An acidic phospholipase A2 with antibacterial activity from Porthidium nasutum snake venom

Vargas, Leidy Johana; LONDOÑO, Mónica; Quintana, Juan Carlos López; Rúa, Carolina; Segura, Cesar; Lomonte, Bruno; Núñez, Vitelbina

doi:10.1016/j.cbpb.2011.12.010

Cited by 49 publications

(33 citation statements)

References 42 publications

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“…Which was higher than that of other snakes venom, such as Porthidium nasutum snake venom has molecular mass of 15,802.6 Da migrates a single band under both non-reducing and reducing conditions, Piper umbellatum and Piper peltatum untreated toxin migrated as *15 kDa under reducing conditions and corresponding to the mass of its monomeric subunits in SDS-PAGE. In nonreducing condition, the spanning was reported as 28 kDa (homodimer) to 15 kDa (monomer) [17,18].…”

Section: Determination Of Molecular Weightmentioning

confidence: 99%

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

et al. 2015

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This study is designed to isolate and purify a novel anti-clotting protein component from the venom of Enhydrina schistosa, and explore its biochemical and biological activities. The active protein was purified from the venom of E. schistosa by ion-exchange chromatography using DEAE-cellulose. The venom protein was tested by various parameters such as, proteolytic, haemolytic, phospholipase and anti-coagulant activities. 80 % purity was obtained in the final stage of purification and the purity level of venom was revealed as a single protein band of about 44 kDa in SDS-polyacrylamide electrophoresis under reducing conditions. The results showed that the Potent hemolytic activity was observed against cow, goat, chicken and human (A, B and O positive) erythrocytes. Furthermore, the clotting assays showed that the venom of E. schistosa significantly prolonged in activated partial thromboplastin time, thrombin time, and prothrombin time. Venomous enzymes which hydrolyzed casein and gelatin substrate were found in this venom protein. Gelatinolytic activity was optimal at pH 5-9 and 1 H NMR analysis of purified venom was the base line information for the structural determination. These results suggested that the E. schistosa venom holds good promise for the development of novel lead compounds for pharmacological applications in near future.

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Section: Determination Of Molecular Weightmentioning

confidence: 99%

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

et al. 2015

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“…In particular, many of the myotoxic snake venom (sv) PLA 2 s possess bactericidal activity based on common effects of group II PLA 2 s [44]. Bactericidal effects of Porthidium nasutum phospholipase A 2 (PnPLA 2 ) occur against S. aureus but not Escherichia coli at a 32 mg/ml dose [45].…”

Section: Antimicrobial Activity Of Pla 2 Smentioning

confidence: 99%

Novel phospholipase A2 inhibitors from python serum are potent peptide antibiotics

et al. 2015

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“…Snake venom PLA 2 are enzymes that are able to resist extreme chemical conditions, such as low pH, higher ion concentrations and temperature, among others [21,22]. In addition, several studies have demonstrated that snake venom PLA 2 can be purified by HPLC using acetonitrile without changes in their enzyme and biological activities [21,23,24].…”

Section: Purification Of Pla 2 Smentioning

confidence: 99%

CHARACTERIZATION OF THE MOST PROMISING FRACTION OF Swietenia macrophylla ACTIVE AGAINST MYOTOXIC PHOSPHOLIPASES A2 : IDENTIFICATION OF CATECHIN AS ONE OF THE ACTIVE COMPOUNDS

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et al. 2016

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Background: The pharmacological effects produced by snakebite accidents involve the actions of several enzymes, of which those of the phospholipases A 2 (PLA 2 ) exhibit a wide variety of effects such as edema and myotoxicity. Some plant extracts have been antagonists of crude snake venoms and toxins. Based on promising bioactivity, Swietenia macrophylla King was selected for further studies. Objective: The purpose of this study was to identify the PLA 2 inhibitors present in the crude extract of S. macrophylla that could be promising leads in neutralizing the local effects of ophidian accidents. Methods: Bioassay-guided fractionation of the ethanolic extract of the leaves of S. macrophylla lead to the detection of (+)-catechin, characterized through gas chromatography coupled with mass spectrometry (GC-MS), and confirmed by HPLC. The PLA 2 inhibitory activity was measured with the Dole method and a spectrophotometric assay with 4-Nitro-3-octanoyloxy-benzoic acid (4N3OBA). Cytotoxicity was done on C2C12 murine myoblast. Results: Fraction F5 and (+)-Catechin inhibited the PLA 2 activity of B. asper venom, in a dosedependent way. In addition, (+)-Catechin showed an inhibition level of 83.1 ± 3.1 % of the enzymatic activity of one PLA 2 purified from the venom of Crotalus durissus cumanensis using 4N3OBA as substrate. Also the ethanolic extract and fraction F5 showed inhibition of the cytotoxicity induced by the Bothrops atrox venom and their Lys 49 PLA 2 (80 and 100% respectively). Molecular docking results suggested that OH from 4´ and 5' carbons of (+)-catechin could form hydrogen bonds with carboxylate moiety of residue Asp49, while OH from 5 could form a hydrogen bond with Asn 6. Additional Van der Waals interactions were also proposed. Conclusion: Swietenia macrophylla exhibited strong inhibitory activity against PLA 2 s enzymes. Catechin, one of the components in the active fraction F5, is proposed as being partially responsible for the bioactivity.

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An acidic phospholipase A2 with antibacterial activity from Porthidium nasutum snake venom

Cited by 49 publications

References 42 publications

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

Novel phospholipase A2 inhibitors from python serum are potent peptide antibiotics

CHARACTERIZATION OF THE MOST PROMISING FRACTION OF Swietenia macrophylla ACTIVE AGAINST MYOTOXIC PHOSPHOLIPASES A2 : IDENTIFICATION OF CATECHIN AS ONE OF THE ACTIVE COMPOUNDS

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