واکنش پروتئوم لوبیا در اثر تغذیه کنه تارتن دولکه‌ای Tetranychus urticae Koch با رویکرد تکنیک پروتئومیکس

نوع مقاله : مقاله کامل، فارسی

نویسنده

بخش علوم کشاورزی، دانشگاه پیام‌نور

چکیده

کنه تارتن دولکه­ای،Koch  Tetranychus urticae، از مهمترین آفات لوبیا محسوب می­گردد که باعث خسارت وسیعی روی این گیاه می‌شود. مطالعه حاضر به منظور بررسی پاسخ پروتئینی گیاه لوبیا در حضور و عدم حضور آفت کنه تارتن دولکه­ای با استفاده از روش الکتروفورز دوبعدی صورت گرفت. جهت تعیین مقدار کمی پروتئین­ها از روش برادفورد استفاده گردید. نتایج نشان داد که در اثر تنش تغذیه­ای آفت، مقدار کمی پروتئین کل نسبت به حالت شاهد کاهش می­یابد. 266 لکه پروتئینی با رنگ­آمیزی کوماسی‌بلو R-250، از نمونه برگی لوبیا شناسایی گردید. الکتروفورز دوبعدی پروتئین تحت تنش تغذیه­ای آفت نشان­دهنده اختلافاتی در شدت بیان لکه­های پروتئینی برگ نسبت به گیاه در شرایط شاهد بود. به‌طورکلی تعداد هشت لکه­ پروتئینی نسبت به شاهد دارای کاهش بیان و تعداد چهار لکه بیان بیشتری نشان دادند. اکثر پروتئین­های شناخته شده دارای ارتباط مستقیم با سیستم دفاعی در برابر تنش بودند و نقش مهمی در این زمینه داشتند. از جمله این پروتئین­ها HSP، مالات دهیدروژناز و پلی‌فنل‌اکسیداز بودند. این نتایج شواهدی مبنی بر پاسخ سلول‌های مواجه شده با تنش برای ایجاد مقاومت به تغذیه آفت است. نتایج این مطالعه پس از بررسی الگوی باندی به کمک الکتروفورز یک بعدی (SDS-PAGE) نیز تنوع در بیان باندها در شرایط شاهد و شرایط تحت تیمار با آفت کنه تارتن دولکه‌ای را نشان داد. 

کلیدواژه‌ها


عنوان مقاله [English]

Response of Common Bean proteome to Two-Spotted Spider Mite Tetranychus urticae Koch using Proteomics Techniques

نویسنده [English]

  • M. Kakaei
Department of Agriculture, Payame Noor University
چکیده [English]

Two-spotted spider mite, Tetranychus urticae Koch, is one of the most important pests of Common bean, which causes severe damage on the plants. The purpose of the current study, was determining the bean proteome response to presence and nonpresence of T. urticae using Two-dimensional gel electrophoresis. Bradford method was used to determine the amount of proteins. The results showed that under a nutritional stress, total amount of protein was slightly reduced in comparison with the control. 266 protein spots were identified from bean leaf samples painted by Coomassie Brilliant BlueR-250. Two-dimensional electrophoresis of proteins under a pest nutritional stress showed differences in expression level of leaf protein spots on the control. Overally, eight protein spots lower than the control, had decrease of expression and high expression was showed by four spots. Most of the
recognized proteins were related to a direct relationship with system defenses against the stress
including HSP, malate dehydrogenase and polyphenol oxidase. These results confirms the response of cells exposed to stress for resistance to the pest feeding. The bands pattern with SDS-PAGE, showed the variation in the expression of bands, in control conditions and the conditions under the treatment with Two-spotted spider mite.

کلیدواژه‌ها [English]

  • Two-dimensional gel electrophoresis
  • Leaf protein
  • Phaseolus vulgaris
  • Protein expression
  • Two-spotted spider mite
Amini, F. & Ehsanpour, A. A. (2008) Study of protein changes in tomato (Lycopersicon esculentum) under salt stress using two dimensional electrophoresis. Iranian Journal of Plant Biology 1, 1324. (In Persian)
Askari, H., Edqvist, J., Hajheidari, M., Kafi, M. & Hosseini Salekdeh, G. (2006) Effect of salinity levels on proteome of Suaeda aegyptica leaves. Proteomics 6, 25462554.
Berenbaulm, M. R. (1995) The chemistry of defense: theory and oractice. Proceedings of the National Academy of Sciences USA. 92, 28.
Bradford, M. M. (1976) A rapid and sensitive method for quantitation of microgram of protein utilizing the principle of protein-dye binding. Analytical Biochemistery
Quantities
72, 248254.
Bakhsi Moqadam, F., Mortazavi, S. A., Melani, A. & Hashemi, M. (2012) Evaluation of nitrogen fractions diversity and functional specification (Cicer arietinum L.) pea
protein isolate. Journal of Food Science and Technology Innovation 5 (4), 93103.
Bongani, K. N., Stephen, C., William, J. S. & Antoni, R. S. (2005) Identification of
Arabidopsis salt and osmotic stress responsive proteins using two-dimensional
difference gel electrophoresis and mass spectrometry. Proteomics 5, 4185–4196.
Cooper, A. & Geoffrey, M. (2000) The Chloroplast Genome. The Cell: A Molecular
Approach
. 2nd ed. ASM Press.
Crevel, G., Bates, H., Huikeshoven, H. & Cotterill, S. (2001) The Drosophila Dpit47 protein is a nuclear Hsp90 co-chaperone that interacts with DNA polymerase alpha. Journal of Cell Science 114 (11), 20152025.
Chanda, A., Roze, L. V., Kang, S., Artymovich, K. A., Hicks, G. R. & Raikel, N. (2009) A key role for vesicles in fungal secondary metabolism. PNAS 106: 19533–19538. [PMC free article] [PubMed]
Damerval, C., Vienne, D., Zivy, M. & Thiellement, H. (1986) Technical improvements in two-dimensional electrophoresis increase the level of genetic variation detected in wheat-seedling proteins. Electrophoresis 7, 5254.
Di Carli, M., Zamboni, A., Enrico, Pe. M., Pezzotti, M., Lilley, S., Benvenuto, E. & Desiderio, A. (2011) Two-Dimensional Differential in Gel Electrophoresis
(2D-DIGE) Analysis of Grape Berry Proteome during Post harvest Withering.
Journal of Proteome Research 10 (1), 429446.
Dixon, A. F. (1973) Biology of aphids. The institute of biology studies. No 44. Edward Avnold Ltd londoni 52.
Dworak, A., Nykiel, M., Walczak, B., Miazek, A., Szworst-Łupina, D., Zagdańska, B. & Kiełkiewicz, M. (2016) Maize proteomic responses to separate or overlapping soil drought and two-spotted spider mite stresses. Planta 244, 939960.
Egas, M., Norde, D. J. & Sabelis, M. W. (2003) Adaptive learning in arthropods: spider mites learn to distinguish food quality. Experimental Applied Acarology 30, 233247.
Fatehi, F. (2009). Evaluation of long-term response to salinity in Hordeum using
Proteomics. PhD thesis. Tehran University, Tehran, Iran.
Feller, U., Anders, I. & Mae, T. (2008) Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated. Journal of Experimental Botany 59 (7), 161524.
Fenton, W. A. & Horwich, A. L. (2003) Chaperonin-mediated protein folding: fate of substrate polypeptide. Quarterly Reviews of Biophysics 36 (2), 22956.
Flott, B. E., Moerschbacher, B. M. & Reisener, H. (1989) Peroxidase isoenzyme patterns of resistant and susceptible wheat leaves following stem rust infection. New
 Phytologist
111, 413421.
Green, T. R. & Ryan, C. A. (1972) Wound-induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects. Science 175, 776777.
Gupta, A. K. & Govindarajan, V. (2010) Knowledge Flows within the Multinational Corporation. Strategic Management Journal 21, 473496.
Gygi, S. P., Rist, B. & Aebersold, R. (2000) Measuring gene expression by quantitative proteome analysis. Current Opinion Biotechnology 11 (4), 396401.
Hajheidari, M., Abdollahian-Noghabi, M. & Askari. H. (2005) Proteome analysis of sugar beet leaves under draught stress. Proteomics 5, 46399.
Hashimoto, M. & Komatsu, S. (2007) Proteomic analysis of rice seedlings during cold stress. Proteomics 7, 12931302.
Herbert, B. (1999) Advances in protein solubilization for two- dimensional
electrophoresis. Electrophoresis 2, 660663.
Kakaei, M. (2015) Screening and Identification of Resistance and Susceptibility factors in Alfalfa (Medicago sativa L.) Towards Alfalfa Weevil (Hypera postica Gyll.) with Bioassay and Proteomics. Thesis of Doctor of Philosophy in Plant Breeding, the field Molecular Genetics in Bu-Ali Sina University.
Kamen, D. E. & Woody, R. W. (2002) Folding kinetics of the protein pectate lyase C
reveal fast-forming intermediates and slow proline isomerization. Biochemistry 41 (14), 47134723.
Kerby, K. & Somerville, S. (1989) Enhancement of specific intercellular peroxidases
following inoculation of barley with Erysiphe graminis f. sp. hordei. Physiological and Molecular Plant Pathology  35, 323337.
Klug, W. S. & Cumming, M. R. (2000) Concepts of genetics. Sixth edition. Prentice Hall Inc. New Jersey.
Klampfi, T., Gisslinger, H., Harutyunyan, A. S., Nivarthi, H., Rumi, E., Milosevic, J. D., Them, N. C., Berg, T., Gisslinger, B., Pietra, D., Chen, D., Vladimer, G. I., Bagienski, K., Milanesi, C., Casetti, I. C., Sant Antonio, E., Ferretti, V., Elena, C., Schischlik, F., Cleary, C., Six, M., Schalling, M., Schalling, M., Schonegger, A., Bock, C., Malcovati, L., Pascutto, C., Superti-Furga, G., Cazzola, M.,
Kralovics, R.
(2013) Somatic mutations of calreticulin in myeloproliferative
neoplasms. New England Journal Medicine 369 (25), 23792390.
La Fuente, M. D., Borrajo, A., Bermúdez, J., Lores, M., Alonso, J., López, M.,
Santalla, M., De Ron, A. M., Zapata, C.
& Alvarez, G. (2011) 2-DE-based
proteomic analysis of common bean (Phaseolus vulgaris L.) seeds. Proteomics 74 (2), 262267.
Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680685.
Li, C., Fang, B., Yang, C., Sbi, D. & Wang, D. (2009)Effects of varions salt-alkaline mixed stresscs on the stat of nineral elemets in nutrient solution and the growth of
alkali resistant halophyte chloris virgatn. Journal of plant nutrition 32 (7),
11371147.
Mazandarani, A. (2010) Genetic diversity in seed storage proteins in beans Iranian part of the collection. Agricultural Biotechnology Master's Thesis of Payame Noor
University. (In Persian)
Mesquita, R. O., de Almeida Soares, E., Gonçalves de Barros, E. & Ehlers Loureiro, M. (2012) Method optimization for proteomic analysis of soybean leaf:
Improvements in identification of new and low-abundance proteins. Genetics and Molecular Biology 35 (1), 353361.
Mohammadi, M. & Kazemi, H. (2002) Changes in peroxidase and polyphenol oxidase activities in susceptible and resistant wheat heads inoculated with Fusarium
graminearum
and induced resistance. Plant Science 162, 491498.
Mechanic, M., Fotovat, R. & Moradi Hagh-go, L. (2014) Comparison of bioinformatics of large and small subunits of Ribulose1,5bisphosphate Carboxylase (Rubisco(
enzymes in several plant families. First International Congress and 13th Genetic
Congress of Iran. CIGS 130567.
Nangalia, J., Massie, C. E., Baxter, E. J., Nice, F. L., Nangalia, J., Massie, C. E.,
Baxter, E. J., Nice, F. L., Gundem, G., Wedge, D. C., Avezov, E., Li, J., Kollmann, K., Kent, DG., Aziz, A., Godfrey, A. L., Hinton, J., Martincorena, I., Van Loo, P., Jones, A.V., Guglielmelli, P., Tarpey, P., Harding, H. P., Fitzpatrick, J. D.,
Goudie, C. T., Ortmann, C. A., Loughran, S. J., Raine, K, Jones, D. R., Butler, A. P., Teague, J. W., O'Meara, S., McLaren, S., Bianchi, M., Silber, Y,
Dimitropoulou, D, Bloxham, D., Mudie, L., Maddison, M., Robinson, B.,
Keohane, C, Maclean, C, Hill K, Orchard, K, Tauro, S., Du M. Q., Greaves, M, Bowen, D., Huntly, B. J, Harrison, C. N, Cross, N. C., Ron, D., Vannucchi, A. M., Papaemmanuil, E., Campbell, P. J. & Green, A. R. (2013). Somatic CALR
mutations in myeloproliferative neoplasms with nonmutated JAK2. NewEngland Journal of Medicine 369, 23912405.
Natarajan, S. S., Pastor-Corrales, M. A., Khan, F. H. & Garrett, W. M. (2013)
Proteomic Analysis of Common Bean (Phaseolus vulgaris L.) by Two-Dimensional Gel Electrophoresis and Mass Spectrometry. Journal of Basic & Applied Sciences 9, 424437.
Pereira, J., Queiroz, R. M. L., Charneau, S. O., Felix, C. R., Ricart, C. A. O., Lopes da Silva, F., Steindorff, A. S., Ulhoa, C. J. & Noronha, E. F. (2014) Analysis of
Phaseolus vulgaris Response to Its Association with Trichoderma harzianum
(ALL-42) in the Presence or Absence of the Phytopathogenic Fungi Rhizoctonia
solani
and Fusarium solani. PLOS ONE 9(5), e98234. Doi: 10.1371.
Raeisi sadati, S. E., Gedeh Kahrizi, S. & Ebadi, A. (2014) Expression of proteins
induced the leaves of two wheat varieties under cadmium and mercury using
two-dimensional electrophoresis technique. Journal of Crop Production and Processing 5 (18), 233243. (In Persian)
Rinalducci, S., Egidi, M. G., Mahfoozi, S., Godekahriz, S. J. & Zolla, L.(2011) The influence of temperature on plant development in a vernalization- requiring winter wheat: A 2-DE based proteomic investigation. Proteomics 74, 643659.
Rubio, L. A., Perez, A., Ruiz, R., Guzman, M. A., Aranda-Olmedo, I. & Clemente, A. (2013).Characterization of pea (Pisum sativum) seed protein fractions. Journal Science Food Agriculture (wileyonlinelibrary.com) DOI 10.1002/jsfa. 6250.
Stiasna, K., Presinszka, M., Vyhnanek, T., Trojan, V., Mrkvicova, E., Hrivna, L. & Havel, L. (2014) Granule-bound starch synthase and endosperm mealiness correlation in wheat (Triticum aestivum L.) with nonstandard colored caryopses. Mendel Net, 479483 pp.
Shararbar, H., Kakaei, M. & Safarolahi, M. (2016).Study of the mechanisms and
protein expression associated with the resistance of eleven eggplant genotypes to
Tetranychus urticae. Iranian Journal of Plant Protection Science 47 (2), 209218.
Tahmasebi, Z., Bihamta, M. R., Hossein-zadeh, A., Saboori, A., Kosar, A. S. & doori, H. R. (2008) Response of Common Bean Genotypes to Two-Spotted Spider Mite
(Tetranychus urticae Koch) in Greenhouse and Field. Seed and Plant Journal 2 (25), 329348. (In Persian)
Tahmasebi, Z., Hossein-zadeh, A., Bihamta, M. R. & Saboori, A. (2011) Seedling
resistance of common bean (Phaseolus vulgaris) genotypes to two spotted spider mite
(Tetranychus urticae) (Acari: Tetranychidae). Journal of Science Agriculture 5,
7378. (In Persian)
Toorchi, M. (2015) The Response of Rice Root to Time Course Water Deficit Stress-Two Dimensional Electrophoresis Approach. Journal of Crop Eco physiology 3 (35),
371386. (In Persian)
Valizadeh kamran, R., Toorchi, M., Moghaddam, M. & Mohammadi, H. (2015)
Proteomic Analysis of Spring Barley Leaves under Short Term Cold Stress. Genetic Engineering and Biosafety Journal 1, 6778. (In Persian)
Wang, W., Vinocur, B., Shoseyov, O. & Altman, A. (2004)Role of plant heat-shock
proteins and molecular chaperones in the abiotic stress response. Trends Plant Science 9, 244252.
Walia, H.,  Wilson, C., Zeng,L., Ismail, A. M., Condamine, P. & Close, T. J. (2007) Genome-wide transcriptional analysis of salinity stressed japonica and indica rice
genotypes during panicle initiation stage. Plant Molecular Biology 63 (5),
609623.
Xu, Ch., Garrett, W. M., Sullivan, J., Caperna, T. J. & Natarajan, S. (2006) Separation and identification of soybean leaf proteins by two-dimensional gel electrophoresis and mass spectrometry. Photochemistry 67, 24312440.
Zerrad L., Merli A., Schroder G. F., Varga A., Graczer E., Pernot, P., Round, A., Vas, M. & Bowler, M. W. (2011) A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase. Journal of Biological Chemistry 286 (16), 1404014048.
Zivy, M. & de Vienne, D. (2000) Proteomics: A link between genomics, genetics and
physiology. Plant Molecular Biology 44, 575580.
Zinovieva, R. D., Tomarev, S. I. & Piatigorsky, J. (1993) Aldehydrogenase-derived
crystallins of squid and octopus. Specializationfor lens expression. Journal Biological Chemistry 26, 1144911455.