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Screening of Antifungal Proteins from Plants of Cucurbitaceae family against Fusarium oxysporum: Potential as Biofungicides

Author Affiliations

  • 1 Department of Biophysics, All India Institute of Medical Sciences, New Delhi, INDIA
  • 2 Department of Chemistry, RRC, Alwar (Rajasthan University), INDIA

Int. Res. J. Environment Sci., Volume 2, Issue (6), Pages 90-96, May,22 (2013)


Natural enemies like microbes and insects cause severe damage to the crops globally, resulting in a large economic loss. Plants of Cucurbitaceae family are known as the richest sources of carbohydrates, proteins, water and oil. Fusarium oxysporum causes the ‘fusarium wilt’ in the plants of this family and regarded as the major threat in growing cucurbits and thus, ensuing reduction in the total productivity of the crop. To overcome this problem, chemical fungicides are commonly spread over the crops which control the spreading of fungal diseases and subsequently increase the overall productivity. However, these synthetic chemicals are associated with various diseases and genetic disorders and are considered very lethal and risky for human beings, plants, animals and their environments. There are several proteins reported in the various plants with potential anti-fungal properties. We believe that these proteins can serve as useful resources for the formulation of future bio-fungicides which are natural, non-toxic and non-hazardous for us and our environment and surely merit over chemical fungicides. In this review, we have discussed about anti-fungal proteins reported in plants of Cucurbitaceae family which in near future, can be tested to get rid of ‘fusarium wilt’.


  1. Borris R.P., Natural products research: perspectives from a major pharmaceutical company, J. Ethnopharmacol., 51, 29-38 (1996)
  2. Tivy J., Biogeography: a study of plants in the ecosphere, Longman Scientific and Technical, J. Wiley, Burnt Mill, Harlow, New York (1993)
  3. Van Etten H.D., Mansfield J.W., Bailey J.A. and Farmer E.E., Two classes of plant antibiotics: Phytoalexins versus phytoanticipins, Plant Cell, 1191-1192 (1994)
  4. Rocio G.L., Gabriel M., Mariza G., et al., Plant Antimicrobial Agents and Their Effects on Plant and Human Pathogens, Int. J. Mol. Sci., 10(8), 3400-3419 (2009)
  5. Osbourn A.E., Saponins in cereals, Phytochemistry, 62(1), 1-4 (2003)
  6. Schlumbauam, Mauchf, Vogeliv and Bollert, Plant chitinases are potent inhibitors of fungal growth, Nature, 324, 365-367 (1986)
  7. Roberts W.K. and Selitrennikocf F.P., Plant proteins that inactivate foreign ribosomes, Biosci. Rep. 6, 19-29 (1986)
  8. Mauch F., Mauch M.B. and Boller T., Antifungal hydrolases in pea tissue II. Inhibition of fungal growth by combinations of chitinase and - 1,3-glucanase, Plant Physiology, 88, 936-942 (1988)
  9. Bhattacharya S., Chattopadhyay D. and Mukhopadhyay A., Changing Dimensions of Food Security in a Globalized World: A Review of the Perspectives for Environment, Economy and Health, Int. Res. J. Environment Sci., 2(3), 67-73 (2013)
  10. Hrelia P., Fimognari C., Maffei F., et al., The genetic and non-genetic toxicity of the fungicide Vinclozolin,Mutagenesis, 11, 445-453 (1996)
  11. Loper J.E., Henkels M.D., Roberts R.G., et al., Evaluation of streptomycin, oxytetracycline, and copper resistance of Erwinia amylovora isolated from pear orchards in Washington State, Plant Disease, 75, 287-290 (1991)
  12. Arawwawala M., Thabrew I., Arambewela L. and Handunnetti S., Anti-inflammatory activity of Trichosanthes cucumerina Linn. in rats, J. Ethnopharmacol., 131, 538-543 (2010)
  13. Huyen V.T., Phan D.V., Thang P., et al., Antidiabetic effect of Gynostemma pentaphyllum tea in randomly assigned type 2 diabetic patients, Horm. Metab. Res., 42, 353-357 (2010)
  14. Asghar M.N., Khan I.U. and Bano N., In vitro antioxidant and radical-scavenging capacities of Citrullus colocynthes(L) and Artemisia absinthium extracts using promethazine hydrochloride radical cation and contemporary assays, Food Sci. Technol. Int., 17, 481-494 (2011)
  15. Santos K.K., Matias E.F., Sobral S.C.E., et al.,Trypanocide, cytotoxic, and antifungal activities of Momordica charantia, Pharm. Biol., 50, 162-166 (2012)
  16. Xu X. and Ma J.K., The clinical observation of watermelonseeds on 52 cases of benign prostatic hyperplasia, Pract. Journal of Integration Chin. Mod. Med., 1(5), 462-463 (1998)
  17. Bai H. and Bai G.X., The treatment of watermelon rind for 17 cases of surface ulcers, Journal of Extern. Ther. Tradit. Chin. Med.10(2), 51 (2001)
  18. Yang Z.X., Watermelon healed 2 cases of chronic diarrhea, Chin. Commun. Health, 18(14), 36 (2002)
  19. Gao M.X., Ma H.L. and Guo K.Q., The bactericidal test of watermelon juice pulsed magnetic field, Food Fermentat. Ind., 30(3), 14-17 (2004)
  20. Peng W.Y., The treatment of croton and watermelon seeds through Shikishimaing the Yintang point for the thrush of children, Chin. Journal of Pract. Chin. Mod. Med., 17(19), 2927 (2004)
  21. Zhou Y.J., The clinical observations of watermelon frost spray on cervical erosion, Pract. J. Integration Chin. Mod. Med., 7(6), 34 (2007)
  22. Deng J.G., Wang S., Guo L.C. and Fan L.L., Anti-inflammatory and analgesic effects of extract from roots and leaves of Citrullus lanatus, Chinese Herbal Medicine, 2(3), 231-235 (2010)
  23. Gao Y., Cai R.L., Xie C., et al., Pharmacological basis for the medicinal use of musk melon base (Pedicellus Melo.) for abdominal distention and constipation, J. Ethnopharmacol., 142(1), 129-135 (2012)
  24. Ghule B.V., Ghante M.H., Uparganlawar A.B. and Yeole O.G., Analgesic and anti-inflammatory activities of Lagenaria siceraria (Mol.) stand, fruit juice extract in rats and mice, Pharmacogn. Mag., 232-238 (2006)
  25. Ghule B.V., Ghante M.H., Saoji A.N. and Yeole O.G., Hypolipidemic and anti-hyperlipidemic effects of Lagenaria siceraria fruit extracts, Indian J. Exp. Biol., 44, 905-909 (2006)
  26. Ghule B.V., Ghante M.H., Saoji A.N. and Yeole O.G., Diuretic activity of Lagenaria siceraria fruit extract in rats, Int. J. Pharm. Science, 69, 817-819 (2007)
  27. Saha P., Sen S.K., Bala A., et al., Evaluation of anticancer activity of Lagenaria siceraria Aerail parts, Int. J. Cancer Res., 7(3), 244-253 (2011)
  28. Nagao T., Lanaka R., Iwase Y., et al., Studies on the constituents of Luffa acutangula Roxb, Clin. Pharm. Bull, 39, 599-606 (1991)
  29. Bailey L.H., The Garden of Gourds. The Gourd Society of America, Inc. Mt. Gilead, Ohio, United States (1989)
  30. McGrath M.S., Hwang S.E., Caldwell S.E., et al., GLQ 223: An inhibitor of human immunodeficiency virus replication in acutely and chemically infected cells of lymphocyte and mononuclear phagocyte lineage, Natl. Acad. Sci. USA, 86, 2844-2848 (1989)
  31. Ng T.B., Feng Z., Li W.W. and Yeung H.W., Improved isolation and further characteristation of beta trichosanthin: A ribosome inactivating and abortifacient protein from tubers of Trichosanthes cucumeroicles (Cucurbitaceae), Int. J. Biochem., 23, 561-567 (1991)
  32. Ng T.B., Chan W.Y. and Yeung H.W., Proteins with abortifacient, ribosome inactivating, immunomodulatory, antitumor and anti-AIDS activities from Cucurbitaceae plants, Gen. Pharmacol., 23(4), 579-590 (1992)
  33. Lee H.S., Huang P.L., Bourinbaiar A.S., et al., Inhibition of the integrase of human immunodeficiency virus (HIV) type 1 by anti-HIV plant proteins MAP30 and GAP31, Proc. Natl. Acad. Sci. USA, 92(19), 8818-8822 (1995)
  34. Au T.K., Collins R.A., Lam T.L., et al., The plant ribosome inactivating proteins luffin and saporin are potent inhibitors of HIV-1 integrase, FEBS Letters471(2/3), 169-172 (2000)
  35. Nielsen K. and Boston R.S., Ribosome-inactivating proteins: a plant perspective, Annu. Rev. Plant Physiol. Plant Mol. Biol., 52, 785-816 (2001)
  36. Puri M., Kaur I., Kanwar R.K., et al., Ribosome inactivating proteins (RIPs)from Momordica charantia for antiviral therapy, Curr. Mol. Med., 9(9), 1080-1094 (2009)
  37. Broekaert W.F., Terras F.R., Cammue B.P. and Osborn R.W., Plant defensins: novel antimicrobial peptides as components of host defense system, Plant Physiol., 108, 1353-1358 (1995)
  38. Selitrennikoff C., Antifungal proteins, Appl. Environ. Microbiol., 67, 2883-2894 (2001)
  39. Oku H., Plant pathogens and disease control, CRS Press, Boca Raton, Florida (1994)
  40. Walton J.D., Biochemical plant pathology,In:Plant biochemistry, Academic Press, California, 487-502 (1997)
  41. Edreva A., Pathogenesis-related proteins: research progress in the last 15 years, Gen. Appl. Plant Phys., 31, 105-124 (2005)
  42. Van Loon L.C., Rep M. and Pieterse C.M., Significance of inducible defense-related proteins in infected plants, Ann. Rev. Phytopathol., 44, 135-162 (2006)
  43. Stanislava G., Biological and Technological Functions of Barley Seed Pathogenesis- Related Proteins (PRs), J. Inst. Brew., 115(4), 334-360 (2009)
  44. Van Loon L.C., Occurrence and Properties of plant pathogenesis-related protein, In:Datta S.K. and Muthukrishnan S. (eds), Pathogenesis-related proteins in plants, CRC Press, Boca Raton, 1-19 (1999)
  45. Brederode F.T., Linthorst H.J. and Bol J.F., Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephon treatment, UV light and wounding, Plant Mol. Biol., 17(6), 1117-1125 (1991)
  46. Roberts W.K. and Selitrennikoff C., Zeamatin, antifungal protein from maize with membrane - permiabilizing activity, J. Gen. Microbiol., 46, 1771-1778 (1990)
  47. Hejgaard J., Jacobsen S. and Svendsen I., Two thaumatin- like proteins from barley grain, FEBS Letters, 291, 127-131 (1991)
  48. Abad L.R., Urzo D., Liu M.P., et al., Antifungal activity of tobacco osmotin has specificity and involves plasma membrane permeabilization, Plant Sci., 118, 11-23 (1996)
  49. Park S.C., Lee J.R., Kim J.Y., et al., PR-1, a novel antifungal protein from pumpkin rinds, Biotechnol. Lett.32(1), 125-130 (2010)
  50. Park S.C., Kim J.Y., Lee J.K., et al., Antifungal Mechanism of a Novel Antifungal Protein from Pumpkin Rinds against Various Fungal Pathogens, J. Agric. Food Chem.57(19), 9299-9304 (2009)
  51. Cheong N.E., Choi Y.O., Kim W.Y., et al., Purification and characterization of an antifungal PR-5 protein from pumpkin leaves, Mol. Cells, 7(2), 214-219 (1997)
  52. Endo Y. and Tsurugi K., The RNA N-glycosidase activity or ricin A-chain: The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with r RNA, J. Bio. Chem., 263, 8735-8739 (1988)
  53. Bolognesi A., Olivieri F., Battelli M.G., et al., Ribosome-inactivating proteins (RNA N-glycosidases) from the seeds of Saponaria ocymoides and Vaccaria pyramidata,Eur. J. Biochem., 228(3), 935-940 (1995)
  54. Ng T.B. and Parkash A., Hispin, a novel ribosome inactivating protein with antifungal activity from hairy melon seeds, Protein Expr. Purif., 26(2), 211-217 (2002)
  55. Wang S., Zhang Y., Liu H., et al., Molecular cloning and functional analysis of a recombinant ribosome-inactivating protein (alpha-momorcharin) from Momordica charantia. Appl. Microbiol. Biotechnol., 96(4), 939-950 (2012)
  56. Parkash A., Ng T.B. and Tso W.W., Isolation and characterization of luffacylin, a ribosome inactivating peptide with anti-fungal activity from sponge gourd (Luffa cylindrica) seeds, Peptides, 23(6), 1019-1024 (2002)
  57. Wang H. and Ng T.B., Luffangulin, a novel ribosome inactivating peptide from ridge gourd (Luffa acutangula) seeds, Life Sci., 70(8), 899-906 (2002)
  58. Ribeiro S.F.F., Agizzio A.P., Machado O.L.T., et al., A new peptide of melon seeds which shows sequence homology with vicilin: Partial characterization and antifungal activity, Scientia Horticulturae, 111, 399-405 (2007)
  59. Yadav S., Tomar A.K., Jithesh O., et al., Purification and partial characterization of low molecular weight vicilin-like glycoprotein from the seeds of Citrullus lanatus,Protein J., 30(8), 575-580 (2011)
  60. Wang H.X. and Ng T.B., Isolation of cucurmoschin, a novel antifungal peptide abundant inarginine, glutamate and glycine residues from black pumpkin seeds, Peptides, 24(7), 969-972 (2003)