Structural insights regarding an insecticidal Talisia esculenta protein and its biotechnological potential for Diatraea saccharalis larval control |
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Authors: | Freire Maria das Graças M Franco Octávio L Kubo Carlos Eduardo G Migliolo Ludovico Vargas Rodrigo H de Oliveira Caio Fernando Ramalho Parra José Roberto P Macedo Maria Ligia R |
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Institution: | a LAQUIBIO, ISECENSA, Campos dos Goytacazes-RJ, Brazilb Universidade Católica de Brasília, Brasilia-DF, Brazilc LPPFB, CCBS/UFMS, Campo Grande, MS, Brazild Departamento de Entomologia, Fitopatologia e Zoologia Agrícola, Escola Superior de Agricultura Luiz de Queiroz (ESALQ), USP, Piracicaba, SP, Brazil |
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Abstract: | Talisin is a seed-storage protein from Talisia esculenta that presents lectin-like activities, as well as proteinase-inhibitor properties. The present study aims to provide new in vitro and in silico biochemical information about this protein, shedding some light on its mechanistic inhibitory strategies. A theoretical three-dimensional structure of Talisin bound to trypsin was constructed in order to determine the relative interaction mode. Since the structure of non-competitive inhibition has not been elucidated, Talisin-trypsin docking was carried out using Hex v5.1, since the structure of non-competitive inhibition has not been elucidated. The predicted non-coincidence of the trypsin binding site is completely different from that previously proposed for Kunitz-type inhibitors, which demonstrate a substitution of an Arg64 for the Glu64 residue. Data, therefore, provide more information regarding the mechanisms of non-competitive plant proteinase inhibitors. Bioassays with Talisin also presented a strong insecticide effect on the larval development of Diatraea saccharalis, demonstrating LD50 and ED50 of ca. 2.0% and 1.5%, respectively. |
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Keywords: | Reserve protein Insecticidal activity Binding sites Homology modeling Docking studies |
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