Erythrocyte haemotoxicity profiling of snake venom toxins after nanofractionation

Xie, Cuicui; Bittenbinder, Mátyás A.; Slagboom, Julien; Arrahman, Arif; Bruijns, Sven C. M.; Somsen, Govert W.; Vonk, Freek J.; Casewell, Nicholas R.; García-Vallejo, Juan J.; Kool, Jeroen

doi:10.1016/j.jchromb.2021.122586

Cited by 10 publications

(2 citation statements)

References 42 publications

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“…The direct hemolytic activity is largely associated with the cytotoxins/cardiotoxins of the 3FTx toxins family of snake venoms. The cytotoxins/cardiotoxins directly perturb and destabilize the structural integrity of the plasma membrane resulting in lysis [ 42 , 43 , 44 ]. The lack of direct hemolytic activity is likely due to the absence of direct lytic factors/cytotoxins/cardiotoxins in this venom.…”

Section: Resultsmentioning

confidence: 99%

Hump-Nosed Pit Viper (Hypnale hypnale) Venom-Induced Irreversible Red Blood Cell Aggregation, Inhibition by Monovalent Anti-Venom and N-Acetylcysteine

Sandesha,

Naveen,

Manikanta

et al. 2024

Cells

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Envenomation by the Hypnale hypnale in the Western Ghats of India (particularly in the Malabar region of Kerala) and the subcontinent island nation of Sri Lanka is known to inflict devastating mortality and morbidity. Currently, H. hypnale bites in India are devoid of anti-venom regimens. A detailed characterization of the venom is essential to stress the need for therapeutic anti-venom. Notably, the deleterious effects of this venom on human blood cells have largely remained less explored. Therefore, in continuation of our previous study, in the present study, we envisioned investigating the effect of venom on the morphological and physiological properties of red blood cells (RBCs). The venom readily induced deleterious morphological changes and, finally, the aggregation of washed RBCs. The aggregation process was independent of the ROS and the intracellular Ca2+ ion concentration. Confocal and scanning electron microscopy (SEM) images revealed the loss of biconcave morphology and massive cytoskeletal disarray. Crenation or serrated plasma membrane projections were evenly distributed on the surface of the RBCs. The venom did not cause the formation of methemoglobin in washed RBCs but was significantly induced in whole blood. Venom did not affect glucose uptake and Na+/K+ -ATPase activity but inhibited glucose 6 phosphate dehydrogenase activity and decreased the fluidity of the plasma membrane. Venom-induced RBC aggregates exhibited pro-coagulant activity but without affecting platelet aggregation. In pre-incubation or co-treatment studies, none of the bioactive compounds, such as melatonin, curcumin, fisetin, berberine, and quercetin, sugars such as mannose and galactose, and therapeutic polyvalent anti-venoms (Bharat and VINS) were inhibited, whereas only N-acetylcysteine and H. hypnale monovalent anti-venom could inhibit venom-induced deleterious morphological changes and aggregation of RBCs. In post-treatment studies, paradoxically, none of the bioactives and anti-venoms, including N-acetylcysteine and H. hypnale monovalent anti-venom, reversed the venom-induced RBC aggregates.

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Section: Resultsmentioning

confidence: 99%

Hump-Nosed Pit Viper (Hypnale hypnale) Venom-Induced Irreversible Red Blood Cell Aggregation, Inhibition by Monovalent Anti-Venom and N-Acetylcysteine

Sandesha,

Naveen,

Manikanta

et al. 2024

Cells

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“…PLA2s are ubiquitous in many venomous snakes such as elapid, rattlesnake and pit viper. PLA2s isolated from elapid venom could hydrolyze phospholipids, whereas those isolated from viper venoms could not unless exogenous phospholipids were added [ 81 , 82 , 83 ]. In addition, PLA2s from elapid and viper were reported to exert hemolytic activities, while PLA2s from centipede exhibited no directly cytotoxic effects [ 22 , 82 ].…”

Section: Centipede Toxins Acting On Other Systemsmentioning

confidence: 99%

Bioactive Peptides and Proteins from Centipede Venoms

et al. 2022

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Venoms are a complex cocktail of biologically active molecules, including peptides, proteins, polyamide, and enzymes widely produced by venomous organisms. Through long-term evolution, venomous animals have evolved highly specific and diversified peptides and proteins targeting key physiological elements, including the nervous, blood, and muscular systems. Centipedes are typical venomous arthropods that rely on their toxins primarily for predation and defense. Although centipede bites are frequently reported, the composition and effect of centipede venoms are far from known. With the development of molecular biology and structural biology, the research on centipede venoms, especially peptides and proteins, has been deepened. Therefore, we summarize partial progress on the exploration of the bioactive peptides and proteins in centipede venoms and their potential value in pharmacological research and new drug development.

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