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Proteomics-Based Analysis of Phalaenopsis amabilis in Response toward Cymbidium Mosaic Virus and/or Odontoglossum Ringspot Virus Infection

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DOI: 10.4236/ajps.2013.49228    3,593 Downloads   5,034 Views   Citations


Stress response at the protein level to viral infection in orchid plants has not been extensively investigated to date. To understand the proteomic basis of Phalaenopsis amabilis’s responses to Cymbidium Mosaic virus (CymMV), and/or Odontoglossum ring spot virus (ORSV), the total proteins were extracted from Phalaenopsis amabilis leaves infected with CymMV, ORSV, or both respectively. Differentially expressed proteins were identified by two-dimensional electrophoresis, and 27 of these proteins that had significant changes were further examined by mass spectrometry. Comparing CymMV-infected leaves with mock-inoculated ones, 2 proteins were significantly up-regulated, 9 were significantly down-regulated and 1 previously undetected protein was identified. 10 proteins were significantly up-regulated, 3 significantly down-regulated and 1 previously undetected protein was identified in ORSV-infected leaves. 6 proteins were significantly up-regulated and 9 significantly down-regulated proteins were found in co-infected leaves. These identified proteins are involved in disease resistance, stress response, transcriptional regulation, energy metabolism, protein modification and the previously unknown proteins were not involved with known protein pathways. Proteins significantly up-regulated were ATP sulfurylase, down-regulated proteins included glutamate decarboxylase isozyme 2, RNA polymerase alpha subunit and chloroplastic peptide deformylase 1A were proteins with similar alteration trend after all infection treatments. Significantly up-regulated were Thioredoxin H-type and down-regulated Cytosolic phosphoglycerate kinase I which were proteins that have been shown to be specifically regulated by the infection with CymMV. Significantly up-regulated were proteins like Rubisco large subunit, Triosephosphate isomerase, NADP-specific isocitrate dehydrogenase and Cinnamoyl CoA reductase CCR2 by the infection of ORSV. Protein regulation in coinfected leaves followed a pattern similar to that of any of the single virus infection results. The

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T. Lai, Y. Deng, P. Zhang, Z. Chen, F. Hu, Q. Zhang, Y. Hu and N. Shi, "Proteomics-Based Analysis of Phalaenopsis amabilis in Response toward Cymbidium Mosaic Virus and/or Odontoglossum Ringspot Virus Infection," American Journal of Plant Sciences, Vol. 4 No. 9, 2013, pp. 1853-1862. doi: 10.4236/ajps.2013.49228.


[1] X. Q. Chen, Z. H. Ji and Y. F. Zheng, “The Orchids of China,” China Forestry Press, Beijing, 1998.
[2] F. W. Zettler, N. J. Ko, G. C. Wisler, M. S. Elliott and S. M. Wong, “Viruses of Orchids and Their Control,” Plant Disease, Vol. 74, No. 9, 1990, pp. 621-626. doi:10.1094/PD-74-0621
[3] J. S. Hu, S. Ferreira, M. Wang and M. Q. Xu, “Detection of Cymbidium Mosaic Virus, Odontoglossum Ringspot Virus, Tomato Spotted Wilt Virus and Potyviruses Infecting Orchids in Hawaii,” Plant Disease, Vol. 77, No. 5, 1993, pp. 464-468. doi:10.1007/s10658-008-9293-2
[4] L. J. Liao, I. C. Pan, Y. L. Chan, Y. H. Hsu, W. H. Chen and M. T. Chan, “Transgene Silencing in Phalaenopsis Expressing the Coat Protein of Cymbidium Mosaic Virus Is a Manifestation of RNA-Mediated Resistance,” Molecular Breeding, Vol. 13, No. 3, 2004, pp. 229-242. doi:10.1023/B:MOLB.0000022527.68551.30
[5] X. Y. Qin, Y. Liu, S. J. Mao, T. B. Li, H. K. Wu, C. C. Chu and Y. P. Wang, “Genetic Transformation of Lipid Transfer Protein Encoding Gene in Phalaenopsis amabilis to Enhance Cold Resistance,” Euphytica, Vol. 177, No. 1, 2011, pp. 33-43. doi:10.1007/s10681-010-0246-4
[6] S. F. Fu, C. W. Lin, T. W. Kao, D. D. Huang and H. J. Huang, “PaPTP1, a Gene Encoding Protein Tyrosine Phosphatase from Orchid, Phalaenopsis amabilis, Is Regulated during Floral Development and Induced by Wounding,” Plant Molecular Biology Reporter, Vol. 29, No. 1, 2011, pp. 106-116. doi:10.1007/s11105-010-0216-y
[7] H. Yang, Y. P. Huang, H. J. Zhi and D. Y. Yu, “Proteomics-Based Analysis of Novel Genes Involved in Response toward Soybean Mosaic Virus Infection,” Molecular Biology Reporter, Vol. 38, No. 1, 2011, pp. 511-521. doi:10.1007/s11033-010-0135-x
[8] H. Y. Fan, J. Chen, C. M. Lv, C. Y. Zhang and Q. Sun, “Proteomic Analysis of F2 Generation of Cucumber against the Cucumber Powdery Mildew Disease,” Acta Horticulturae Sinica, Vol. 34, No. 2, 2007, pp. 349-354.
[9] J. P. Brizard, C. Carapito, F. Delalande, A. Van Dorsselaer and C. Brugidou, “Proteome Analysis of Plant-Virus Interactome: Comprehensive Data for Virus Multiplication inside Their Hosts,” Molecular and Cell Proteomics, Vol. 5, No. 12, 2006, pp. 2279-2297. doi:10.1074/mcp.M600173-MCP200
[10] M. Ventelon-Debout, F. Delalande, J. P. Brizard, H. Diemer, D. A. Van and C. Brugidou, “Proteome Analysis of Cultivar-Specific Degradation of Oryza sativa Indica and O. sativa Japonica Cellular Suspensions Undergoing Rice Yellow Mottle Virus Infection,” Proteomics, Vol. 4, No. 1, 2004, pp. 216-225. doi:10.1002/pmic.200300502
[11] C. L. Yu, Y. Yang, X. M. Wang, C. Q. Yan and J. P. Chen, “Recent Advances in Proteomic Studies on Rice-Pathogen Interactions,” China Journal of Rice Science, Vol. 24, No. 6, 2010, pp. 647-651.
[12] J. Zhao, Q. Liu, H. Zhang, Q. Jia, Y. Hong and Y. Liu, “The RuBisCO Small Subunit Is Involved in the Tobamovirus Movement and Tm-22-Mediated Extreme Resistance,” Plant Physiology, Vol. 161, No. 1, 2013, pp. 374-383. doi:10.1104/pp.112.209213
[13] M. Babu, A. Gagarinova, J. Brandle and A. Wang, “Association of the Transcriptional Response of Soybean Plants with Soybean Mosaic Virus Systemic Infection,” Journal of General Virology, Vol. 89, No. 4, 2008, pp. 1069-1080. doi:10.1099/vir.0.83531-0
[14] J. Casado-Vela, S. Selles and R. Martinez, “Proteomic Analysis of Tobacco Mosaic Virus-Infected Tomato (Lycopersicon esculentum M.) Fruits and Detection of Viral Coat Protein,” Proteomics, Vol. 6, No. 1, 2006, pp. 196-206. doi:10.1002/pmic.200500317
[15] S. Golem and J. Culver, “Tobacco Mosaic Virus Induced Alterations in the Gene Expression Profile of Arabidopsis thaliana,” Molecular Plant Microbe Interaction, Vol. 16, No. 8, 2003, pp. 681-688. doi:10.1094/MPMI.2003.16.8.681
[16] T. Kühne, N. N. Shi, G. Proeseler, M. J. Adams and K. Kanyuka, “The Ability of a Bymovirus to Overcome the rym4-Mediated Resistance in Barley Correlates with a Codon Change in the VPg Coding Region on RNA1,” Journal of General Virology, Vol. 84, No. 10, 2003, pp. 2853-2859. doi:10.1099/vir.0.19347-0
[17] N. N. Shi, Y. Xu, K. F. Yang, Y. Chen, H. Z. Wang, X. B. Xu and Y. G. Hong, “Development of a Sensitive Diagnostic Assay to Detect Cymbidium Mosaic Virus and Odontoglossum Ringspot Virus in Members of the Orchidaceae,” The Journal of Horticultural Science and Biotechnology, Vol. 86, No. 1, 2011, pp. 69-73.
[18] M. M. Bradford, “A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding,” Analytical Biochemistry, Vol. 72, 1976, pp. 248-254. doi:10.1016/0003-2697(76)90527-3
[19] J. P. Reichheld, D. Mestres-Ortega, C. Laloi and Y. Meyer, “The Multigenic Family of Thioredoxin h in Arabidopsis thaliana: Specific Expression and Stress Response,” Plant Physiology and Biochemistry, Vol. 40, 2002, pp. 685-690. doi:10.1016/S0981-9428(02)01406-7
[20] T. Song, “Cloning and Functional Analyses of a Tobacco Thioredoxin Gene,” Journal of Ludong University, Vol. 23, No. 3, 2007, pp. 256-260.
[21] N. J. Poysti and I. J. Oresnik, “Characterization of Sinorhizobium meliloti Triose Phosphate Isomerase Genes,” Journal of Bacteriology, Vol. 189, No. 9, 2007, pp. 3445-3451. doi:10.1128/JB.01707-06
[22] C. C. Fritz, F. P. Wolter, V. Schenkemeyer, T. Herget and P. H. Schreier, “The Gene Family Encoding the Ribulose-(1,5)-Bisphosphate Carboxylase/Oxygenase (Rubisco) Small Subunit of Potato,” Gene, Vol. 137, No. 2, 1993, pp. 271-274. doi:10.1126/science.1106974G. P. Zhu, G. B. Golding and A. M. Dean, “The Selective Cause of an Ancient Adaptation,” Science, Vol. 307, No. 5713, 2005, pp. 1279-1282.
[23] I. L. Jung, S. K. Kim and I. G. Kim, “The RpoS-Mediated Regulation of Isocitrate Dehydrogenase Gene Expression in Escherichia coli,” Current Microbiology, Vol. 52, No. 1, 2006, pp. 21-26. doi:10.1007/s00284-005-8006-8
[24] A. Schmidt and K. Jager, “Open Questions about Sulfur Metabolism in Plants,” Annual Review of Plant Physiology and Plant Molecular Biology, Vol. 43, 1992, pp. 325-349. doi:10.1146/annurev.pp.43.060192.001545
[25] Y. L. Zhuang, G. J. Ren, C. M. He, X. Y. Li, Q. M. Meng, C. F. Zhu, R. C. Wang and J. R. Zhang, “Cloning and Characterization of a Maize cDNA Encoding Glutamate Decarboxylase,” Plant Molecular Biology Reporter, Vol. 28, No. 4, 2010, pp. 620-626. doi:10.1007/s11105-010-0191-3
[26] J. H. Lee, Y. J. Kim, D. Y. Jeone, G. Sathiyaraj, R. K. Pulla, J. S. Shim, J. G. Yin and D. C. Yang, “Isolation and Characterization of a Glutamate Decarboxylase (GAD) Gene and Their Differential Expression in Response to Abiotic Stresses from Panax Ginseng C. A. Meyer,” Molecular Biology Reporter, Vol. 37, No. 7, 2010, pp. 3455-3463. doi:10.1007/s11033-009-9937-0
[27] R. Valentina, C. Claudia, D. P. Benedetta, D. Nunzianna, A. Angela and D. Angela, “The Ribosomal Protein L2 Interacts with the RNA Polymerase α Subunit and Acts as a Transcription Modulator in Escherichia coli,” Journal of bacteriology, Vol. 192, 2010, pp. 1882-1889. doi:10.1128/JB.01503-09
[28] K. T. Nguyen, X. B. Hu, C. Colton, R. Chakrabarti, M. X. Zhu and D. H. Pei, “Characterization of a Human Peptide Deformylase: Implications for Antibacterial Drug Design,” Biochemistry, Vol. 42, No. 33, 2003, pp. 9952-9958. doi:10.1021/bi0346446

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