Snake Venom, A Natural Library of New Potential Therapeutic Molecules: Challenges and Current Perspectives

Simões-Silva, Rodrigo; Alfonso, Jorge; Gomez, Ana; Holanda, Rudson J.; Sobrinho, Juliana C.; Zaqueo, Kayena Delaix; Moreira-Dill, Leandro S.; Kayano, Anderson M.; Grabner, Fernando P.; Silva, Saulo L. da; Almeida, José R.; Stábeli, Rodrigo G.; Zuliani, Juliana Pavan; Soares, Andreimar M.

doi:10.2174/1389201019666180620111025

Cited by 22 publications

(11 citation statements)

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“…Genomic and transcriptomic studies have proved to be an invaluable tool in the discovery of the snake venom evolution and proteoform [ 28 , 29 , 30 , 31 , 32 , 33 , 34 ]. Consequently, investigations are directed towards the discovery of pharmacologically active snake venom compounds [ 35 , 36 , 37 , 38 ]. For example, a recent study reported Mambaquaretin-1 (peptide from green mamba venom), as a promising candidate for the treatment of polycystic kidney disease [ 39 ].…”

Section: Introductionmentioning

confidence: 99%

Proteomic Investigations of Two Pakistani Naja Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles

Manuwar

Dreyer

Böhmert

et al. 2020

Toxins

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Latest advancement of omics technologies allows in-depth characterization of venom compositions. In the present work we present a proteomic study of two snake venoms of the genus Naja i.e., Naja naja (black cobra) and Naja oxiana (brown cobra) of Pakistani origin. The present study has shown that these snake venoms consist of a highly diversified proteome. Furthermore, the data also revealed variation among closely related species. High throughput mass spectrometric analysis of the venom proteome allowed to identify for the N. naja venom 34 protein families and for the N. oxiana 24 protein families. The comparative evaluation of the two venoms showed that N. naja consists of a more complex venom proteome than N. oxiana venom. Analysis also showed N-terminal acetylation (N-ace) of a few proteins in both venoms. To the best of our knowledge, this is the first study revealing this posttranslational modification in snake venom. N-ace can shed light on the mechanism of regulation of venom proteins inside the venom gland. Furthermore, our data showed the presence of other body proteins, e.g., ankyrin repeats, leucine repeats, zinc finger, cobra serum albumin, transferrin, insulin, deoxyribonuclease-2-alpha, and other regulatory proteins in these venoms. Interestingly, our data identified Ras-GTpase type of proteins, which indicate the presence of extracellular vesicles in the venom. The data can support the production of distinct and specific anti-venoms and also allow a better understanding of the envenomation and mechanism of distribution of toxins. Data are available via ProteomeXchange with identifier PXD018726.

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Section: Introductionmentioning

confidence: 99%

Proteomic Investigations of Two Pakistani Naja Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles

Manuwar

Dreyer

Böhmert

et al. 2020

Toxins

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“…In this sense, molecules of animal origin have stood out in the scientific literature for presenting microbicidal properties and within this group, snake venoms have been the target of numerous studies ( Harvey et al, 1998 ; Koh et al, 2006 ). Snake venoms are characterized by the complex constitution of molecules, mainly of a protein nature, which are related to a wide spectrum of pharmacological effects ( Lomonte et al, 2014 ; Simoes-Silva et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

Antimalarial activity of basic phospholipases A2 isolated from Paraguayan Bothrops diporus venom against Plasmodium falciparum

et al. 2020

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Malaria is a parasitic infectious disease and was responsible for 400.000 deaths in 2018. Plasmodium falciparum represents the species that causes most human deaths due to severe malaria. In addition, studies prove the resistance of P. falciparum to drugs used to treat malaria, making the search for new drugs with antiplasmodial potential necessary. In this context, the literature describes snake venoms as a rich source of molecules with microbicidal potential, including phospholipases A 2 (PLA 2 s). In this sense, the present study aimed to isolate basic PLA 2 s from Paraguayan Bothrops diporus venom and evaluate their antiplasmodial potential. Basic PLA 2 s were obtained using two chromatographic steps. Initially, B. diporus venom was subjected to ion exchange chromatography (IEC). The electrophoretic profile of the fractions from the IEC permitted the selection of 3 basic fractions, which were subjected to reverse phase chromatography, resulting in the isolation of the PLA 2 s. The toxins were tested for enzymatic activity using a chromogenic substrate and finally, the antiplasmodial, cytotoxic potential and hemolytic activity of the isolated toxins were evaluated. The electrophoretic profile of the fractions from the IEC permitted the selection of 3 basic fractions, which were subjected to reverse phase chromatography, resulting in the isolation of the two enzymatically active PLA 2 s, BdTX-I and BdTX-II and the PLA 2 homologue BdTX-III. The antiplasmodial potential was evaluated and the toxins showed IC 50 values of: 2.44, 0.0153 and 0.59 μg/mL respectively, presenting PLA 2 selectivity according to the selectivity index results (SI) calculated against HepG2 cells. The results show that the 3 basic phospholipases isolated in this study have a potent antiparasitic effect against the W2 strain of P. falciparum . In view of the results obtained in this work, further research are necessary to determine the mechanism of action by which these toxins cause cell death in parasites.

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“…To date, various bioactive proteins and peptides have been reported from the venom of different species of snakes, conus, scorpions, centipedes, lizards, spiders, sea anemones, bees and octopus [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 ]. In this context, venomous snakes are a focus of investigations, and a large number of pharmacologically useful molecules have already been isolated and characterized from snake venoms [ 10 , 11 ]. Among the approximately 3000 known snake species, only a relatively small number are venomous, mainly belonging to Viperidae and Elapidae families.…”

Section: Introductionmentioning

confidence: 99%

Snake Venom Peptides: Tools of Biodiscovery

Munawar

Ali

Akrem

et al. 2018

Toxins

108

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Nature endowed snakes with a lethal secretion known as venom, which has been fine-tuned over millions of years of evolution. Snakes utilize venom to subdue their prey and to survive in their natural habitat. Venom is known to be a very poisonous mixture, consisting of a variety of molecules, such as carbohydrates, nucleosides, amino acids, lipids, proteins and peptides. Proteins and peptides are the major constituents of the dry weight of snake venoms and are of main interest for scientific investigations as well as for various pharmacological applications. Snake venoms contain enzymatic and non-enzymatic proteins and peptides, which are grouped into different families based on their structure and function. Members of a single family display significant similarities in their primary, secondary and tertiary structures, but in many cases have distinct pharmacological functions and different bioactivities. The functional specificity of peptides belonging to the same family can be attributed to subtle variations in their amino acid sequences. Currently, complementary tools and techniques are utilized to isolate and characterize the peptides, and study their potential applications as molecular probes, and possible templates for drug discovery and design investigations.

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Snake Venom, A Natural Library of New Potential Therapeutic Molecules: Challenges and Current Perspectives

Cited by 22 publications

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Proteomic Investigations of Two Pakistani Naja Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles

Proteomic Investigations of Two Pakistani Naja Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles

Antimalarial activity of basic phospholipases A2 isolated from Paraguayan Bothrops diporus venom against Plasmodium falciparum

Snake Venom Peptides: Tools of Biodiscovery

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