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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Potential of the Lectin/Inhibitor Isolated from Crataeva tapia Bark (CrataBL) for Controlling Callosobruchus maculatus Larva Development

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Author(s):
Nunes, Natalia N. S. [1] ; Ferreira, Rodrigo S. [1] ; Silva-Lucca, Rosemeire A. [2] ; de Sa, Leonardo F. R. [3] ; de Oliveira, Antonia Elenir A. [3] ; Correia, Maria Tereza dos S. [4] ; Paiva, Patricia Maria G. [4] ; Wlodawer, Alexander [5] ; Oliva, Maria Luiza V. [1]
Total Authors: 9
Affiliation:
[1] Univ Fed Sao Paulo, UNIFESP, Dept Bioquim, EPM, BR-04044020 Sao Paulo, SP - Brazil
[2] Univ Estadual Oeste do Parana, Ctr Engn & Ciencias Exatas, Toledo, Parana - Brazil
[3] Univ Estadual Norte Fluminense Darcy Ribeiro UENF, CBB, Lab Quim & Funcao Prot & Peptideos, Campos Dos Goytacazes, RJ - Brazil
[4] Univ Fed Pernambuco, Dept Bioquim, Recife, PE - Brazil
[5] NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 - USA
Total Affiliations: 5
Document type: Journal article
Source: Journal of Agricultural and Food Chemistry; v. 63, n. 48, p. 10431-10436, DEC 9 2015.
Web of Science Citations: 6
Abstract

Callosobruchus maculatus is an important predator of cowpeas. Due to infestation during storage, this insect affects the quality of seed and crop yield. This study aimed to investigate the effects of CrataBL, a multifunction protein isolated from Crataeva tapia bark, on C. maculatus larva development. The protein, which is stable even in extreme pH conditions, showed toxic activity, reducing the larval mass 45 and 70% at concentrations of 0.25 and 1.0% (w/w), respectively. Acting as an inhibitor, CrataBL decreased by 39% the activity of cysteine proteinases from larval gut. Conversely, the activity of serine proteinases was increased about 8-fold. The toxic properties of CrataBL may also be attributed to its capacity of binding to glycoproteins or glycosaminoglycans. Such binding interferes with larval metabolism, because CrataBL FITC was found in the fat body, Malpighian tubules, and feces of larvae. These results demonstrate the potential of this protein for controlling larva development. (AU)

FAPESP's process: 09/17058-6 - Purification and characterization of compounds isolated from plants with larvicidal activity.
Grantee:Natalia Neto dos Santos Nunes
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 09/53766-5 - Proteins from plant source with selectivity for inhibition of mammalian enzymes and their role as an anti-inflammatory, antithrombotic, anti-diabetic and anti-tumor agent
Grantee:Maria Luiza Vilela Oliva
Support Opportunities: Research Projects - Thematic Grants