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Purification and biological effects of a C-type lectin isolated from Bothrops moojeni

Snake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and i...

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Published in:The journal of venomous animals and toxins including tropical diseases 2010, Vol.16 (3), p.493-504
Main Authors: Barbosa, PSF(Federal University of Ceará Department of Physiology and Pharmacology), Martins, AMC(Federal University of Ceará Department of Clinical and Toxicological Analyses), Toyama, MH(São Paulo State University São Paulo Experimental Coast Campus), Joazeiro, PP(State University of Campinas Institute of Biology Department of Histology), Beriam, LOS(Biological Institute Experimental Center Laboratory of Plant Microbiology), Fonteles, MC(Federal University of Ceará Department of Physiology and Pharmacology), Monteiro, HSA(Federal University of Ceará Department of Physiology and Pharmacology)
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container_issue 3
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container_title The journal of venomous animals and toxins including tropical diseases
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creator Barbosa, PSF(Federal University of Ceará Department of Physiology and Pharmacology)
Martins, AMC(Federal University of Ceará Department of Clinical and Toxicological Analyses)
Toyama, MH(São Paulo State University São Paulo Experimental Coast Campus)
Joazeiro, PP(State University of Campinas Institute of Biology Department of Histology)
Beriam, LOS(Biological Institute Experimental Center Laboratory of Plant Microbiology)
Fonteles, MC(Federal University of Ceará Department of Physiology and Pharmacology)
Monteiro, HSA(Federal University of Ceará Department of Physiology and Pharmacology)
description Snake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 µg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function.
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We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 µg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. 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BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 µg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. 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During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 µg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. 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1678-9199
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subjects antibacterial activity
Bothrops moojeni
insulin
kidney
platelet aggregation
TOXICOLOGY
TROPICAL MEDICINE
title Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
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