| Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: Phospholipase A2 and L-amino acid oxidase. | |
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MedLine Citation:
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PMID: 19944711 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Some 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 microg/mL and MLC=200 microg/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 IC(50)=2.55 microg/mL and 2.86 microg/mL for L. amazonensis and L. chagasi, respectively. BmarTV also provided significant inhibition of parasitic growth, with an IC(50) of 86.56 microg/mL for L. amazonensis and 79.02 microg/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. |
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Authors:
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Alba Fabiola Costa Torres; Rodrigo Tavares Dantas; Marcos H Toyama; Eduardo Diz Filho; Fernando Jos? Zara; Maria Goretti Rodrigues de Queiroz; Nadia Accioly Pinto Nogueira; M?rcia Rosa de Oliveira; Daniela de Oliveira Toyama; Helena S A Monteiro; Alice M C Martins |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-11-26 |
Journal Detail:
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Title: Toxicon : official journal of the International Society on Toxinology Volume: 55 ISSN: 1879-3150 ISO Abbreviation: Toxicon Publication Date: 2010 Apr |
Date Detail:
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Created Date: 2010-02-17 Completed Date: 2010-06-14 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 1307333 Medline TA: Toxicon Country: England |
Other Details:
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Languages: eng Pagination: 795-804 Citation Subset: IM |
Copyright Information:
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Copyright 2009 Elsevier Ltd. All rights reserved. |
Affiliation:
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Post-graduate Program in Pharmaceutical Sciences, Pharmacy Faculty, Federal University of Cear?, Fortaleza, Cear?, Brazil. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Anti-Bacterial Agents / pharmacology* Antiprotozoal Agents / pharmacology* Bothrops Chromatography, DEAE-Cellulose Chromatography, High Pressure Liquid Crotalid Venoms / chemistry, enzymology, pharmacology* Electrophoresis, Polyacrylamide Gel L-Amino Acid Oxidase / chemistry, pharmacology* Macrophages / drug effects Microbial Sensitivity Tests Molecular Sequence Data Phospholipases A2 / chemistry, pharmacology* Sequence Homology, Amino Acid |
| Chemical | |
Reg. No./Substance:
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0/Anti-Bacterial Agents; 0/Antiprotozoal Agents; 0/Crotalid Venoms; EC 1.4.3.2/L-Amino Acid Oxidase; EC 3.1.1.4/Phospholipases A2 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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