IE1's Cys-X-X-Cys motif and cysteine residue 55 were necessary for DNA binding. Measurement of the ratio of reduced glutathione to oxidized glutathione (GSH/GSSG) in WSSV-infected shrimp showed that oxidative stress was significantly increased at 48 h postinfection. The biological significance of Trx was also demonstrated in a double-strand RNA Trx knockdown experiment where suppression of shrimp Trx led to significant decreases in mortality and viral copy numbers. Innovation and Conclusion: WSSV's pathogenicity is enhanced by the virus' use of host Trx to rescue the DNA binding activity of WSSV IE1 under oxidizing conditions. Antioxid. Redox Signal. 17, 914–926. |
| تدمد: | 1557-7716 1523-0864 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::549986d66e2592bf3762cb2ff13a2541Test https://doi.org/10.1089/ars.2011.4264Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....549986d66e2592bf3762cb2ff13a2541 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15577716 15230864 |
|---|