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Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp

Lectins are sugar-binding proteins widely distributed in nature with many biological functions. Although many lectins have a remarkable biotechnological potential, some of them can be cytotoxic. Thus, the aim of this study was to assess the toxicity of five lectins, purified from seeds of different...

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Autores principales: Arruda, Francisco Vassiliepe Sousa, Melo, Arthur Alves, Vasconcelos, Mayron Alves, Carneiro, Romulo Farias, Barroso-Neto, Ito Liberato, Silva, Suzete Roberta, Pereira-Junior, Francisco Nascimento, Nagano, Celso Shiniti, Nascimento, Kyria Santiago, Teixeira, Edson Holanda, Saker-Sampaio, Silvana, Sousa Cavada, Benildo, Sampaio, Alexandre Holanda
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3860074/
https://www.ncbi.nlm.nih.gov/pubmed/24380079
http://dx.doi.org/10.1155/2013/154542
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author Arruda, Francisco Vassiliepe Sousa
Melo, Arthur Alves
Vasconcelos, Mayron Alves
Carneiro, Romulo Farias
Barroso-Neto, Ito Liberato
Silva, Suzete Roberta
Pereira-Junior, Francisco Nascimento
Nagano, Celso Shiniti
Nascimento, Kyria Santiago
Teixeira, Edson Holanda
Saker-Sampaio, Silvana
Sousa Cavada, Benildo
Sampaio, Alexandre Holanda
author_facet Arruda, Francisco Vassiliepe Sousa
Melo, Arthur Alves
Vasconcelos, Mayron Alves
Carneiro, Romulo Farias
Barroso-Neto, Ito Liberato
Silva, Suzete Roberta
Pereira-Junior, Francisco Nascimento
Nagano, Celso Shiniti
Nascimento, Kyria Santiago
Teixeira, Edson Holanda
Saker-Sampaio, Silvana
Sousa Cavada, Benildo
Sampaio, Alexandre Holanda
author_sort Arruda, Francisco Vassiliepe Sousa
collection PubMed
description Lectins are sugar-binding proteins widely distributed in nature with many biological functions. Although many lectins have a remarkable biotechnological potential, some of them can be cytotoxic. Thus, the aim of this study was to assess the toxicity of five lectins, purified from seeds of different species of Canavalia genus. In order to determine the toxicity, assays with Artemia nauplii were performed. In addition, a fluorescence assay was carried out to evaluate the binding of lectins to Artemia nauplii. In order to verify the relationship between the structure of lectins and their cytotoxic effect, structural analysis was carried out to evaluate the volume of the carbohydrate recognition domain (CRD) of each lectin. The results showed that all lectins exhibited different toxicities and bound to a similar area in the digestive tract of Artemia nauplii. Concerning the structural analysis, differences in spatial arrangement and volume of CRD may explain the variation of the toxicity exhibited by each lectin. To this date, this is the first study that establishes a link between toxicity and structure of CRD from Diocleinae lectins.
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spelling pubmed-38600742013-12-30 Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp Arruda, Francisco Vassiliepe Sousa Melo, Arthur Alves Vasconcelos, Mayron Alves Carneiro, Romulo Farias Barroso-Neto, Ito Liberato Silva, Suzete Roberta Pereira-Junior, Francisco Nascimento Nagano, Celso Shiniti Nascimento, Kyria Santiago Teixeira, Edson Holanda Saker-Sampaio, Silvana Sousa Cavada, Benildo Sampaio, Alexandre Holanda Biomed Res Int Research Article Lectins are sugar-binding proteins widely distributed in nature with many biological functions. Although many lectins have a remarkable biotechnological potential, some of them can be cytotoxic. Thus, the aim of this study was to assess the toxicity of five lectins, purified from seeds of different species of Canavalia genus. In order to determine the toxicity, assays with Artemia nauplii were performed. In addition, a fluorescence assay was carried out to evaluate the binding of lectins to Artemia nauplii. In order to verify the relationship between the structure of lectins and their cytotoxic effect, structural analysis was carried out to evaluate the volume of the carbohydrate recognition domain (CRD) of each lectin. The results showed that all lectins exhibited different toxicities and bound to a similar area in the digestive tract of Artemia nauplii. Concerning the structural analysis, differences in spatial arrangement and volume of CRD may explain the variation of the toxicity exhibited by each lectin. To this date, this is the first study that establishes a link between toxicity and structure of CRD from Diocleinae lectins. Hindawi Publishing Corporation 2013 2013-11-27 /pmc/articles/PMC3860074/ /pubmed/24380079 http://dx.doi.org/10.1155/2013/154542 Text en Copyright © 2013 Francisco Vassiliepe Sousa Arruda et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Arruda, Francisco Vassiliepe Sousa
Melo, Arthur Alves
Vasconcelos, Mayron Alves
Carneiro, Romulo Farias
Barroso-Neto, Ito Liberato
Silva, Suzete Roberta
Pereira-Junior, Francisco Nascimento
Nagano, Celso Shiniti
Nascimento, Kyria Santiago
Teixeira, Edson Holanda
Saker-Sampaio, Silvana
Sousa Cavada, Benildo
Sampaio, Alexandre Holanda
Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp
title Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp
title_full Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp
title_fullStr Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp
title_full_unstemmed Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp
title_short Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp
title_sort toxicity and binding profile of lectins from the genus canavalia on brine shrimp
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3860074/
https://www.ncbi.nlm.nih.gov/pubmed/24380079
http://dx.doi.org/10.1155/2013/154542
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