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

dc.contributor.authorTorres, A. F.C.
dc.contributor.authorDantas, R. T.
dc.contributor.authorMenezes, R. R.P.P.B.
dc.contributor.authorToyama, M. H. [UNESP]
dc.contributor.authorFilho, E. D.
dc.contributor.authorOliveira, M. F.
dc.contributor.authorNogueira, N. A.P.
dc.contributor.authorOliveira, M. R.
dc.contributor.authorMonteiro, H. S.A.
dc.contributor.authorMartins, A. M.C.
dc.contributor.institutionFederal University of Ceará
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionFederal University of Paraíba
dc.date.accessioned2022-04-28T21:39:41Z
dc.date.available2022-04-28T21:39:41Z
dc.date.issued2010-01-01
dc.description.abstractSome 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.en
dc.description.affiliationDepartment of Clinical and Toxicological Analysis School of Pharmacy Federal University of Ceará, Fortaleza, Ceará State
dc.description.affiliationDepartment of Physiology and Pharmacology Federal University of Ceará, Fortaleza, Ceará State
dc.description.affiliationLaboratory 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
dc.description.affiliationDepartment of Biochemistry Institute of Biology State University of Campinas UNICAMP Campinas, São Paulo State
dc.description.affiliationDepartment of Molecular Biology Center of Exact Sciences and Nature Federal University of Paraíba, João Pessoa, Paraíba State
dc.description.affiliationUnespLaboratory 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
dc.format.extent614-622
dc.identifierhttp://dx.doi.org/10.1590/S1678-91992010000400012
dc.identifier.citationJournal of Venomous Animals and Toxins Including Tropical Diseases, v. 16, n. 4, p. 614-622, 2010.
dc.identifier.doi10.1590/S1678-91992010000400012
dc.identifier.issn1678-9199
dc.identifier.scopus2-s2.0-78650332067
dc.identifier.urihttp://hdl.handle.net/11449/226164
dc.language.isoeng
dc.relation.ispartofJournal of Venomous Animals and Toxins Including Tropical Diseases
dc.sourceScopus
dc.subjectAntimicrobial activity
dc.subjectBothrops leucurus
dc.subjectL-amino oxidase
dc.titleAntimicrobial activity of an l-amino acid oxidase isolated from bothrops leucurus snake venomen
dc.typeArtigo
dspace.entity.typePublication
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, São Vicentept
unesp.departmentCiências Biológicas - IBCLPpt

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