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dc.contributor.authorCosta Torres, Alba Fabiola-
dc.contributor.authorDantas, Rodrigo Tavares-
dc.contributor.authorToyama, Marcos H.-
dc.contributor.authorDiz Filho, Eduardo-
dc.contributor.authorZara, Fernando Jose-
dc.contributor.authorRodrigues de Queiroz, Maria Goretti-
dc.contributor.authorPinto Nogueira, Nadia Accioly-
dc.contributor.authorde Oliveira, Marcia Rosa-
dc.contributor.authorToyama, Daniela de Oliveira-
dc.contributor.authorMonteiro, Helena S. A.-
dc.contributor.authorMartins, Alice M. C.-
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V. Ltd, v. 55, n. 4, p. 795-804, 2010.-
dc.description.abstractSome proteins present in snake venom possess enzymatic activities, such as phospholipase A(2) and L-amino acid oxidase. In this study, we verify the action of the Bothrops marajoensis venom (BmarTV), PLA(2) (BmarPLA(2)) and LAAO (BmarLAAO) on strains of bacteria, yeast, and Leishmania sp. The BmarTV was isolated by Protein Pack 5PW, and several fractions were obtained. Reverse phase HPLC showed that BmarPLA(2) was isolated from the venom, and N-terminal amino acid sequencing of sPLA(2) showed high amino acid identity with other lysine K49 sPLA(2)s isolated from Bothrops snakes. The BmarLAAO was purified to high molecular homogeneity and its N-terminal amino acid sequence demonstrated a high degree of amino acid conservation with others LAAOs. BmarLAAO was able to inhibit the growth of P. aeruginosa, C. albicans and S. aureus in a dose-dependent manner. The inhibitory effect was more significant on S. aureus, with a MIC = 50 mu g/mL and MLC = 200 mu g/mL However, the BmarTV and BmarPLA(2) did not demonstrate inhibitory capacity. BmarLAAO was able to inhibit the growth of promastigote forms of L chagasi and L amazonensis, with an IC50 = 2.55 mu g/mL and 2.86 mu g/mL for L. amazonensis and L. chagasi, respectively. BmarTV also provided significant inhibition of parasitic growth, with an IC50 of 86.56 mu g/mL for L. amazonensis and 79.02 mu g/mL for L chagasi. BmarPLA(2) did not promote any inhibition of the growth of these parasites. The BmarLAAO and BmarTV presented low toxicity at the concentrations studied. In conclusion, whole venom as well as the L-amino acid oxidase from Bothrops marajoensis was able to inhibit the growth of several microorganisms, including S. aureus, Candida albicans, Pseudomonas aeruginosa, and Leishmania sp. (C) 2009 Elsevier Ltd. All rights reserved.en
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.publisherPergamon-Elsevier B.V. Ltd-
dc.sourceWeb of Science-
dc.subjectL-amino acid oxidaseen
dc.subjectPhospholipases A(2)en
dc.subjectBothrops marajoensisen
dc.titleAntibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: Phospholipase A(2) and L-amino acid oxidaseen
dc.contributor.institutionUniversidade Federal do Ceará (UFC)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)-
dc.contributor.institutionUniversidade Federal da Paraíba (UFPB)-
dc.contributor.institutionUniv Prebiteriana Mackenzie-
dc.description.affiliationUniversidade Federal do Ceará (UFC), Dept Clin & Toxicol Anal, Fac Pharm, Postgrad Program Pharmaceut Sci, BR-60420970 Fortaleza, Ceara, Brazil-
dc.description.affiliationUniversidade Federal do Ceará (UFC), Dept Physiol & Pharmacol, BR-60420970 Fortaleza, Ceara, Brazil-
dc.description.affiliationPaulista State Univ UNESP, Cell Biol & Chem Prot & Peptides Lab, São Paulo, Brazil-
dc.description.affiliationUniv Estadual Campinas, Inst Biol, Dept Biochem, São Paulo, Brazil-
dc.description.affiliationUniversidade Federal da Paraíba (UFPB), Dept Mol Biol, Ctr Exact Sci & Nat, BR-58059900 Joao Pessoa, Paraiba, Brazil-
dc.description.affiliationUniv Prebiteriana Mackenzie, Biol & Hlth Sci Ctr, São Paulo, Brazil-
dc.description.affiliationUnespPaulista State Univ UNESP, Cell Biol & Chem Prot & Peptides Lab, São Paulo, Brazil-
dc.rights.accessRightsAcesso restrito-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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