Snake venom toxins: toxicity and medicinal applications

Chan, Yau Sang; Cheung, Randy Chi Fai; Xia, Lixin; Wong, Jack Ho; Ng, Tzi Bun; Chan, Wai Yee

doi:10.1007/s00253-016-7610-9

Cited by 108 publications

(72 citation statements)

References 119 publications

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“…Venoms have evolved over millions of years to facilitate prey capture and/or defense from predators and rivals. Snake venoms, in particular, likely originated in the Cenozoic Era (Fry, 2005;Fry et al, 2006), and they are amongst the most well-characterized of animal venoms, comprising a complex mixture of toxic, and pharmacologically-active proteins and peptides Chan et al, 2016). Tragically, snake envenomation is a significant health and economic burden worldwide.…”

Section: Introductionmentioning

confidence: 99%

Multifunctional Toxins in Snake Venoms and Therapeutic Implications: From Pain to Hemorrhage and Necrosis

et al. 2019

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Animal venoms have evolved over millions of years for prey capture and defense from predators and rivals. Snake venoms, in particular, have evolved a wide diversity of peptides and proteins that induce harmful inflammatory and neurotoxic effects including severe pain and paralysis, hemotoxic effects, such as hemorrhage and coagulopathy, and cytotoxic/myotoxic effects, such as inflammation and necrosis. If untreated, many envenomings result in death or severe morbidity in humans and, despite advances in management, snakebite remains a major public health problem, particularly in developing countries. Consequently, the World Health Organization recently recognized snakebite as a neglected tropical disease that affects ∼2.7 million p.a. The major protein classes found in snake venoms are phospholipases, metalloproteases, serine proteases, and three-finger peptides. The mechanisms of action and pharmacological properties of many snake venom toxins have been elucidated, revealing a complex multifunctional cocktail that can act synergistically to rapidly immobilize prey and deter predators. However, despite these advances many snake toxins remain to be structurally and pharmacologically characterized. In this review, the multifunctional features of the peptides and proteins found in snake venoms, as well as their evolutionary histories, are discussed with the view to identifying novel modes of action and improving snakebite treatments.

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Section: Introductionmentioning

confidence: 99%

Multifunctional Toxins in Snake Venoms and Therapeutic Implications: From Pain to Hemorrhage and Necrosis

et al. 2019

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“…Bothropic venoms are biochemically complex, with varying protein components, including serine proteases [1], metalloproteinases [2], L-amino acid oxidases [3], C-type lectins [4], myotoxins [5], disintegrins [6], and group II PLA 2 s [7], which have proven to be invaluable research tools and have provided leads for development of new therapies [8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

BmajPLA 2 -II, a basic Lys49-phospholipase A 2 homologue from Bothrops marajoensis snake venom with parasiticidal potential

Grabner

Alfonso

Kayano

et al. 2017

International Journal of Biological Macromolecules

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Snake venoms contain various proteins, especially phospholipases A (PLAs), which present potential applications in diverse areas of health and medicine. In this study, a new basic PLA from Bothrops marajoensis with parasiticidal activity was purified and characterized biochemically and biologically. B. marajoensis venom was fractionated through cation exchange followed by reverse phase chromatographies. The isolated toxin, BmajPLA-II, was structurally characterized with MALDI-TOF (Matrix-assisted laser desorption/ionization-time of flight) mass spectrometry, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), followed by two-dimensional electrophoresis, partial amino acid sequencing, an enzymatic activity assay, circular dichroism, and dynamic light scattering assays. These structural characterization tests presented BmajPLA-II as a basic Lys49 PLA homologue, compatible with other basic snake venom PLAs (svPLA), with a tendency to form aggregations. The in vitro anti-parasitic potential of B. marajoensis venom and of BmajPLA-II was evaluated against Leishmania infantum promastigotes and Trypanosoma cruzi epimastigotes, showing significant activity at a concentration of 100μg/mL. The venom and BmajPLA-II presented IC of 0.14±0.08 and 6.41±0.64μg/mL, respectively, against intraerythrocytic forms of Plasmodium falciparum with CC cytotoxicity values against HepG2 cells of 43.64±7.94 and >150μg/mL, respectively. The biotechnological potential of these substances in relation to leishmaniasis, Chagas disease and malaria should be more deeply investigated.

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“…Current situation has prompted the search for new antimicrobial compounds with alternative mechanisms of action that could be used solely or combined with traditional drugs to tackle bacterial, fungal, parasites and virus drugs resistance. Antimicrobial activity is a common feature of animal venoms and is related to a wide range of peptidic toxins such as mastoparans [32], cardiotoxins [133], cecropins [134], mellitin [135] and some enzymes [136]. Unlike conventional antibiotics, which interact with specific bacterial targets, some venom AMPs act by direct disruption of cell surface [136][137][138].…”

Section: Antimicrobial and Antifungal Activitymentioning

confidence: 99%

Wasp venomic: Unravelling the toxins arsenal of Polybia paulista venom and its potential pharmaceutical applications

Pérez-Riverol

Santos-Pinto

Lasa

et al. 2017

Journal of Proteomics

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Polybia paulista (Hymenoptera: Vespidae) is a neotropical social wasp from southeast Brazil. As most social Hymenoptera, venom from P. paulista comprises a complex mixture of bioactive toxins ranging from low molecular weight compounds to peptides and proteins. Several efforts have been made to elucidate the molecular composition of the P. paulista venom. Data derived from proteomic, peptidomic and allergomic analyses has enhanced our understanding of the whole envenoming process caused by the insect sting. The combined use of bioinformatics, -omics- and molecular biology tools have allowed the identification, characterization, in vitro synthesis and recombinant expression of several wasp venom toxins. Some of these P. paulista - derived bioactive compounds have been evaluated for the rational design of antivenoms and the improvement of allergy specific diagnosis and immunotherapy. Molecular characterization of crude venom extract has enabled the description and isolation of novel toxins with potential biotechnological applications. Here, we review the different approaches that have been used to unravel the venom composition of P. paulista. We also describe the main groups of P. paulista - venom toxins currently identified and analyze their potential in the development of component-resolved diagnosis of allergy, and in the rational design of antivenoms and novel bioactive drugs.

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Snake venom toxins: toxicity and medicinal applications

Cited by 108 publications

References 119 publications

Multifunctional Toxins in Snake Venoms and Therapeutic Implications: From Pain to Hemorrhage and Necrosis

Multifunctional Toxins in Snake Venoms and Therapeutic Implications: From Pain to Hemorrhage and Necrosis

BmajPLA 2 -II, a basic Lys49-phospholipase A 2 homologue from Bothrops marajoensis snake venom with parasiticidal potential

Wasp venomic: Unravelling the toxins arsenal of Polybia paulista venom and its potential pharmaceutical applications

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