scholarly journals Snake venomics of Bothrops punctatus, a semi-arboreal pitviper species from Antioquia, Colombia

2013 ◽  
Author(s):  
Maritza Fernández Culma ◽  
Jaime A Pereañez ◽  
Vitelbina Núñez Rangel ◽  
Bruno Lomonte
Keyword(s):  
Amino Acid ◽  
Protein Composition ◽  
Secretory Proteins ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Analytical Strategy ◽  
Phospholipases A2 ◽  
Snake Venomics

Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panamá, Colombia, and Ecuador, whose venom is poorly characterized. In the present work, the protein composition of this venom was profiled using the 'snake venomics' analytical strategy. Decomplexation of the crude venom by RP-HPLC and SDS-PAGE, followed by tandem mass spectrometry of tryptic digests, showed that it consists of proteins assigned to at least nine snake toxin families. Metalloproteinases are predominant in this secretion (41.5% of the total proteins), followed by C-type lectin/lectin-like proteins (16.7%), bradykinin-potentiating peptides (10.7%), phospholipases A2 (9.3%), serine proteinases (5.4%), disintegrins (3.8%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (1.7%), and cysteine-rich secretory proteins (1.2%). Altogether, 6.6% of the proteins were not identified. In vitro, the venom exhibited proteolytic, phospholipase A2, and L-amino acid oxidase activities, as well as angiotensin-converting enzyme (ACE)-inhibitory activity, in agreement with the obtained proteomic profile. Cytotoxic activity on murine C2C12 myoblasts was negative, suggesting that the majority of venom phospholipases A2 likely belong to the acidic type, which often lack major toxic effects. The protein composition of B. punctatus venom shows a good correlation with toxic activities here and previously reported, and adds further data in support of the wide diversity of strategies that have evolved in snake venoms to subdue prey, as increasingly being revealed by proteomic analyses.

scholarly journals Snake venomics of Bothrops punctatus, a semi-arboreal pitviper species from Antioquia, Colombia

2013 ◽  
Author(s):  
Maritza Fernández Culma ◽  
Jaime A Pereañez ◽  
Vitelbina Núñez Rangel ◽  
Bruno Lomonte
Keyword(s):  
Amino Acid ◽  
Protein Composition ◽  
Secretory Proteins ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Analytical Strategy ◽  
Phospholipases A2 ◽  
Snake Venomics

Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panamá, Colombia, and Ecuador, whose venom is poorly characterized. In the present work, the protein composition of this venom was profiled using the 'snake venomics' analytical strategy. Decomplexation of the crude venom by RP-HPLC and SDS-PAGE, followed by tandem mass spectrometry of tryptic digests, showed that it consists of proteins assigned to at least nine snake toxin families. Metalloproteinases are predominant in this secretion (41.5% of the total proteins), followed by C-type lectin/lectin-like proteins (16.7%), bradykinin-potentiating peptides (10.7%), phospholipases A2 (9.3%), serine proteinases (5.4%), disintegrins (3.8%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (1.7%), and cysteine-rich secretory proteins (1.2%). Altogether, 6.6% of the proteins were not identified. In vitro, the venom exhibited proteolytic, phospholipase A2, and L-amino acid oxidase activities, as well as angiotensin-converting enzyme (ACE)-inhibitory activity, in agreement with the obtained proteomic profile. Cytotoxic activity on murine C2C12 myoblasts was negative, suggesting that the majority of venom phospholipases A2 likely belong to the acidic type, which often lack major toxic effects. The protein composition of B. punctatus venom shows a good correlation with toxic activities here and previously reported, and adds further data in support of the wide diversity of strategies that have evolved in snake venoms to subdue prey, as increasingly being revealed by proteomic analyses.

Purification and Characterization of Lupus Anticoagulant Like Protein from Agkistrodon Halys Brevicaudus Venom

1996 ◽  
Vol 76 (06) ◽  
pp. 0993-0997
Author(s):  
Zhao-Yan Li ◽  
Xiao-Wei Wu ◽  
Tie-Fu Yu ◽  
Eric C-Y Lian
Keyword(s):  
Amino Acid ◽  
Lupus Anticoagulant ◽  
Inhibitory Effect ◽  
Clotting Factor ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Sds Page ◽  
The Individual ◽  
Reducing Condition

SummaryBy means of CM-Sephadex C-25, DEAE-Sephadex A-50, Sephadex G-200, and Sephadex G-75 chromatographies, a lupus anticoagulant like protein (LALP) from Agkistrodon halys brevicaudus was purified. On SDS-PAGE, the purified LALP had a molecular weight of 25,500 daltons under non-reducing condition and 15,000 daltons under reducing condition. The isoelectric point was pH 5.6. Its N terminal amino acid sequencing revealed a mixture of 2 sequences: DCP(P/S)(D/G)WSSYEGH(C/R)Q(Q/K). It was devoid of phospho-lipaseA, fibrino(geno)lytic, 5′-nucleotidase, L-amino acid oxidase, phosphomonoesterase, phosphodiesterase and thrombin-like activities, which were found in crude venom. In the presence of LALP, PT, aPTT, and dRVVT of human plasma were markedly prolonged and its effects were concentration-dependent but time-independent. The inhibitory effect of LALP on the plasma clotting time was enhanced by decreasing phospholipid concentration in TTI test. The individual clotting factor activity was not affected by LALP when higher dilutions of LALP-plasma mixture were used for assay. Russell’s viper venom time was shortened when high phospholipid confirmatory reagent was used. Therefore, the protein has lupus anticoagulant property.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

scholarly journals The anti-ovarian carcinoma activity of L-amino Acid Oxidase from Crotalus adamanteus venom in vivo and in vitro

2021 ◽  
Author(s):  
Li Bo ◽  
Yan Xiong ◽  
Qiyi He ◽  
Xiaodong Yu ◽  
Bo Li ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Amino Acid ◽  
Cancer Cells ◽  
Morphological Changes ◽  
Complex Mixture ◽  
Ovarian Cancer Cells ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Apoptosis Pathway

Abstract The anti-tumor potential of animal toxins has fully attracted the attention of researchers. Snake venoms is a complex mixture of different components and has revealed high toxicity on normal and tumoral tissues or cells. The snake venom L-Amino-acid oxidase (svLAAO) has grown up to be a critical research target in molecular biology sciences and medicine sciences since widespread presence and various biological roles, including antitumor application. We found that Crotalus adamanteus (C. adamanteus) venom LAAO significantly decreased the viability of ovarian cancer cells and caused morphological changes preceded cell death. Cell experiments confirmed that C. adamanteus venom LAAO caused alterations of intrinsic or extrinsic apoptosis pathway-related genes in ovarian cancer cells. Animal experiments and histological analysis also proved that C. adamanteus venom LAAO could effectively inhibit the damage of ovarian cancer to tissues. The major apoptosis induction of C. adamanteus venom LAAO on ovarian cancer cells can be blocked by catalase, suggesting that the cytotoxicity of C. adamanteus venom LAAO on ovarian cancer cells was mainly mediated by H2O2. Our preliminary results revealed that C. adamanteus venom LAAO may induce apoptosis of ovarian cancer cells through the death receptor pathway and mitochondrial pathway. It is inferred that C. adamanteus venom LAAO will be some advantages in New Drug Research and Development of antitumor drugs in the future. Nevertheless, extra studies on the pharmacological actions and molecular mechanism of svLAAO in anti-cancer are necessary in order to better promote its application.

In vitro cytotoxicity of L-amino acid oxidase from the venom of Crotalus mitchellii pyrrhus

Toxicon ◽  
2017 ◽  
Vol 139 ◽  
pp. 20-30 ◽  
Author(s):  
Kok Keong Tan ◽  
Siok Ghee Ler ◽  
Jayantha Gunaratne ◽  
Boon Huat Bay ◽  
Gopalakrishnakone Ponnampalam
Keyword(s):  
Amino Acid ◽  
In Vitro Cytotoxicity ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Crotalus Mitchellii

scholarly journals Vipera berus berus Venom from Russia: Venomics, Bioactivities and Preclinical Assessment of Microgen Antivenom

Toxins ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 90 ◽  
Author(s):  
Ruslan I. Al-Shekhadat ◽  
Ksenia S. Lopushanskaya ◽  
Álvaro Segura ◽  
José María Gutiérrez ◽  
Juan J. Calvete ◽  
...  
Keyword(s):  
Binding Capacity ◽  
Secretory Protein ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Vipera Berus ◽  
Phospholipases A2 ◽  
Toxin Binding ◽  
Main Effects

The common European adder, Vipera berus berus, is a medically relevant species, which is widely distributed in Russia and thus, is responsible for most snakebite accidents in Russia. We have investigated the toxic and enzymatic activities and have determined the proteomic composition of its venom. Phospholipases A2 (PLA2, 25.3% of the venom proteome), serine proteinases (SVSP, 16.2%), metalloproteinases (SVMP, 17.2%), vasoactive peptides (bradykinin-potentiating peptides (BPPs), 9.5% and C-type natriuretic peptides (C-NAP, 7.8%), cysteine-rich secretory protein (CRISP, 8%) and L-amino acid oxidase (LAO, 7.3%) represent the major toxin classes found in V. b. berus (Russia) venom. This study was also designed to assess the in vivo and in vitro preclinical efficacy of the Russian Microgen antivenom in neutralizing the main effects of V. b. berus venom. The results show that this antivenom is capable of neutralizing the lethal, hemorrhagic and PLA2 activities. Third-generation antivenomics was applied to quantify the toxin-recognition landscape and the maximal binding capacity of the antivenom for each component of the venom. The antivenomics analysis revealed that 6.24% of the anti-V. b. berus F(ab’)2 molecules fraction are toxin-binding antibodies, 60% of which represent clinically relevant antivenom molecules.

scholarly journals Evaluation of human D-amino acid oxidase inhibition by anti-psychotic drugs in vitro

2014 ◽  
Vol 8 (3) ◽  
pp. 149-154 ◽  
Author(s):  
Miho Shishikura ◽  
Hitomi Hakariya ◽  
Sumiko Iwasa ◽  
Takashi Yoshio ◽  
Hideaki Ichiba ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Anti Psychotic ◽  
Amino Acid Oxidase ◽  
Oxidase Inhibition

scholarly journals Antagonism of Trichoderma harzianum ETS 323 on Botrytis cinerea Mycelium in Culture Conditions

2012 ◽  
Vol 102 (11) ◽  
pp. 1054-1063 ◽  
Author(s):  
Chi-Hua Cheng ◽  
Chia-Ann Yang ◽  
Kou-Cheng Peng
Keyword(s):  
Amino Acid ◽  
Botrytis Cinerea ◽  
Trichoderma Harzianum ◽  
Hyphal Growth ◽  
Extracellular Proteins ◽  
In Vitro Assays ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Trichoderma Spp

Previous studies have shown that the extracellular proteins of Trichoderma harzianum ETS 323 grown in the presence of deactivated Botrytis cinerea in culture include a putative l-amino acid oxidase and have suggested the involvement of this enzyme in the antagonistic mechanism. Here, we hypothesized that the mycoparasitic process of Trichoderma spp. against B. cinerea involves two steps; that is, an initial hyphal coiling stage and a subsequent hyphal coiling stage, with different coiling rates. The two-step antagonism of T. harzianum ETS 323 against B. cinerea during the mycoparasitic process in culture was evaluated using a biexponential equation. In addition, an l-amino acid oxidase (Th-l-AAO) was identified from T. harzianum ETS 323. The secretion of Th-l-AAO was increased when T. harzianum ETS 323 was grown with deactivated hyphae of B. cinerea. Moreover, in vitro assays indicated that Th-l-AAO effectively inhibited B. cinerea hyphal growth, caused cytosolic vacuolization in the hyphae, and led to hyphal lysis. Th-l-AAO also showed disease control against the development of B. cinerea on postharvest apple fruit and tobacco leaves. Furthermore, an apoptosis-like response, including the generation of reactive oxygen species, was observed in B. cinerea after treatment with Th-l-AAO, suggesting that Th-l-AAO triggers programmed cell death in B. cinerea. This may be associated with the two-step antagonism of T. harzianum ETS 323 against B. cinerea.

scholarly journals Shedding Lights on Crude Venom from Solitary Foraging Predatory Ant Ectatomma opaciventre: Initial Toxinological Investigation

Toxins ◽  
2022 ◽  
Vol 14 (1) ◽  
pp. 37
Author(s):  
Lucas Ian Veloso Correia ◽  
Fernanda Van Petten de Vasconcelos Azevedo ◽  
Fernanda Gobbi Amorim ◽  
Sarah Natalie Cirilo Gimenes ◽  
Lorena Polloni ◽  
...  
Keyword(s):  
Biological Activities ◽  
Biological Effects ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Cytotoxic Effects ◽  
Primary Hemostasis ◽  
High Enzymatic Activity ◽  
Predatory Ants

Some species of primitive predatory ants, despite living in a colony, exercise their hunting collection strategy individually; their venom is painful, paralyzing, digestive, and lethal for their prey, yet the toxins responsible for these effects are poorly known. Ectatomma opaciventre is a previously unrecorded solitary hunting ant from the Brazilian Cerrado. To overcome this hindrance, the present study performed the in vitro enzymatic, biochemical, and biological activities of E. opaciventre to better understand the properties of this venom. Its venom showed several proteins with masses ranging from 1–116 kDa, highlighting the complexity of this venom. Compounds with high enzymatic activity were described, elucidating different enzyme classes present in the venom, with the presence of the first L-amino acid oxidase in Hymenoptera venoms being reported. Its crude venom contributes to a state of blood incoagulability, acting on primary hemostasis, inhibiting collagen-induced platelet aggregation, and operating on the fibrinolysis of loose red clots. Furthermore, the E. opaciventre venom preferentially induced cytotoxic effects on lung cancer cell lines and three different species of Leishmania. These data shed a comprehensive portrait of enzymatic components, biochemical and biological effects in vitro, opening perspectives for bio-pharmacological application of E. opaciventre venom molecules.

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