Biochemical and biological characterization of a PLA2 from crotoxin complex of Crotalus durissus cumanensis

Pereañez, Jaime Andrés; Núñez, Vitelbina; Huancahuire-Vega, Salomón; Marangoni, Sérgio; Ponce-Soto, Luis Alberto

doi:10.1016/j.toxicon.2009.01.021

Cited by 48 publications

(43 citation statements)

References 42 publications

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“…Edema activity has been associated to metalloproteinases that also cause hemorrhage. Therefore, the absence of hemorrhagic activity in these venoms may suggest that the edema is induced by proteins different from these proteinases with edematous activity like myotoxins and phospholipases A 2 (19,20,30). In previous studies with C. durissus venoms from other South American regions, no edematous or hemorrhagic activity was observed (9)(10)(11)31).…”

Section: Discussionmentioning

confidence: 92%

“…Recent studies on the biochemical functional characterization of C. durissus cumanensis venom from Venezuela have indicated high intraspecies variability whereas different isoforms of crotoxin complex from this venom have been isolated, purified and characterized by other researchers (16)(17)(18)(19)(20)(21). In the current study, we present preliminary chemical and functional characterization of venom obtained from a snake family composed of adult C. durissus cumanensis (parents), captured in different regions of Colombia, and from six young offspring born in captivity.…”

Section: Introductionmentioning

confidence: 99%

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Biochemical comparison of venoms from young Colombian Crotalus durissus cumanensis and their parents

Céspedes

Castro

Jimenez³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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ABSTRACT:Crotalus durissus cumanensis, a rattlesnake endemic to Colombia and Venezuela, is considered one of the most lethal snake species in Latin America. The aim of the present study was to compare the protein content and biological activity of the venom obtained from eight specimens of C. durissus cumanensis, namely two adults from different localities of Colombia and six offspring born in captivity. Protein profiles of crude venoms were analyzed by SDS-PAGE and RP-HPLC, and biological activities were evaluated for lethality, edema, defibrination, hemolytic and coagulant activities to assess individual venoms of adults and a pool of young snake venoms. Transient edema appeared rapidly after venom inoculation, whereas hemorrhagic effect was not observed. Differences in protein profiles, lethality, hemolytic, coagulant and defibrinating activities between both adult snake venoms were observed; those from the mother snake exhibited higher activities. Venoms from young snakes were similar to the one obtained from the mother, but the coagulant effect was stronger in offspring venoms. Notably, biological effects of the father snake venom were not comparable to those previously described for C. durissus cumanensis from Venezuela and C. durissus terrificus from Brazil, confirming the high variability of the venom from Crotalus species.

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Section: Discussionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Biochemical comparison of venoms from young Colombian Crotalus durissus cumanensis and their parents

Céspedes

Castro

Jimenez³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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“…Peak of interest were purified by reverse-phase HPLC on C 18 column eluted at 1 mL/min with a gradient from 0% to 100% acetonitrile in 0.1% trifluoroacetic acid (v/v). Absorbance in the effluent solution was recorded at 280 nm [21]. 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].…”

Section: Purification Of Pla 2 Smentioning

confidence: 99%

“…Absorbance in the effluent solution was recorded at 280 nm [21]. 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%

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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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Pereañez

Núñez

et al. 2016

Vitae

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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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Biochemical and pharmacological characterization of Trimersurus malabaricus snake venom

Gowda

Rajesh

Angaswamy

et al. 2018

J of Cellular Biochemistry

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Trimeresurus malabaricus is a venomous pit viper species endemic to southwestern part of India. In earlier reports, we have shown that envenomation by T. malabaricus venom leading to strong local tissue damage but the mechanism of action is not clearly revealed. Local tissue damage affected by T. malabaricus venom is of great importance since the poison has serious systemic effects including death in the case of multiple attacks. The present study details the major manifestations of T. malabaricus venom and the induction of local tissue damage, which suggests that most toxins are present in the form of hydrolytic enzymes. Hydrolytic activity of the enzymes was measured and the data indicated that protease and phospholipase A activity was high which is responsible for local tissue damage. Furthermore, the role of hydrolytic enzymes in the induction of pathological events such as hemorrhage, edema, myotoxicity, and blood coagulation examination were assessed through animal models.

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Biochemical and biological characterization of a PLA2 from crotoxin complex of Crotalus durissus cumanensis

Cited by 48 publications

References 42 publications

Biochemical comparison of venoms from young Colombian Crotalus durissus cumanensis and their parents

Biochemical comparison of venoms from young Colombian Crotalus durissus cumanensis and their parents

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

Biochemical and pharmacological characterization of Trimersurus malabaricus snake venom

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