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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...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2013
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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. |
format | Online Article Text |
id | pubmed-3860074 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
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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