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Updated: Jun 4, 2026
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom
Erika dos Santos Nunes1, Mary Angela Aranda de Souza, Antônio Fernando de Melo Vaz
1Departamento de Bioquímica, Universidade Federal de Pernambuco, Avenida Professor Moraes Rêgo s/n, Cidade Universitária, Recife, Pernambuco, Brazil.
Abstract:
A novel lectin was isolated from Bothrops leucurus snake venom using a combination of affinity and gel filtration chromatographies. The lectin (BlL) agglutinated glutaraldehyde-treated rabbit and human erythrocytes with preference for rabbit erythrocytes. Galactose, raffinose, lactose, fetal bovine serum and casein inhibited lectin-induced rabbit erythrocyte agglutination. BlL, with a molecular mass of 30 kDa and composed of two subunits of 15 kDa, showed dependence on calcium. BlL is an acidic protein with highest activity over the pH range of 4.0-7.0 and stable under heating to 70°C. Fluorescence emission spectra showed tryptophan residues partially buried within the lectin structure. The percentages of secondary structure revealed by circular dichroism were 1% α-helix, 44% β-sheet, 24% β-turn and 31% unordered. BlL showed effective antibacterial activity against Gram-positive bacteria Staphylococcus aureus, Enterococcus faecalis and Bacillus subtilis with minimal inhibitory concentrations of 31.25, 62.25 and 125 μg/mL, respectively. In conclusion, B. leucurus snake venom contains a galactoside-binding lectin with antibacterial activity.
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