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Toxicity and binding profile of lectins from the Genus canavalia on brine shrimp.

Arruda FV, Melo AA, Vasconcelos MA, Carneiro RF, Barroso-Neto IL, Silva SR, Pereira-Junior FN, Nagano CS, Nascimento KS, Teixeira EH, Saker-Sampaio S, Sousa Cavada B, Sampaio AH - Biomed Res Int (2013)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Integrated Laboratory of Biomolecules (LIBS-BioMol Group), Department of Pathology and Legal Medicine, Federal University of Ceará, 62042-280 Fortaleza, CE, Brazil.

ABSTRACT
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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Binding of FITC-labeled lectins to Artemia nauplii detected by fluorescence microscopy. The green color indicates the presence of FITC-labeled lectins in the digestive tract of the animal. (a) FITC-ConBr; (b) FITC-ConA; (c) FITC-ConBol; (d) FITC-ConM; (e) FITC-ConGF; and (f) FITC-BSA. The same images were also acquired in bright field without fluorescence excitation.
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fig2: Binding of FITC-labeled lectins to Artemia nauplii detected by fluorescence microscopy. The green color indicates the presence of FITC-labeled lectins in the digestive tract of the animal. (a) FITC-ConBr; (b) FITC-ConA; (c) FITC-ConBol; (d) FITC-ConM; (e) FITC-ConGF; and (f) FITC-BSA. The same images were also acquired in bright field without fluorescence excitation.

Mentions: Microscopy confirmed that lectins bound to Artemia nauplii (Figure 2). All lectins bound to a similar area of the organism and this area represents the digestive tract of the nauplii. The binding in this area was probably due to specific carbohydrate recognition, since the addition of α-methyl mannoside reduced the binding of the FITC-labeled lectins to the digestive tract of the nauplii (data not shown).


Toxicity and binding profile of lectins from the Genus canavalia on brine shrimp.

Arruda FV, Melo AA, Vasconcelos MA, Carneiro RF, Barroso-Neto IL, Silva SR, Pereira-Junior FN, Nagano CS, Nascimento KS, Teixeira EH, Saker-Sampaio S, Sousa Cavada B, Sampaio AH - Biomed Res Int (2013)

Binding of FITC-labeled lectins to Artemia nauplii detected by fluorescence microscopy. The green color indicates the presence of FITC-labeled lectins in the digestive tract of the animal. (a) FITC-ConBr; (b) FITC-ConA; (c) FITC-ConBol; (d) FITC-ConM; (e) FITC-ConGF; and (f) FITC-BSA. The same images were also acquired in bright field without fluorescence excitation.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3860074&req=5

fig2: Binding of FITC-labeled lectins to Artemia nauplii detected by fluorescence microscopy. The green color indicates the presence of FITC-labeled lectins in the digestive tract of the animal. (a) FITC-ConBr; (b) FITC-ConA; (c) FITC-ConBol; (d) FITC-ConM; (e) FITC-ConGF; and (f) FITC-BSA. The same images were also acquired in bright field without fluorescence excitation.
Mentions: Microscopy confirmed that lectins bound to Artemia nauplii (Figure 2). All lectins bound to a similar area of the organism and this area represents the digestive tract of the nauplii. The binding in this area was probably due to specific carbohydrate recognition, since the addition of α-methyl mannoside reduced the binding of the FITC-labeled lectins to the digestive tract of the nauplii (data not shown).

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Integrated Laboratory of Biomolecules (LIBS-BioMol Group), Department of Pathology and Legal Medicine, Federal University of Ceará, 62042-280 Fortaleza, CE, Brazil.

ABSTRACT
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.

Show MeSH
Related in: MedlinePlus