Vicilin from Seeds: An Alternative Tool to Combat

Overview

Journal Saudi J Biol Sci

Specialty Biology

Date 2021 Sep 1

PMID 34466101

Citations 3

Authors

A F J Franca

J N Araujo

Y Q Santos

G S C Carelli

D A Silva

T M L Amorim

L Migliolo

E A Santos

A S Oliveira

A F Uchoa

Affiliations

Soon will be listed here.

Abstract

Vicilins are seed proteins, and they constitute 70-80% of the total protein in leguminous seeds; with amolecular mass between 150 and 190 kDa, they are composed of subunits without disulfide bridges, with high affinity for chitin-binding. They are also associated with seed defense against insect pests. The chitin-binding vicilin from seeds was purified by ammonium sulfate, followed by affinity chromatography on a chitin column, molecular exclusion on Superdex 75 Tricorn in FPLC system and Phenomenex C8 chromatography in HPLC system. The vicilin, named AcV, is a tetrameric glycoprotein composed of 1.55% carbohydrates and molecular weight determined by SDS-PAGE, consisting of 70, 73, 43 and 41 kDa. The AcV homogeneity was confirmed in native PAGE, where it was observed to be a unique band with slow mobility in this gel, with approximately 230 kDa. AcV added to the diet in the bioassays resulted in a strong effect on adult emergence (ED50 of 0.096%), and in larvae caused a marked reduction in mass (WD50 of 0.32%) and lethality (LD50 of 0.33%) (w:w). The digestibility of AcV was evaluated in vitro with the digestive enzymes of larvae of of fourth instar, showing major fragments of 10 and 30 kDa. AcV showed reactivity against the anti-EvV antibody from vicilin. The deleterious effects of AcV are likely to be associated with the chitin-binding fragments generated by proteolysis in the bruchid gut, similarly to that found for vicilins from other leguminous plant species, and . AcV might be a candidate protein for a possible bioinsecticidal control of the bruchid weevil, .

Citing Articles

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Studies Calculated a New Chitin Oligomer Binding Site Inside Vicilin: A Potent Antifungal and Insecticidal Agent.

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References

Wang P, Granados R . Molecular structure of the peritrophic membrane (PM): identification of potential PM target sites for insect control. Arch Insect Biochem Physiol. 2001; 47(2):110-8. DOI: 10.1002/arch.1041. View

Wang P, Granados R . An intestinal mucin is the target substrate for a baculovirus enhancin. Proc Natl Acad Sci U S A. 1997; 94(13):6977-82. PMC: 21270. DOI: 10.1073/pnas.94.13.6977. View

War A, Murugesan S, Boddepalli V, Srinivasan R, Nair R . Mechanism of Resistance in Mungbean [ (L.) R. Wilczek var. ] to bruchids, spp. (Coleoptera: Bruchidae). Front Plant Sci. 2017; 8:1031. PMC: 5477293. DOI: 10.3389/fpls.2017.01031. View

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

Macedo L, Amorim T, Uchoa A, Oliveira A, Ribeiro J, de Macedo F . Larvicidal effects of a chitin-binding vicilin from Erythrina velutina seeds on the mediterranean fruit fly Ceratitis capitata. J Agric Food Chem. 2008; 56(3):802-8. DOI: 10.1021/jf072746n. View

Teixeira F, Oliveira A, Macedo L, Santos E, de Sales M . Effects of a chitin binding vicilin from Erythrina velutina seeds on bean bruchid pests (Callosobruchus maculatus and Zabrotes subfasciatus). Protein Pept Lett. 2008; 15(3):270-4. DOI: 10.2174/092986608783744171. View

Macedo M, Fernandes K, Sales M, Xavier-Filho J . Purification and properties of storage proteins (vicilins) from cowpea (Vigna unguiculata) seeds which are susceptible or resistant to the bruchid beetle Callosobruchus maculatus. Braz J Med Biol Res. 1995; 28(2):183-90. View

Lehane M . Peritrophic matrix structure and function. Annu Rev Entomol. 1997; 42:525-50. DOI: 10.1146/annurev.ento.42.1.525. View

Souza A, Ferreira A, Perales J, Beghini D, Fernandes K, Xavier-Filho J . Identification of Albizia lebbeck seed coat chitin-binding vicilins (7S globulins) with high toxicity to the larvae of the bruchid Callosobruchus maculatus. Braz J Med Biol Res. 2012; 45(2):118-24. PMC: 3854254. DOI: 10.1590/s0100-879x2012007500008. View

10.

Uchoa A, DaMatta R, Retamal C, Albuquerque-Cunha J, Souza S, Samuels R . Presence of the storage seed protein vicilin in internal organs of larval Callosobruchus maculatus (Coleoptera: Bruchidae). J Insect Physiol. 2005; 52(2):169-78. DOI: 10.1016/j.jinsphys.2005.10.002. View

11.

Watanabe H, Tokuda G . Cellulolytic systems in insects. Annu Rev Entomol. 2009; 55:609-32. DOI: 10.1146/annurev-ento-112408-085319. View

12.

Amorim T, Macedo L, Uchoa A, Oliveira A, Pitanga J, Macedo F . Proteolytic digestive enzymes and peritrophic membranes during the development of Plodia interpunctella (Lepidoptera: Piralidae): targets for the action of soybean trypsin inhibitor (SBTI) and chitin-binding vicilin (EvV). J Agric Food Chem. 2008; 56(17):7738-45. DOI: 10.1021/jf801224d. View

13.

Rufino F, Pedroso V, Araujo J, Franca A, Rabelo L, Migliolo L . Inhibitory effects of a Kunitz-type inhibitor from Pithecellobium dumosum (Benth) seeds against insect-pests' digestive proteinases. Plant Physiol Biochem. 2012; 63:70-6. DOI: 10.1016/j.plaphy.2012.11.013. View

14.

Towbin H, Staehelin T, Gordon J . Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979; 76(9):4350-4. PMC: 411572. DOI: 10.1073/pnas.76.9.4350. View

15.

Oliveira A, Migliolo L, Aquino R, Ribeiro J, Macedo L, Andrade L . Purification and characterization of a trypsin-papain inhibitor from Pithecelobium dumosum seeds and its in vitro effects towards digestive enzymes from insect pests. Plant Physiol Biochem. 2007; 45(10-11):858-65. DOI: 10.1016/j.plaphy.2007.08.002. View

16.

Uchoa A, de Miranda M, de Souza A, Gomes V, Fernandes K, Lemos F . Toxicity of hydrolyzed vicilins toward Callosobruchus maculatus and phytopathogenic fungi. J Agric Food Chem. 2009; 57(17):8056-61. DOI: 10.1021/jf900999m. View

17.

Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

18.

Candido E, Pinto M, Pelegrini P, Lima T, Silva O, Pogue R . Plant storage proteins with antimicrobial activity: novel insights into plant defense mechanisms. FASEB J. 2011; 25(10):3290-305. DOI: 10.1096/fj.11-184291. View

19.

Miranda M, Uchoa A, Ferreira S, Ventury K, Costa E, Carmo P . Chemical Modifications of Vicilins Interfere with Chitin-Binding Affinity and Toxicity to (Coleoptera: Chrysomelidae) Insect: A Combined In Vitro and In Silico Analysis. J Agric Food Chem. 2020; 68(20):5596-5605. DOI: 10.1021/acs.jafc.9b08034. View

20.

Kunz D, Oliveira G, Uchoa A, Samuels R, Macedo M, Silva C . Receptor mediated endocytosis of vicilin in Callosobruchus maculatus (Coleoptera: Chrysomelidae) larval midgut epithelial cells. Comp Biochem Physiol B Biochem Mol Biol. 2017; 210:39-47. DOI: 10.1016/j.cbpb.2017.06.003. View