Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom

A novel lectin was isolated from Bothrops leucurus snake venom using a combination of affinity and gel filtration chromatographies. the lectin (BIL) agglutinated glutaraldehyde-treated rabbit and human erythrocytes with preference for rabbit erythrocytes. Galactose, raffinose, lactose, fetal bovine...

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Detalles Bibliográficos
Autores: Nunes, Erika dos Santos, Aranda de Souza, Mary Angela, Melo Vaz, Antonio Fernando de, Sa Santana, Giselly Maria de, Gomes, Francis Soares, Breitenbach Barroso Coelho, Luana Cassandra, Guedes Paiva, Patricia Maria, Lira da Silva, Rejane Maria, Silva-Lucca, Rosemeire Aparecida [UNIFESP], Oliva, Maria Luiza Vilela [UNIFESP], Guarnieri, Miriam Camargo, Santos Correia, Maria Tereza dos
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2011
País:Brasil
Institución:Universidade Federal de São Paulo (UNIFESP)
Repositorio:Repositório Institucional da UNIFESP
Idioma:inglés
OAI Identifier:oai:repositorio.unifesp.br:11600/33645
Acceso en línea:http://dx.doi.org/10.1016/j.cbpb.2011.02.001
http://repositorio.unifesp.br/handle/11600/33645
Access Level:acceso abierto
Palabra clave:Antibacterial activity
Fluorescence
Circular dichroism
Bothrops leucurus
Lectin
Snake venom
Descripción
Sumario:A novel lectin was isolated from Bothrops leucurus snake venom using a combination of affinity and gel filtration chromatographies. the lectin (BIL) 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. BIL, with a molecular mass of 30 kDa and composed of two subunits of 15 kDa, showed dependence on calcium. BIL is an acidic protein with highest activity over the pH range of 4.0-7.0 and stable under heating to 70 degrees C. Fluorescence emission spectra showed tryptophan residues partially buried within the lectin structure. the percentages of secondary structure revealed by circular dichroism were 1% alpha-helix, 44% beta-sheet, 24% beta-turn and 31% unordered. BIL 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 mu g/mL, respectively. in conclusion, B. leucurus snake venom contains a galactoside-binding lectin with antibacterial activity. (C) 2011 Elsevier Inc. All rights reserved.

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