Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/15511
Title: Purification and identification of metabolites produced by Bacillus cereus and B. subtilis active against Meloidogyne exigua, and their in silico interaction with a putative phosphoribosyltransferase from M. incognita
Keywords: Plant-parasitic nematode - Control
Fihydrouracil
Molecular modelling
Nematicidal activity
Root-knot nematode
Uracil
Nematoide parasita de plantas - Controle
Di-idrouracila
Modelagem molecular
Atividade nematicida
Nematoide das galhas
Uracila
Issue Date: Jun-2014
Publisher: Academia Brasileira de Ciências
Citation: OLIVEIRA, D. F. et al. Purification and identification of metabolites produced by Bacillus cereus and B. subtilis active against Meloidogyne exigua, and their in silico interaction with a putative phosphoribosyltransferase from M. incognita. Anais da Academia Brasileira de Ciências. Rio de Janeiro, v. 86, n. 2, p. 525-538, June 2014.
Abstract: To contribute to the development of products to controlMeloidogyne exigua, the bacteria Bacillus cereus and B. subtilis were cultivated in liquid medium to produce metabolites active against this plant-parasitic nematode. Fractionation of the crude dichloromethane extracts obtained from the cultures afforded uracil, 9H-purine and dihydrouracil. All compounds were active against M. exigua, the latter being the most efficient. This substance presented a LC50 of 204 µg/mL against the nematode, while a LC50 of 260 µg/mL was observed for the commercial nematicide carbofuran. A search for protein-ligand complexes in which the ligands were structurally similar to dihydrouracil resulted in the selection of phosphoribosyltransferases, the sequences of which were used in an in silico search in the genome of M. incognita for a similar sequence of amino acids. The resulting sequence was modelled and dihydrouracil and 9H-purine were inserted in the active site of this putative phosphoribosyltransferase resulting in protein-ligand complexes that underwent molecular dynamics simulations. Calculation of the binding free-energies of these complexes revealed that the dissociation constant of dihydrouracil and 9H-purine to this protein is around 8.3 x 10-7 and 1.6 x 10-6 M, respectively. Consequently, these substances and the putative phosphoribosyltransferase are promising for the development of new products to control M. exigua.
URI: http://repositorio.ufla.br/jspui/handle/1/15511
Appears in Collections:DQI - Artigos publicados em periódicos



This item is licensed under a Creative Commons License Creative Commons