title: Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: Phospholipase A2 and L-amino acid oxidase.
abstract: 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.
authors: Post-graduate Program in Pharmaceutical Sciences, Pharmacy Faculty, Federal University of Ceará, Fortaleza, Ceará, Brazil.
authors: Alba Fabiola
authors: AF
authors: Costa Torres
authors: Rodrigo Tavares
authors: RT
authors: Dantas
authors: Marcos H
authors: MH
authors: Toyama
authors: Eduardo
authors: E
authors: Diz Filho
authors: Fernando José
authors: FJ
authors: Zara
authors: Maria Goretti
authors: MG
authors: Rodrigues de Queiroz
authors: Nadia Accioly
authors: NA
authors: Pinto Nogueira
authors: Márcia
authors: M
authors: Rosa de Oliveira
authors: Daniela
authors: D
authors: de Oliveira Toyama
authors: Helena S A
authors: HS
authors: Monteiro
authors: Alice M C
authors: AM
authors: Martins
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D000981:Antiprotozoal Agents / Q000494:pharmacology*; D017837:Bothrops; D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D003435:Crotalid Venoms / Q000737:chemistry / Q000201:enzymology / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D050830:L-Amino Acid Oxidase / Q000737:chemistry / Q000494:pharmacology*; D008264:Macrophages / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D054467:Phospholipases A2 / Q000737:chemistry / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid
chemical_list: D000900:Anti-Bacterial Agents; D000981:Antiprotozoal Agents; D003435:Crotalid Venoms; D050830:L-Amino Acid Oxidase; D054467:Phospholipases A2