Euphorbia trigona latex nematicidal activity on the root-knot nematode Meloidogyne incognita
Keywords:Nematicidal; Protease; Meloidogyne incognita; Trigonin.
The aim of this study was to test nematicidal activity of the Euphorbia trigona latex on Meloidogyne incognita juveniles and to partially purify and characterize three proteases present in this latex. Three distinct proteases were partially purificated from E. trigona latex. They were named here trigonin 1, 2 and 3. Their molecular weights were estimated at: 36, 31 and 29 kDa, for trigonin 1, 2 and 3, respectively. The pH and temperature that provided highest protease activity were pH values of 4.0, 6.0 and 9.0, and 70 °C. The crude extract containing the three proteases present in E. trigona latex reduced significantly (p < 0.01) the number of live M. incognita juveniles in 96% after 24 hours treatment. The present study is the first report of E. trigona latex with nematicidal activity, therefore more studies regarding latex proteases action on nematodes are needed.
Adegbite, A. A. (2011). Effects of some indigenous plant extracts as inhibitors of egg hatch in root-knot nematode (Meloidogyne incognita race 2). American Journal of Experimental Agriculture, 1, 96–100.
Badgujar, S. B. & Mahajan, R.T. (2012). Comparison of cysteine proteases of four laticiferous plants and characterization of Euphorbia nivulia Buch.-Ham. latex glycosylated cysteine peptidase. Indian Journal of Natural Products and Resources, 3, 152–160.
Badgujar, S. B. & Mahajan, R.T. (2013). Characterization of thermo- and detergent stable antigenic glycosylated cysteine protease of Euphorbia nivulia Buch.-Ham. and evaluation of its ecofriendly applications. The Scientific World Journal, 2013, 716545.
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254.
Carneiro, R. M. D. G. & Almeida, M. R. A. (2001). Técnica de eletroforese usada no estudo de enzimas dos nematóides de galhas para identificação de espécies. Nematologia Brasileira, 25, 35–44.
Domsalla, A., Görick, C. & Melzig, M. F. (2010). Proteolytic activity in latex of the genus Euphorbia - A chemotaxonomic marker? Pharmazie, 65, 227–230.
Fibriana, F. & Upaichit, A. (2015). Proteases from latex of Euphorbia spp. and its application on milk clot formation. Biosaintifika, 7, 92–99.
Flemmig, M., Domsalla, A., Rawel, H. & Melzig, M. F. (2017). Isolation and characterization of mauritanicain, a serine protease from the latex of Euphorbia mauritanica L. Planta Medica, 83, 551–556.
Fonseca, K. C., Morais, N. C. G., Queiroz, M. R., Silva, M. C., Gomes, M. S., Costa, J. O., Mamede, C. C. N., Torres, F. S., Penha-Silva, N., Beletti, M. E., Canabrava, H. A. N. & Oliveira, F. (2010). Purification and biochemical characterization of Eumiliin from Euphorbia milii var. hislopii latex. Phytochemistry, 71, 708–715.
Gomes, E. H., Soares, F. E. F., Souza, D. C., Lima, L. T., Sufiate, B. L., Ferreira, T. F. & Queiroz, J.H. (2019). Role of Synadenium grantii latex proteases in nematicidal activity on Meloidogyne incognita and Panagrellus redivivus. Brazilian Journal of Biology, 79, 665–668.
Gunawardana, M., Hyde, E. R., Lahmeyer, S., Dorsey, B. L., La Val, T. P., Mullen, M., Yoo, J., Knight, R. & Baum, M. M. (2015). Euphorbia plant latex is inhabited by diverse microbial communities. American Journal of Botany, 102, 1966–1977.
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685.
Mahajan, R. T. & Adsul, Y. D. (2015). Isolation, purification and characterization of serine protease from latex of Euphorbia. International Journal of Advanced Research, 3, 388–395.
Moro, L. P., Cabral, H., Okamoto, D. N., Hirata, I., Juliano, M. A., Juliano, L. & Bonilla-Rodriguez, G. O. (2013). Characterization, subsite mapping and N-terminal sequence of miliin, a serine-protease isolated from the latex of Euphorbia milii. Process Biochemistry, 48, 633–637.
Patel, G. K., Kawale, A. A. & Sharma, A. K. (2012). Purification and physicochemical characterization of a serine protease with fibrinolytic activity from latex of a medicinal herb Euphorbia hirta. Plant Physiology and Biochemistry, 52, 104–111.
Rezanejad, H., Karbalaei-Heidari, H. R., Rezaei, S. & Yousefi, R. (2015). Microsciadin, a new milk-clotting cysteine protease from an endemic species, Euphorbia microsciadia. Biomacromolecular Journal, 1, 93–103.
Soares, F. E. F., Braga, F. R., Araújo, J. V., Geniêr, H. L. A., Gouveia, A. S. & Queiroz, J. H. (2013). Nematicidal activity of three novel extracellular proteases of the nematophagous fungus Monacrosporium sinense. Parasitology Research, 112, 1557–1565.
Sufiate, B. L., Soares, F. E. F., Roberti, Á. S. & Queiroz, J. H. (2017). Nematicidal activity of proteases from Euphorbia milii. Biocatalysis and Agricultural Biotechnology, 10, 239–241.
Villanueva, J., Quirós, L. M. & Castañón, S. (2015). Purification and partial characterization of a ribosome-inactivating protein from the latex of Euphorbia trigona Miller with cytotoxic activity toward human cancer cell lines. Phytomedicine, 22, 689–695.
Yadav, R. P., Patel, A. K. & Jagannadham, M. V. (2012). Neriifolin S, a dimeric serine protease from Euphorbia neriifolia Linn.: Purification and biochemical characterisation. Food Chemistry, 132, 1296–1304.
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