Snake Venom Components Affecting the Coagulation System

Alvarez-Flores, Miryam Paola; Faria, Fernanda; Andrade, Sofia; Chudzinski-Tavassi, Ana Marisa

doi:10.1007/978-94-007-6648-8_31-1

Cited by 7 publications

(10 citation statements)

References 53 publications

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“…48 Furthermore, Zhang and Du 2021, 49 disclosed that the most lethal enzyme in BV formation of the melittin-PLA2 complex is referred to as the bee hemolytic factor which cleaves cellular membrane phospholipids and cellular lysis. Moreover, Alvarez-Flores et al, 2016, 50 indicated that the PLA2 had a hematological effect including coagulation abnormalities. Moreover, Abdulsalam et al, 2016, 46 reported that PLA2 from BV inhibited platelet aggregation through the formation of lysophosphatidylcholine.…”

Section: Discussionmentioning

confidence: 99%

The role of bee venom on immunological and hematological parameters in albino rats

Abo-Zaid

Yatimi

Ismail

2023

EJI

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Bee venom (BV) showed therapeutical effects to treat various diseases as it contains at least 18 pharmacologically active components including various enzymes, peptides, and amines. This study aimed to evaluate the action of BV on some hematological parameters, humoral and cellular immunity, and the determination of antioxidant levels in male albino rats. The study included 40 male albino rats (190–210 g), divided into four groups. Three groups were injected subcutaneously with three different doses of BV (2.5, 5, and 10 mg/kg, respectively). The control group was injected with saline solution. Blood samples were obtained to measure total leucocytes count (TLC), differential leukocytes count, hematological parameters (hemoglobin (Hb), hematocrit (HCT), red blood cells (RBCs), mean cell volume (MCV), mean cell hemoglobin (MCH), mean cell hemoglobin concentration (MCHC) and Platelets. Sera were used to assess immunoglobulins (IgM, IgG, IgA, and IgE), some cytokines e.g., tumor necrosis factor-alpha (TNF-α), tumor growth factor beta (TGF-β), interleukins 6 and 10 (IL-6, IL-10), and some antioxidant levels malondialdehyde (MDA), super oxide dismutase (SOD), and glutathione (GSH). Data showed that BV therapy increased antibody production levels (IgM, IgG, and IgA) while decreasing IgE levels. Hematological markers (Hb and lymphocytes) were increased. BV increased total TGF- β and IL-10 but decreased total TNF- α and IL-6. On the antioxidant scale, an increase in SOD, CAT, and GSH levels was observed, accompanied by a decrease in MDA levels. However, the BV treatment led to a significant reduction in the number of eosinophils, monocytes, and neutrophils (p < 0.05). In conclusion, our findings suggested that BV may be utilized to increase the effectiveness of various immunological and hematological parameters.

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Section: Discussionmentioning

confidence: 99%

The role of bee venom on immunological and hematological parameters in albino rats

Abo-Zaid

Yatimi

Ismail

2023

EJI

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“…To interpret the result, it is important to consider that proteins as SVSP, SVMP, CTL, PLA 2 and other toxins play roles in the coagulation process. Some are procoagulant and others are anticoagulant [61]. Thus, synergistic effect [14,62] and a balance of actions produce the final venom activity.…”

Section: Discussionmentioning

confidence: 99%

Comparative gender peptidomics of Bothrops atrox venoms: are there differences between them?

Simizo

Kitano

Sant’Anna

et al. 2020

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

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Background: Bothrops atrox is known to be the pit viper responsible for most snakebites and human fatalities in the Amazon region. It can be found in a wide geographical area including northern South America, the east of Andes and the Amazon basin. Possibly, due to its wide distribution and generalist feeding, intraspecific venom variation was reported by previous proteomics studies. Sex-based and ontogenetic variations on venom compositions of Bothrops snakes were also subject of proteomic and peptidomic analysis. However, the venom peptidome of B. atrox remains unknown. Methods: We conducted a mass spectrometry-based analysis of the venom peptides of individual male and female specimens combining bottom-up and top-down approaches. Results: We identified in B. atrox a total of 105 native peptides in the mass range of 0.4 to 13.9 kDa. Quantitative analysis showed that phospholipase A 2 and bradykinin potentiating peptides were the most abundant peptide families in both genders, whereas disintegrin levels were significantly increased in the venoms of females. Known peptides processed at non-canonical sites and new peptides as the Ba1a, which contains the SVMP BATXSVMPII1 catalytic site, were also revealed in this work. Conclusion: The venom peptidomes of male and female specimens of B. atrox were analyzed by mass spectrometry-based approaches in this work. The study points to differences in disintegrin levels in the venoms of females that may result in distinct pathophysiology of envenomation. Further research is required to explore the potential biological implications of this finding.

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“…Due to its high specificity, RVV-X is a remarkable biotechnological tool widely used in coagulation research and medical diagnostics. ,, For example, the Stypven time is determined by a clotting assay that measures the FX to FXa conversion by RVV-X and subsequent prothrombin activation that initiates clot formation. − In particular, a long Stypven time is a diagnostic of FX deficiency, also called Stuart–Prower factor deficiency …”

Section: Introductionmentioning

confidence: 99%

Unraveling the Reaction Mechanism of Russell’s Viper Venom Factor X Activator: A Paradigm for the Reactivity of Zinc Metalloproteinases?

Castro-Amorim

Oliveira

Mukherjee

et al. 2023

J. Chem. Inf. Model.

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Snake venom metalloproteinases (SVMPs) are important drug targets against snakebite envenoming, the neglected tropical disease with the highest mortality worldwide. Here, we focus on Russell’s viper (Daboia russelii), one of the “big four” snakes of the Indian subcontinent that, together, are responsible for ca. 50,000 fatalities annually. The “Russell’s viper venom factor X activator” (RVV-X), a highly toxic metalloproteinase, activates the blood coagulation factor X (FX), leading to the prey’s abnormal blood clotting and death. Given its tremendous public health impact, the WHO recognized an urgent need to develop efficient, heat-stable, and affordable-for-all small-molecule inhibitors, for which a deep understanding of the mechanisms of action of snake’s principal toxins is fundamental. In this study, we determine the catalytic mechanism of RVV-X by using a density functional theory/molecular mechanics (DFT:MM) methodology to calculate its free energy profile. The results showed that the catalytic process takes place via two steps. The first step involves a nucleophilic attack by an in situ generated hydroxide ion on the substrate carbonyl, yielding an activation barrier of 17.7 kcal·mol–1, while the second step corresponds to protonation of the peptide nitrogen and peptide bond cleavage with an energy barrier of 23.1 kcal·mol–1. Our study shows a unique role played by Zn2+ in catalysis by lowering the pK a of the Zn2+-bound water molecule, enough to permit the swift formation of the hydroxide nucleophile through barrierless deprotonation by the formally much less basic Glu140. Without the Zn2+ cofactor, this step would be rate-limiting.

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Snake Venom Components Affecting the Coagulation System

Cited by 7 publications

References 53 publications

The role of bee venom on immunological and hematological parameters in albino rats

The role of bee venom on immunological and hematological parameters in albino rats

Comparative gender peptidomics of Bothrops atrox venoms: are there differences between them?

Unraveling the Reaction Mechanism of Russell’s Viper Venom Factor X Activator: A Paradigm for the Reactivity of Zinc Metalloproteinases?

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