1. Vicilin from Anadenanthera colubrina Seeds: An alternative tool to combat Callosobruchus maculatus
- Author
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Adeliana S. Oliveira, J.N. Araújo, Gabriella Silva Campos Carelli, D.A. Silva, Anderson Felipe Jácome de França, T.M.L. Amorim, Elizeu Antunes dos Santos, Ludovico Migliolo, Adriana F. Uchoa, and Yago Queiroz dos Santos
- Subjects
0106 biological sciences ,0301 basic medicine ,QH301-705.5 ,viruses ,01 natural sciences ,Vigna ,03 medical and health sciences ,Affinity chromatography ,Callosobruchus maculatus ,Biology (General) ,skin and connective tissue diseases ,biology ,Chemistry ,fungi ,Bioinsecticidal ,food and beverages ,virus diseases ,Fast protein liquid chromatography ,Chitin-binding protein seeds ,biology.organism_classification ,030104 developmental biology ,Enterolobium contortisiliquum ,Biochemistry ,Vicilin ,Original Article ,General Agricultural and Biological Sciences ,Anadenanthera colubrina ,Erythrina velutina ,010606 plant biology & botany - Abstract
Highlights • Vicilins from Anadenanthera colubrina seeds (AcVs) interfered with the development of cowpea weevil (Callosobruchus maculatus) larvae. • AcVs present a strong effect at low concentrations on adult emergence (ED50 of 0.096%), on larvae, showing a marked reduction in mass (WD50 of 0.32%) and lethality (LD50 of 0.33%) (w:w). • AcV is a chitin-binding protein with approximately 230 kDa. • AcV chitin-binding fragments are associated with deleterious effects in larvae., Vicilins are seed proteins, and they constitute 70–80% of the total protein in leguminous seeds; with amolecular mass between 150 and 190 kDa, they are composed of subunits without disulfide bridges, with high affinity for chitin-binding. They are also associated with seed defense against insect pests. The chitin-binding vicilin from Anadenanthera colubrina seeds was purified by ammonium sulfate, followed by affinity chromatography on a chitin column, molecular exclusion on Superdex 75 Tricorn in FPLC system and Phenomenex C8 chromatography in HPLC system. The A. colubrina vicilin, named AcV, is a tetrameric glycoprotein composed of 1.55% carbohydrates and molecular weight determined by SDS-PAGE, consisting of 70, 73, 43 and 41 kDa. The AcV homogeneity was confirmed in native PAGE, where it was observed to be a unique band with slow mobility in this gel, with approximately 230 kDa. AcV added to the Callosobruchus maculatus diet in the bioassays resulted in a strong effect on adult emergence (ED50 of 0.096%), and in larvae caused a marked reduction in mass (WD50 of 0.32%) and lethality (LD50 of 0.33%) (w:w). The digestibility of AcV was evaluated in vitro with the digestive enzymes of larvae of C. maculatus of fourth instar, showing major fragments of 10 and 30 kDa. AcV showed reactivity against the anti-EvV antibody from Erythrina velutina vicilin. The deleterious effects of AcV are likely to be associated with the chitin-binding fragments generated by proteolysis in the bruchid gut, similarly to that found for vicilins from other leguminous plant species, Enterolobium contortisiliquum and Vigna unguiculata. AcV might be a candidate protein for a possible bioinsecticidal control of the bruchid weevil, C. maculatus.
- Published
- 2021