XXXV Reunião Anual da SBBqResumoID:9436


Analysis in silico of primary sequence of defense proteins in plants: determination and comparison of putative chitin-binding domains with hevein (Hevea brasiliensis)

1Aquino, R.O.; 1Migliolo, L.; 1Ribeiro, J.K.C.; 1Macedo, L.L.P.; 1Moura, F.T.; 1Vianna, A.L.B.R.; 1Oliveira, A.S.; Monteiro, 1N.K.V.; 1Dias, A.S.F.; 1Macedo, C.S.; 1Jacinto, K.A.; 2Queiroz, A.F.S.; 1Santos, E.A.; 1Sales, M.P.



1Departamento de Bioquímica, 2Departamento de Biofísica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal, RN.


The resistance is the capacity that the plants have developed to prevent, restrict or to delay the attack of pest and pathogen using principally defense chemical compounds such as secondary metabolites and proteins. Among defense proteins, enzyme inhibitors, lectins, chitinases and chitin-binding vicilins are principally studied. In this work, through of bioinformatic data bases (EBI and NCBI), amino acids sequences of chitin-binding proteins were analyzed to determine if similar chitin-binding domain of hevein, from Hevea brasiliensis latex, was present in others chitin binding proteins. Amino acids sequences of vicilins (canavalin from Canavalia gladiata, phaseolin from Phaseolus vulgaris and vicilin from Theobroma cacao, Guazuma ulmifolia, Herrania kanukuensis and Abroma augustum), GlyNac lectins (Laburnum alpinum, Ulex europaeus, Griffonia simplicifolia, Amaranthus caudatus and Phytolacca americana), wheat germ agglutinin (WGA) and class I chitinases (Vitis vinifera, Vigna unguiculata, Nicotiana tabacum, H. brasiliensis, Cicer arietinum, Zea mays, Pisum sativum, Triticum aestivum, P. vulgaris, Gossypium hirsutum, Medicago sativa, Glycine max, Psophocarpus tetragonolobus and T. cacao) were analyzed. Also amino acid sequence of the Kunitz type inhibitor of Adenanthera pavonina, a new chitin-binding protein class, was included. Results showed that the amino acids sequences of C-terminus region of canavalin and phaseolin were 55.8% and 48.8% similar to hevein, respectively. N-terminus region of T. cacao G. ulmifolia H. kanukuensis and A. augustum vicilins were 25.5% similar to hevein. Internal region of GlyNac lectins was 39.5% and region N-terminus of class I chitinases and WGA were 76.6% and 79% similar to hevein, respectively. Region C-terminus of α chain of A. pavonina Kunitz type inhibitor was 84.6% similar to hevein. This analysis in silico showed that analyzed proteins presented different affinities to chitin and that this fact could be related with the defense functions that these proteins could be exerting in plants.

 

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