Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2011 |
| Outros Autores: | , , , , , , , , , , |
| Tipo de documento: | Artigo |
| Idioma: | eng |
| Título da fonte: | Repositório Institucional da UNIFESP |
| Texto Completo: | http://dx.doi.org/10.1016/j.cbpb.2011.02.001 http://repositorio.unifesp.br/handle/11600/33645 |
Resumo: | 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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Purification of a lectin with antibacterial activity from Bothrops leucurus snake venomAntibacterial activityFluorescenceCircular dichroismBothrops leucurusLectinSnake venomA 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.Univ Fed Pernambuco, Dept Bioquim, BR-50670420 Recife, PE, BrazilUniv Fed Bahia, Dept Zool, BR-40170210 Salvador, BA, BrazilUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, BrazilUniv Fed Pernambuco, Dept Zool, BR-50670420 Recife, PE, BrazilUniv Estadual Oeste Parana, Ctr Engn & Ciencias Exatas, BR-85903000 Toledo, Parana, BrazilUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, BrazilWeb of ScienceConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Elsevier B.V.Universidade Federal de Pernambuco (UFPE)Universidade Federal da Bahia (UFBA)Universidade Federal de São Paulo (UNIFESP)Univ Estadual Oeste ParanaNunes, Erika dos SantosAranda de Souza, Mary AngelaMelo Vaz, Antonio Fernando deSa Santana, Giselly Maria deGomes, Francis SoaresBreitenbach Barroso Coelho, Luana CassandraGuedes Paiva, Patricia MariaLira da Silva, Rejane MariaSilva-Lucca, Rosemeire Aparecida [UNIFESP]Oliva, Maria Luiza Vilela [UNIFESP]Guarnieri, Miriam CamargoSantos Correia, Maria Tereza dos2016-01-24T14:06:26Z2016-01-24T14:06:26Z2011-05-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion57-63application/pdfhttp://dx.doi.org/10.1016/j.cbpb.2011.02.001Comparative Biochemistry and Physiology B-biochemistry & Molecular Biology. New York: Elsevier B.V., v. 159, n. 1, p. 57-63, 2011.10.1016/j.cbpb.2011.02.001WOS000289448600007.pdf1096-4959http://repositorio.unifesp.br/handle/11600/33645WOS:000289448600007engComparative Biochemistry and Physiology B-biochemistry & Molecular Biologyinfo:eu-repo/semantics/openAccesshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-07-31T19:49:52Zoai:repositorio.unifesp.br/:11600/33645Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-07-31T19:49:52Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
| dc.title.none.fl_str_mv |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
| title |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
| spellingShingle |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom Nunes, Erika dos Santos Antibacterial activity Fluorescence Circular dichroism Bothrops leucurus Lectin Snake venom |
| title_short |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
| title_full |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
| title_fullStr |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
| title_full_unstemmed |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
| title_sort |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
| author |
Nunes, Erika dos Santos |
| author_facet |
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 |
| author_role |
author |
| author2 |
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 |
| author2_role |
author author author author author author author author author author author |
| dc.contributor.none.fl_str_mv |
Universidade Federal de Pernambuco (UFPE) Universidade Federal da Bahia (UFBA) Universidade Federal de São Paulo (UNIFESP) Univ Estadual Oeste Parana |
| dc.contributor.author.fl_str_mv |
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 |
| dc.subject.por.fl_str_mv |
Antibacterial activity Fluorescence Circular dichroism Bothrops leucurus Lectin Snake venom |
| topic |
Antibacterial activity Fluorescence Circular dichroism Bothrops leucurus Lectin Snake venom |
| description |
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. |
| publishDate |
2011 |
| dc.date.none.fl_str_mv |
2011-05-01 2016-01-24T14:06:26Z 2016-01-24T14:06:26Z |
| dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
| dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.cbpb.2011.02.001 Comparative Biochemistry and Physiology B-biochemistry & Molecular Biology. New York: Elsevier B.V., v. 159, n. 1, p. 57-63, 2011. 10.1016/j.cbpb.2011.02.001 WOS000289448600007.pdf 1096-4959 http://repositorio.unifesp.br/handle/11600/33645 WOS:000289448600007 |
| url |
http://dx.doi.org/10.1016/j.cbpb.2011.02.001 http://repositorio.unifesp.br/handle/11600/33645 |
| identifier_str_mv |
Comparative Biochemistry and Physiology B-biochemistry & Molecular Biology. New York: Elsevier B.V., v. 159, n. 1, p. 57-63, 2011. 10.1016/j.cbpb.2011.02.001 WOS000289448600007.pdf 1096-4959 WOS:000289448600007 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
Comparative Biochemistry and Physiology B-biochemistry & Molecular Biology |
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info:eu-repo/semantics/openAccess http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
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openAccess |
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http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
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57-63 application/pdf |
| dc.publisher.none.fl_str_mv |
Elsevier B.V. |
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Elsevier B.V. |
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reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
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Universidade Federal de São Paulo (UNIFESP) |
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UNIFESP |
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UNIFESP |
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Repositório Institucional da UNIFESP |
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Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
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biblioteca.csp@unifesp.br |
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1814268402218303488 |