Antimicrobial activity of an l-amino acid oxidase isolated from bothrops leucurus snake venom

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorFederal University of Ceará-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade Estadual de Campinas (UNICAMP)-
Autor(es): dc.contributorFederal University of Paraíba-
Autor(es): dc.creatorTorres, A. F.C.-
Autor(es): dc.creatorDantas, R. T.-
Autor(es): dc.creatorMenezes, R. R.P.P.B.-
Autor(es): dc.creatorToyama, M. H.-
Autor(es): dc.creatorFilho, E. D.-
Autor(es): dc.creatorOliveira, M. F.-
Autor(es): dc.creatorNogueira, N. A.P.-
Autor(es): dc.creatorOliveira, M. R.-
Autor(es): dc.creatorMonteiro, H. S.A.-
Autor(es): dc.creatorMartins, A. M.C.-
Data de aceite: dc.date.accessioned2025-08-21T18:41:53Z-
Data de disponibilização: dc.date.available2025-08-21T18:41:53Z-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2010-01-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1590/S1678-91992010000400012-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/226164-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/226164-
Descrição: dc.descriptionSome snake venom proteins present enzymatic activities, such as L-amino acid oxidase (LAAO). The aim of this paper was to investigate the effect of Bothrops leucurus total venom (BleuTV) and its fraction LAAO (BleuLAAO) on bacteria, yeast, and promastigote forms of Leishmania amazonensis and Leishmania chagasi, and epimastigote forms of Trypanosoma cruzi. BleuTV was isolated with a Protein Pack 5PW®(Waters Corporation, USA), and several fractions were obtained. BleuLAAO was purified to high molecular homogeneity, and its N-terminal amino acid sequence shared a high degree of amino acid conservation with other LAAOs. BleuTV inhibited Staphylococcus aureus growth in a dose-dependent manner, with a minimum inhibitory concentration (MIC) of 25 μg/mL, which corresponded to its minimum lethal concentration (MLC). BleuTV also inhibited the growth of promastigote forms of L. chagasi and L. amazonensis, with respective IC50 values of 1.94 μg/mL and 5.49 μg/mL. Furthermore, it repressed T. cruzi growth with an IC50 of 1.14 μg/mL. However, BleuLAAO did not inhibit the growth of the microorganisms studied and was not toxic to macrophages. BleuTV had low toxicity against macrophages at the concentrations studied. In conclusion, whole venom from Bothrops leucurus inhibited the growth of some microorganisms, including S. aureus, Leishmania sp., and T. cruzi. © CEVAP 2010.-
Descrição: dc.descriptionDepartment of Clinical and Toxicological Analysis School of Pharmacy Federal University of Ceará, Fortaleza, Ceará State-
Descrição: dc.descriptionDepartment of Physiology and Pharmacology Federal University of Ceará, Fortaleza, Ceará State-
Descrição: dc.descriptionLaboratory of Cell Biology and Chemistry for Proteins and Peptides São Paulo Experimental Coast Campus São Paulo State University (UNESP - Univ Estadual Paulista), São Vicente, São Paulo State-
Descrição: dc.descriptionDepartment of Biochemistry Institute of Biology State University of Campinas UNICAMP Campinas, São Paulo State-
Descrição: dc.descriptionDepartment of Molecular Biology Center of Exact Sciences and Nature Federal University of Paraíba, João Pessoa, Paraíba State-
Descrição: dc.descriptionLaboratory of Cell Biology and Chemistry for Proteins and Peptides São Paulo Experimental Coast Campus São Paulo State University (UNESP - Univ Estadual Paulista), São Vicente, São Paulo State-
Formato: dc.format614-622-
Idioma: dc.languageen-
Relação: dc.relationJournal of Venomous Animals and Toxins Including Tropical Diseases-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAntimicrobial activity-
Palavras-chave: dc.subjectBothrops leucurus-
Palavras-chave: dc.subjectL-amino oxidase-
Título: dc.titleAntimicrobial activity of an l-amino acid oxidase isolated from bothrops leucurus snake venom-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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