Protein Profile Analysis of Tungro and Dwarf Virus-Infected Rice Plants using SDS-PAGE
DOI:
10.29303/jbt.v23i2.6120Published:
2023-12-03Downloads
Abstract
Viruses in rice plants are one of the causes of decreased harvest yields and rice farming productivity. This study aims to analyze the protein profile of viruses in rice plants infected with tungro and dwarf viruses using the SDS-PAGE method. The study includes six plant samples, including tungro-infected plants from Pinrang and Sidrap districts, as well as dwarf virus-infected plants from Sidrap and Wajo districts. Two healthy plant samples were used as a comparison. The SDS-PAGE technique was employed for the separation and analysis of proteins. The protein profile results in tungro-infected plants showed a protein band pattern between 31-116 kDa. Meanwhile, in dwarf virus-infected plants, a protein band pattern between 31-205 kDa was detected. These results indicate variations in protein expression between viruses and significant differences in protein profiles between tungro and dwarf virus-infected plants compared to healthy plants. Therefore, it is expected that this information can aid in designing more effective strategies for controlling virus infections in rice plants.
Keywords:
Protein profile, rice viruses, SDS-PAGE.References
Abbas, S., Sulandari, S., Hartono, S., Daud, I. D., & Djaya, E. (2023). Molecular Detection Of Five Mixed Rice Viruses By Reverse Transcription-Polymerase Chain Reaction (RT-PCR). Pakistan Journal of Phytopathology, 35(1), 25-34. DOI: https://doi.org/10.33866/phytopathol.035.01.0793
Angeli, L., Conversano, F., Dall'Asta, A., Eggebø, T., Volpe, N., Marta, S., ... & Ghi, T. (2022). Automatic measurement of head-perineum distance during intrapartum ultrasound: description of the technique and preliminary results. The Journal of Maternal-Fetal & Neonatal Medicine, 35(14), 2759-2764. DOI: https://doi.org/10.1080/14767058.2020.1799974
Bunai, K., & Yamane, K. (2005). Effectiveness and limitation of two-dimensional gel electrophoresis in bacterial membrane protein proteomics and perspectives. Journal of Chromatography B, 815(1-2), 227-236. DOI: https://doi.org/10.1016/j.jchromb.2004.08.030
Campbell, N. A., Reece, J. B., & Mitchell, L. G. (2002). Biology, Fith Edition.
Chen, C. C., Hsu, Y. H., Chen, M. J., & Chiu, R. J. (1989). Comparison of proteins and nucleic acids of Echinochloa ragged stunt and rice ragged stunt viruses. Intervirology, 30(5), 278-284. DOI: https://doi.org/10.1159/000150103
Chauhan, B. S., Jabran, K., & Mahajan, G. (Eds.). (2017). Rice production worldwide (Vol. 247). Cham, Switzerland: Springer International Publishing. DOI: https://doi.org/10.1007/978-3-319-47516-5
Davis, L., Kuehl, M., & Battey, J. (1994). Basic method in molecular biology Noiwalk. Appleton and Lange, 310-3.
Di Girolamo, F., Ponzi, M., Crescenzi, M., Alessandroni, J., & Guadagni, F. (2010). A simple and effective method to analyze membrane proteins by SDS-PAGE and MALDI mass spectrometry. Anticancer research, 30(4), 1121-1129.
Erickson, H. P. (2009). Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biological procedures online, 11, 32-51. DOI: https://doi.org/10.1007/s12575-009-9008-x
Fachrurrazie, F., Cahyotomo, A., Untung, J., Panglipur, H. S., Solihat, I., Tirta, A. P., & Wulanawati, A. (2022). Pendekatan secara in silico senyawa inhibitor ACE2 dari Senyawaan Ekstrak Asparagus Sebagai Kandidat Obat SARS-CoV-2. Warta Akab, 46(1). DOI: https://doi.org/10.55075/wa.v46i1.83
Gershoni, J. M. (1988). Protein blotting: a manual. Methods of biochemical analysis, 1-58. DOI: https://doi.org/10.1002/9780470110546.ch1
Guoying, Z., Xiongbin, L. U., Huijuan, L. U., Juanli, L. E. I., Shengxiang, C., & Zuxun, G. (1999). Rice ragged stunt oryzavirus: role of the viral spike protein in transmission by the insect vector. Annals of Applied Biology, 135(3), 573-578. DOI: https://doi.org/10.1111/j.1744-7348.1999.tb00888.x
Gauci, V. J., Padula, M. P., & Coorssen, J. R. (2013). Coomassie blue staining for high sensitivity gel-based proteomics. Journal of proteomics, 90, 96-106. DOI: https://doi.org/10.1016/j.jprot.2013.01.027
Hagiwara, K., Minobe, Y., Nozu, Y., Hibino, H., Kimura, I., & Omura, T. (1986). Component proteins and structure of rice ragged stunt virus. Journal of general virology, 67(8), 1711-1715. DOI: https://doi.org/10.1099/0022-1317-67-8-1711
Helina, S., Sulandari, S., Trisyono, A., & Hartono, S. (2020). Assessments of yield losses due to double infection of rice ragged stunt virus and rice grassy stunt virus at different severity in the field, yogyakarta, indonesia. Pakistan Journal of Phytopathology, 32(2), 129-136. DOI: https://doi.org/10.33866/phytopathol.030.02.0578
Muthayya, S., Sugimoto, J. D., Montgomery, S., & Maberly, G. F. (2014). An overview of global rice production, supply, trade, and consumption. Annals of the new york Academy of Sciences, 1324(1), 7-14. DOI: https://doi.org/10.1111/nyas.12540
Oktavina, M. A. (2015). Pola Protein Sekret Kelenjar Parotoid Tiga Spesies Kodok dan Sekret Kelenjar Kulit Katak Kongkang Racun (Odorrana hosii Boulenger, 1891) Melalui SDS-PAGE. Prosiding KPSDA, 1(1).
Roy, S., & Kumar, V. (2014). A practical approach on SDS PAGE for separation of protein. International Journal of Science and Research, 3(8), 955-960. DOI: https://doi.org/10.12988/astp.2014.48109
Retamal, C. A., Thiebaut, P., & Alves, E. W. (1999). Protein purification from polyacrylamide gels by sonication extraction. Analytical Biochemistry, 268(1), 15-20. DOI: https://doi.org/10.1006/abio.1998.2977
Seidman, L. A., Moore, C. J., & Mowery, J. (2021). Basic laboratory methods for biotechnology: Textbook and laboratory reference. CRC Press. DOI: https://doi.org/10.1201/9780429282799
Setiawan, A. Y. D., Putri, R. I., Indayani, F. D., Widiasih, N. M. S., Anastasia, N., Setyaningsih, D., & Riswanto, F. D. O. (2021). Kandungan kimia dan potensi bawang merah (Allium cepa L.) sebagai inhibitor SARS-CoV-2. Indonesian Journal of Chemometrics and Pharmaceutical Analysis, 143-155. DOI: https://doi.org/10.22146/ijcpa.3584
Sulistyarsi, A., Suranto, S., & Supriyadi, S. (2012). Pola pita protein total wereng hijau (Nephotettix virescens) dan daun tanaman padi (Oryza sativa) yang terinfeksi virus tungro. Asian Journal of Tropical Biotechnology, 9(1), 32-35. DOI: https://doi.org/10.13057/biotek/c090103
Wrolstad, R. E., Acree, T. E., Decker, E. A., Penner, M. H., Reid, D. S., Schwartz, S. J., & Sporns, P. (Eds.). (2005). Handbook of food analytical chemistry, volume 1: Water, proteins, enzymes, lipids, and carbohydrates. John Wiley & Sons.
Yudistian. (2012). Gel Electrophoresis (SDS-PAGE).https://doctorstory.wordpress.com/2012/03/17/gel-electrophoresis-sds-page/ Diakses tanggal 19 November 2023.
Yee, S. F., Chu, C. H., Poili, E., & Sum, M. S. H. (2017). Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli. Journal of virological methods, 240, 69-72. DOI: https://doi.org/10.1016/j.jviromet.2016.12.001
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