Renal and antibacterial effects induced by myotoxin I and II isolated from Bothrops jararacussu venom

Barbosa, Paula; Martins, Alice Maria Costa; Havt, Alexandre; Toyama, Daniela O.; Evangelista, Janaína Serra Azul Monteiro; Ferreira, Débora Paula; Joazeiro, Paulo Pinto; Beriam, L. O. S.; Toyama, Marcos Hikari; Fonteles, M. C.; Monteiro, Helena Serra Azul

doi:10.1016/j.toxicon.2005.04.024

Cited by 49 publications

(21 citation statements)

References 35 publications

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“…This effect could be due to the perturbing action exerted by the PLA 2 homologue in the plasma membrane, thus resulting in an increase in permeability [29]. It has been shown that the C -terminal region of these PLA 2 homologues is responsible for this catalytically-independent membrane perturbation, as demonstrated in bacteria [16,30,31], being, therefore, a different mechanism from the one described for other PLA 2 s [26,27]. …”

Section: Resultsmentioning

confidence: 99%

“…Secreted PLA 2 s (sPLA 2 ) share several characteristics: low molecular mass (13–18 kDa), numerous disulfide bonds, histidyl and aspartyl catalytic residues and a highly conserved calcium (Ca 2+ ) binding region [13,14]. PLA 2 s from snake venom exhibit a variety of pharmacological/toxicological activities, such as myotoxicity, neurotoxicity, anticoagulant activity, edema-forming activity, cardiotoxicity, antibacterial activity, antiparasite effect and anti-aggregation activity on platelets, among others [15,16,17,18,19,20,21,22,23,24,25]. …”

Section: Introductionmentioning

confidence: 99%

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In Vitro Antiplasmodial Activity of Phospholipases A2 and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper

Castillo

Vargas

Segura

et al. 2012

Toxins

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The antimicrobial and antiparasite activity of phospholipase A2 (PLA2) from snakes and bees has been extensively explored. We studied the antiplasmodial effect of the whole venom of the snake Bothrops asper and of two fractions purified by ion-exchange chromatography: one containing catalytically-active phospholipases A2 (PLA2) (fraction V) and another containing a PLA2 homologue devoid of enzymatic activity (fraction VI). The antiplasmodial effect was assessed on in vitro cultures of Plasmodium falciparum. The whole venom of B. asper, as well as its fractions V and VI, were active against the parasite at 0.13 ± 0.01 µg/mL, 1.42 ± 0.56 µg/mL and 22.89 ± 1.22 µg/mL, respectively. Differences in the cytotoxic activity on peripheral blood mononuclear cells between the whole venom and fractions V and VI were observed, fraction V showing higher toxicity than total venom and fraction VI. Regarding toxicity in mice, the whole venom showed the highest lethal effect in comparison to fractions V and VI. These results suggest that B. asper PLA2 and its homologue have antiplasmodial potential.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

In Vitro Antiplasmodial Activity of Phospholipases A2 and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper

Castillo

Vargas

Segura

et al. 2012

Toxins

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“…Myotoxin I Lys 49 PLA 2 from Bothrops atrox venom was weakly bactericidal against E. coli [30]. Myotoxin I Lys 49 PLA 2 and myotoxin II Asp 49 PLA 2 from Bothrops jararacussu venom showed antibacterial effect against gram-negative bacteria Xanthomonas [54]. Myotoxic Asp 49 PLA 2 MTX-I and Lys 49 PLA 2 MTX-II isolated from Botrops brazili venom and cationic synthetic peptides derived from their 115–129 C -terminal region displayed toxic effects against E. coli , Candida albicans and Leishmania sp .…”

Section: Discussionmentioning

confidence: 99%

Interactions of PLA2-s from Vipera lebetina, Vipera berus berus and Naja naja oxiana Venom with Platelets, Bacterial and Cancer Cells

Samel

Vija

Kurvet

et al. 2013

Toxins

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Secretory phospholipasesA2 (sPLA2s) form a large family of structurally related enzymes widespread in nature. Herein, we studied the inhibitory effects of sPLA2s from Vipera lebetina (VLPLA2), Vipera berus berus (VBBPLA2), and Naja naja oxiana (NNOPLA2) venoms on (i) human platelets, (ii) four different bacterial strains (gram-negative Escherichia coli and Vibrio fischeri; gram-positive Staphylococcus aureus and Bacillus subtilis) and (iii) five types of cancer cells (PC-3, LNCaP, MCF-7, K-562 and B16-F10) in vitro. sPLA2s inhibited collagen-induced platelet aggregation: VBBPLA2 IC50 = 0.054, VLPLA2 IC50 = 0.072, NNOPLA2 IC50 = 0.814 μM. p-Bromophenacylbromide-inhibited sPLA2 had no inhibitory action on platelets. 36.17 μM VBBPLA2 completely inhibited the growth of gram-positive Bacillus subtilis whereas no growth inhibition was observed towards gram-negative Escherichia coli. The inhibitory action of sPLA2s (~0.7 μM and ~7 μM) towards cancer cells depended on both venom and cell type. VBBPLA2 (7.2 μM) inhibited significantly the viability of K-562 cells and the cell death appeared apoptotic. The sPLA2s exhibited no inhibitory effect towards LNCaP cells and some effect (8%–20%) towards other cells. Thus, already sub-μM concentrations of sPLA2s inhibited collagen-induced platelet aggregation and from the current suite of studied svPLA2s and test cells, VBBPLA2 was the most growth inhibitory towards Bacillus subtilis and K-562 cells.

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“…On the other hand, BthTX-I (Lys 49 ) and BthTX-II (Asp 49 ) purified from Bothrops jararacussu exhibit antibacterial effects against Xanthomonas axonopodis passiflorae passiflorae (a Gram-negative bacterium) at 125 g/ml. Treatment with 4-bromophenacyl bromide ( -BPB) significantly decreases (37%) the antibacterial effect of both PLA 2 s [95]. Recently reported bactericidal potential were obtained by cloning and expression using an important techniques for obtaining new drugs based on natural molecules including PLA 2 s. The recombinant BmooPLA 2 (B. moojeni snake venom) showed phospholipase and inhibitory activities similar to native protein [96].…”

Section: B Lys 49 and Asp 49 Pla 2 S As Antimicrobial Agentsmentioning

confidence: 99%

Snake Venom Phospholipases A2: A Novel Tool Against Bacterial Diseases

Samy¹,

Gopalakrishnakone²,

Stiles³

et al. 2012

Current Medicinal Chemistry

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The majority of snake venom phospholipases A(2) (svPLA(2)s) are toxic and induce a wide spectrum of biological effects. They are cysteine-rich proteins that contain 119-134 amino acids and share similar structures and functions. About 50% of the residues are incorporated into α-helices, whereas only 10% are in β-sheets. Fourteen conserved cysteines form a network of seven disulfide bridges that stabilize the tertiary structure. They show a high degree of sequence and structural similarity, and are believed to have a common calcium- dependent catalytic mechanism. Additionally, svPLA(2)s display an array of biological actions that are either dependent or independent of catalysis. The PLA(2)s of mammalian origin also exert potent bactericidal activity by binding to anionic surfaces and enzymatic degradation of phospholipids in the target membranes, preferentially of Gram-positive species. The bactericidal activity against Gram-negatives by svPLA(2) requires a synergistic action with bactericidal/permeability-increasing protein (BPI), but is equally dependent on enzymatic- based membrane degradation. Several hypotheses account for the bactericidal properties of svPLA(2)s, which include "fatal depolarization" of the bacterial membrane, creation of physical holes in the membrane, scrambling of normal distribution of lipids between the bilayer leaflets, and damage of critical intracellular targets after internalization of the peptide. The present review discusses several svPLA(2)s and derived peptides that exhibit strong bactericidal activity. The reports demonstrate that svPLA(2)-derived peptides have the potential to counteract microbial infections. In fact, the C-terminal cationic/hydrophobic segment (residues 115-129) of svPLA(2)s is bactericidal. Thus identification of the bactericidal sites in svPLA(2)s has potential for developing novel antimicrobials.

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Renal and antibacterial effects induced by myotoxin I and II isolated from Bothrops jararacussu venom

Cited by 49 publications

References 35 publications

In Vitro Antiplasmodial Activity of Phospholipases A2 and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper

In Vitro Antiplasmodial Activity of Phospholipases A2 and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper

Interactions of PLA2-s from Vipera lebetina, Vipera berus berus and Naja naja oxiana Venom with Platelets, Bacterial and Cancer Cells

Snake Venom Phospholipases A2: A Novel Tool Against Bacterial Diseases

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