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Inhibitory activities of proteinase inhibitors on developmental characteristics of sugarcane Chilo infuscatellus (Snellen)

  • M. PunithavalliEmail author
  • A. Jebamalaimary
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Abstract

A sugarcane wild relative Erianthus arundinaceus was identified as a source of resistance against Chilo infuscatellus, a major devastating pest at the early cropping stage of sugarcane. In the view of earlier studies, inhibitory activities of proteinase inhibitors (PIs) from C. infuscatellus field resistant E. arundinaceus genotypes viz., IK 76 78, IJ 76 400, IK 76 84, IK 76 88, IJ 76 370, FIJI 55, IJ 76 364 and ERI 2798 and a popular variety Co 86032 were done. Although proteinase inhibitors differed significantly among the plant parts of selected genotypes, it was comparatively higher in the apical meristem (70%) followed by leaf sheath (20%) and stalk tissues (11%). The results also showed that E. arundinaceus apical meristem PIs significantly inhibited (> 70%) the midgut proteinase of early shoot borer. Among the genotypes, IJ 76 370 and IJ 76 364 had considerably higher PIs in apical meristem and leaf sheath which showed strong inhibitory activity against gut proteinase of sugarcane shoot borer. Developmental characteristics of the borer showed a significant reduction of larval and pupal survival along with extended larval duration in the genotypes IJ 76 370 and IJ 76 364. Correlation studies indicated negative relationship with shoot borer larval (P < 0.05, r = −0.14) and pupal survival (P < 0.05, r = −0.56**) with apical meristem PIs of E. arundinaceus. Similarly, significant correlations were found between the shoot borer developmental period and apical meristem PIs of E. arundinaceus (P < 0.05, r = 0.52**, P < 0.05, r = 0.24 and P < 0.05, r = 0.56** for larval, pupal and total developmental period of the borer respectively). The study identified two elite genotypes IJ 76 370 and IJ 76 364 which could be used as donors for sugarcane pre-breeding programme for the development of shoot borer resistant varieties. Besides, it could be possible to identify novel insecticidal proteins (PIs) that may be utilized in genetic manipulation work for producing transgenics imparting resistance against sugarcane C. infuscatellus.

Keywords

Erianthus arundinaceus Proteinase inhibitors Midgut proteinase Shoot borer biology Correlation 

Notes

Acknowledgements

The authors thanks to DST-SERB (SERB/F/8218/2015-16 dated 03-03-2016), Government of India for providing financial support to carryout the research work.

Compliance with ethical standards

Conflict of interest

There is no conflict of interest regarding the publication of this article in Phytoparasitica.

References

  1. Allsopp, P. G., & Cox, M. C. (2002). Sugarcane clones vary in their resistance to sugarcane whitegrubs. Australian Journal of Agricultural Research, 10, 53.Google Scholar
  2. Allsopp, P. G., McGhie, T. K., Cox, M. C., & Smith, G. R. (1996). Redesigning sugarcane for resistance to Australian canegrubs: a potential IPM component. Integrated Pest Management Reviews, 2, 79–90.CrossRefGoogle Scholar
  3. Amalraj, V. A., Rakkiyappan, P., & Rema Devi, A. K. (2011). Evaluation of wild sugarcane Erianthus arundinaceus(Retz) Jesw. germplasm. Journal of Sugarcane Research, 1, 23–27.Google Scholar
  4. Balaji, M. P., Manvendra, S., & Kachole. (2012). Identification of potent inhibitors of Chilo partellus (Swinhoe) (Lepidoptera: Pyralidae) Gut proteinases from plant gum PIs. International Journal of Science and Technology, 12, 662–670.Google Scholar
  5. Bown, D. P., Wilkinson, H. S., & Gatehouse, J. A. (1997). Differentially regulated inhibitor-sensitive and insensitive proteinase genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families. Insect Biochemistry and Molecular Biology, 27, 625–638.CrossRefGoogle Scholar
  6. Broadway, R. M., & Duffey, S. A. (1986). Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of the larvae Heliothis zea and Spodoptera exiqua. Journal of Insect Physiology, 34, 1111–1117.Google Scholar
  7. DAC. (2015). Directorate of Economics and statistics, Department of Agriculture and Cooperation. (www.eands.dacnet.nic.in).
  8. Dhaliwal, G. S., Jindal, V., & Mohindru, B. (2015). Crop losses due to insect pests: global and indian scenario. Indian Journal of Entomology, 77, 165–168.CrossRefGoogle Scholar
  9. Edmonds, H. S., Gatehouse, L. N., Hilder, V. A., & Gatehouse, J. A. (1996). The inhibitory effects of the cysteine proteinase inhibitor, oryzacystatin, on digestive proteinases and on larval survival and development of the southern corn rootworm (Diabrotica undecimpunctata howardi). Entomologia Experimentalis et Applicata, 78, 83–94.CrossRefGoogle Scholar
  10. Falco, M. C., & Silva-Filho, M. C. (2003). Expression of soybean proteinase inhibitors in transgenic sugarcane plants: effects on natural defense against Diatraea saccharalis. Plant Physiology and Biochemistry, 41, 761–766.CrossRefGoogle Scholar
  11. Falco, M. C., Marbach, P. A. S., Pompermayer, P., Lopes, F. C. C., & Silva-Filho, M. C. (2001). Mechanisms of sugarcane response to herbivory. Genetics and Molecular Biology, 24, 113–122.CrossRefGoogle Scholar
  12. Haq, S. K., & Khan, R. H. (2003). Characterization of a proteinase inhibitor from Cajanus cajan (L.). Journal of Protein Chemistry, 22, 543–554.Google Scholar
  13. Harsulkar, A. M., Giri, A. P., Patankar, A. G., Gupta, V. S., Sainani, M. N., Ranjekar, P. K., & Deshpande, V. V. (1999). Successive use of non-host plant proteinase inhibitors required for effective inhibition of Helicoverpa armigera gut proteinases and larval growth. Plant Physiology, 121, 497–506.CrossRefGoogle Scholar
  14. Jadhav, A. R., Abdul, R. W., Ashwini, N. N., Anmol, S. A., Vidya, S. G., Sharma, H. C., Giri, A. P., & Tamhane, V. A. (2016). Capsicum annuum proteinase inhibitor ingestion negatively impacts the growth of sorghum pest Chilo partellus and promotes differential protease expression. Biochemistry and Biophysics Reports, 8, 302–309.Google Scholar
  15. Jongsma, M. A., & Bolter, C. (1997). The adaption of insects to plant proteinase inhibitors. Journal of Insect Physiology, 10, 885–895.CrossRefGoogle Scholar
  16. Jongsma, M. A., Bakker, P. L., Peters, J., Bosch, D., & Stiekema, W. J. (1995). Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition. Proceedings of National Academic Sciences, USA, 92, 8041–8045.CrossRefGoogle Scholar
  17. Jouanin, L., Bonade-Bottino, M., Girard, C., Morrot, G., & Giband, M. (1998). Transgenic plants for insect resistance. Plant Science, 131, 1–11.CrossRefGoogle Scholar
  18. Kansal, R., Gupta, R. N., Koundal, K. R., Kuhar, K., & Gupta, V. K. (2008). Purification, characterization and evaluation of insectisidal potential of trypsin inhibitor from mugbean (Vigna radiata L. Wilczek) seeds. Acta physiologiae plantarum, 30, 761–768.Google Scholar
  19. Koiwa, H., Bressan, R. A., & Hasegawa, P. M. (1997). Regulation of proteinase inhibitors and plant defense. Trends in Plant Science, 2, 379–384.CrossRefGoogle Scholar
  20. Lawrence, P. K., & Koundal, K. R. (2002). Plant proteinase inhibitors in control of phytophagous insects. Electronic Journal of Biotechnology, 5, 93–109.CrossRefGoogle Scholar
  21. Mukunthan, N. (2001). Reaction of Erianthus to sugarcane pests. In: T. V. Sreenivasan, V. A. Amalraj, & A. William Jebedas (Eds.), Catalogue on sugarcane genetic resources- IV. Erianthus species Sugarcane Breeding Institute (ICAR) Coimbatore- 641 007 pp.93.Google Scholar
  22. Mukunthan, N., & Jayanthi, R. (2001). Entomology and nematology. Annual Report, Sugarcane Breeding Institute, Coimbatore. 51–52.Google Scholar
  23. Parde, V. D., Sharma, H. C., & Kachole, M. S. (2010). In vivo inhibition of Helicoverpa armigera gut pro-proteinase activation by non-host plant proteinase inhibitors. Journal of Insect Physiology, 56, 1315–1324.CrossRefGoogle Scholar
  24. Paulillo, L. C. M. S., Sebbenn, A. M., De Carvalho Derbyshire, M. T. V., Góes-Neto, A., De Paula Brotto, M. A., & Figueira, A. (2012). Evaluation of in vitro and in vivo effects of semipurified proteinase inhibitors from Theobroma seeds on midgut proteinase activity of lepidopteran pest insects. Archives of Insect Biochemistry and Physiology, 81, 34–52.CrossRefGoogle Scholar
  25. Pompermayer, P., Lopes, A. R., Terra, W. R., Parra, J. R. P., Falco, M. C., & Silva-Filho, M. C. (2001). Effects of soybean proteinase inhibitor on development, survival and reproductive potential of the sugarcane borer, Diatrea sachharalis. Entomologia Experimentalis et Applicata, 99, 79–85.Google Scholar
  26. Prem, K. (1996). Evolving management strategies for pests of millets in India. Journal of Entomological Research, 20, 287–297.Google Scholar
  27. Punithavalli, M., & Jebamalaimary, A. (2017a). Identification of resistant Erianthus arundinaceus genotypes based on bionomics of sugarcane early shoot borer Chilo infuscatellus (Snellen). In: International symposium on sugarcane research since Co 205: 100 years and beyond (SucroSym) (Coimbatore, India, pp. 359–360).Google Scholar
  28. Punithavalli, M., & Jebamalaimary, A. (2017b). Profiling of proteinase inhibitors (PIs) from Erianthus arundinaceus and their evaluation against gut proteinases of Chilo infuscatellus (Snellen) and Chilo sacchariphagus indicus (Kapur) in sugarcane. In: International Conference & Expo on Agriculture & Veterinary Sciences: Research and Technology (Hyderabad, India, pp. 208–209).Google Scholar
  29. Ramesh Babu, S., & Subrahmanyam, B. (2010). Bio-potency of serine proteinase inhibitors from Acacia senegal seeds on digestive proteinases, larval growth and development of Helicoverpa armigera (Hübner). Pesticide Biochemistry and Physiology, 98, 349–358.Google Scholar
  30. Ramesh Babu, S., Subramanyam, B., Srinivasan, & Santha, I. M. (2012). In vivo and in vitro effect of Acacia nilotica seed proteinase inhibitors on Helicoverpa armigera (Hubner) larvae. Journal of Biological Sciences, 37, 269–276.Google Scholar
  31. Rutherford, R. S. (1998). The effect of selected protease inhibitors and lectins in artificial diet on survival and growth of Eldana saccharina larvae. Proceedings South African Sugarcane Technology Association, 72, 91–93.Google Scholar
  32. Rutherford, R. S., Meyer, J. H., Smith, G. S., & Staden, V. J. (1993). Resistance to Eldana saccharina (Lepidoptera: Pyralidae) in sugarcane and some phytochemical correlations. Proceedings South African Sugarcane Technology Association, 67, 82–87.Google Scholar
  33. Ryan, C. A. (1990). Proteinase inhibitors in plants: genes for improving defenses against insects and pathogens. Annual Review of Phytopathology, 28, 425–449.Google Scholar
  34. Santos, J. M., Duarte Filho, L. S. C., Soriano, M. L., & Silva, P. P. (2012). Genetic diversity of the main progenitors of sugarcane from the RIDESA germplasm bank using SSR markers. Industrial Crops and Products, 40, 145–150.CrossRefGoogle Scholar
  35. SAS Institute. (2003). SAS/STAT users guide, release 6.03 edition. Cary: SAS Institute.Google Scholar
  36. Shrivastava, A. K., Srivastava, & Sangeeta. (2016). Diversity of the germplasm of Saccharum species and related genera available for use in directed breeding programmes for sugarcane improvement. Current Science, 3, 475–482.CrossRefGoogle Scholar
  37. Solomon, S. (2000). Post-harvest cane deterioration and its milling consequences. Sugar Tech, 2, 1–18.CrossRefGoogle Scholar
  38. Sreenivasan, T. V., Amalraj, V. A., & Jebadhas, A. W. (2001). A catalogue on sugarcane genetic resources IV: Erianthus spp. Sugarcane BreedingInstitute, Coimbatore, India, p98.Google Scholar
  39. Srinivasan, A., Giri, A. P., Harsulkar, A. M., Gatehouse, J. A., & Gupta, V. S. (2005). A Kunitz trypsin inhibitor from chickpea (Cicer arietinum L.) that exerts anti-metabolic effect on pod borer (Helicoverpa armigera) larvae. Plant Molecular Biology, 57, 359–374.Google Scholar
  40. Sruthy, M. A., Divya, P. S., Premachandran, M. N., Ravichandran, V., & Subramonian, N. (2015). Physiological and molecular insights to drought responsiveness in Erianthus spp. Sugar Tech, 17, 121–129.Google Scholar
  41. Stirling, G. R., Cox, M. C., & Ogden-Brown. (2011). Resistance to plant-parasitic nematodes (Pratylenchus zeae and Meloidogyne javanica) in Erianthus and crosses between Erianthus and sugarcane. Proceedings of Australian Society of Sugar Cane Technology, 33, 1–8.Google Scholar
  42. Tamhane, V. A., Chougule, N. P., Giri, A. P., Dixit, A. R., Sainani, M. N., & Gupta, V. S. (2005). In vivo and in vitro effect of Capsicum annum proteinase inhibitors on Helicoverpa armigera gut proteinases. Biochimica et Biophysica Acta, 1722, 156–167.Google Scholar
  43. Telang, M., Srinivasan, A., Patankar, A., Harsulkar, A. V., Damle, A., Deshpande, V., Sainani, M. N., Ranjekar, P., Gupta, G., Birah, A., Rani, S., Kachole, M., Giri, A., & Gupta, V. (2003). Bitter gourd proteinase inhibitors: potential growth inhibitors of Helicoverpa armigera and Spodoptera litura. Phytochemistry, 63, 643–652.CrossRefGoogle Scholar
  44. Telang, M. A., Giri, A. P., Sainani, M. N., & Gupta, V. S. (2005). Characterization of two midgut proteinases of Helicoverpa armigera and their interaction with proteinase inhibitors. Journal of Insect Physiology, 51, 513–522.CrossRefGoogle Scholar
  45. Wolfson, J. L., & Murdock, A. L. (1995). Potential use of proteinase inhibitors for host plant resistance: a test case. Environmental Entomology, 24, 52–57.CrossRefGoogle Scholar

Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Sugarcane Breeding InstituteCoimbatoreIndia

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