Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/32229
Title: The defensive functions of plant inhibitors are not restricted to insect enzyme inhibition
Authors: Sumikawa, Joana Tomomi
Brito, Marlon Vilela de
Rodrigues Macedo, Maria Ligia
Uchoa, Adriana F.
Miranda, Antonio [UNIFESP]
Araujo, Ana Paula U.
Silva-Lucca, Rosemeire A.
Sampaio, Misako Uemura
Oliva, Maria Luiza Vilela [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Univ Fed Mato Grosso
Univ Estadual Fluminense Darcy Ribeiro
Universidade de São Paulo (USP)
Univ Estadual Oeste Parana
Keywords: Bauhinia sp.
Fabaceae
Caesalpinodae
Callosobruchus maculatus
Vigna unguiculata
Leguminosae
Cowpea
Defense protein
Insect attack
Kunitz inhibitors
Pesticide
Plant peptidase inhibitors
RGD
Trypsin inhibitor
Issue Date: 1-Feb-2010
Publisher: Elsevier B.V.
Citation: Phytochemistry. Oxford: Pergamon-Elsevier B.V., v. 71, n. 2-3, p. 214-220, 2010.
Abstract: Three plant proteinase inhibitors BbKI (kallikrein inhibitor) and BbCI (cruzipain inhibitor) from Bauhinia bouhinioides, and a BrTI (trypsin inhibitor) from B. rufa, were examined for other effects in Callosobruchus maculatus development; of these only BrTI affected bruchid emergence. BrTI and BbKI share 81% identities in their primary sequences and the major differences between them are the regions comprising the RGD and RGE motifs in BrTI. These sequences were shown to be essential for BrTI insecticidal activity, since a modified BbKI [that is a recombinant form (BbKIm) with some amino acid residues replaced by those found in BrTI sequence] also strongly inhibited insect development. By using synthetic peptides related to the BrTI sequence, YLEAPVARGDGGLA-NH(2) (RGE) and IVYYPDRGETGL-NH(2) (RGE), it was found that the peptide with an RGE sequence was able to block normal development of C. maculatus larvae (ED(50) 0.16% and LD(50) 0.09%), this being even more effective than the native protein. (C) 2009 Elsevier B.V. All rights reserved.
URI: http://repositorio.unifesp.br/handle/11600/32229
ISSN: 0031-9422
Other Identifiers: http://dx.doi.org/10.1016/j.phytochem.2009.10.009
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