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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 CearĂ¡, 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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(a) Distances between residues comprising the CRD of ConBr (green) and ConA (blue). (b) ConBr structure with highlighted residues that comprise its CRD in sticks surrounding spheres, which comprise the volume of the CRD.
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fig4: (a) Distances between residues comprising the CRD of ConBr (green) and ConA (blue). (b) ConBr structure with highlighted residues that comprise its CRD in sticks surrounding spheres, which comprise the volume of the CRD.

Mentions: Despite the high structural similarity shared by Canavalia lectins, significant differences were seen when the toxicity was assessed on Artemia nauplii. Key distances between residues comprising the CRD will determine its shape and hence the volume of each domain (Figures 3 and 4). Such characteristics directly impact the carbohydrate recognition and elicitation of biological effects [33, 34].


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)

(a) Distances between residues comprising the CRD of ConBr (green) and ConA (blue). (b) ConBr structure with highlighted residues that comprise its CRD in sticks surrounding spheres, which comprise the volume of the CRD.
© Copyright Policy
Related In: Results  -  Collection

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

fig4: (a) Distances between residues comprising the CRD of ConBr (green) and ConA (blue). (b) ConBr structure with highlighted residues that comprise its CRD in sticks surrounding spheres, which comprise the volume of the CRD.
Mentions: Despite the high structural similarity shared by Canavalia lectins, significant differences were seen when the toxicity was assessed on Artemia nauplii. Key distances between residues comprising the CRD will determine its shape and hence the volume of each domain (Figures 3 and 4). Such characteristics directly impact the carbohydrate recognition and elicitation of biological effects [33, 34].

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 CearĂ¡, 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