State-of-the-art review of snake venom phosphodiesterases (svPDEs)

Oliveira, Isadora Sousa de; Pucca, Manuela Berto; Ferreira, Isabela Gobbo; Cerni, Felipe Augusto; Jacob, Beatriz de Cássia da Silva; Wiezel, Gisele Adriano; Pinheiro-Júnior, Ernesto Lopes; Cordeiro, Francielle Almeida; Bordon, Karla de Castro Figueiredo; Arantes, Eliane Candiani

doi:10.1016/j.toxicon.2022.08.004

Cited by 3 publications

(5 citation statements)

References 83 publications

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“…This protein family is present in just over one third of species and had a mean abundance of 0.7% and a maximum of 3.6%. They are mono or multimeric with a molecular mass of 90 to 160 kDa (Oliveira et al 2022b). They may facilitate venom diffusion through the prey's tissues (Oliveira et al 2022b) and PDEs isolated from rattlesnake venoms (Crotalus spp.)…”

Section: Phosphodiesterase (Pde)mentioning

confidence: 99%

“…They are mono or multimeric with a molecular mass of 90 to 160 kDa (Oliveira et al 2022b). They may facilitate venom diffusion through the prey's tissues (Oliveira et al 2022b) and PDEs isolated from rattlesnake venoms (Crotalus spp.) were found to produce an immediate profound hypotensive crisis but did not interfere with neurotransmission (Russell et al 1963).…”

Section: Phosphodiesterase (Pde)mentioning

confidence: 99%

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A current perspective on snake venom composition and constituent protein families

Tasoulis

2022

Arch Toxicol

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Snake venoms are heterogeneous mixtures of proteins and peptides used for prey subjugation. With modern proteomics there has been a rapid expansion in our knowledge of snake venom composition, resulting in the venom proteomes of 30% of vipers and 17% of elapids being characterised. From the reasonably complete proteomic coverage of front-fanged snake venom composition (179 species-68 species of elapids and 111 species of vipers), the venoms of vipers and elapids contained 42 different protein families, although 18 were only reported in < 5% of snake species. Based on the mean abundance and occurrence of the 42 protein families, they can be classified into 4 dominant, 6 secondary, 14 minor, and 18 rare protein families. The dominant, secondary and minor categories account for 96% on average of a snake's venom composition. The four dominant protein families are: phospholipase A 2 (PLA 2 ), snake venom metalloprotease (SVMP), three-finger toxins (3FTx), and snake venom serine protease (SVSP). The six secondary protein families are: L-amino acid oxidase (LAAO), cysteine-rich secretory protein (CRiSP), C-type lectins (CTL), disintegrins (DIS), kunitz peptides (KUN), and natriuretic peptides (NP). Venom variation occurs at all taxonomic levels, including within populations. The reasons for venom variation are complex, as variation is not always associated with geographical variation in diet. The four dominant protein families appear to be the most important toxin families in human envenomation, being responsible for coagulopathy, neurotoxicity, myotoxicity and cytotoxicity. Proteomic techniques can be used to investigate the toxicological profile of a snake venom and hence identify key protein families for antivenom immunorecognition.

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Section: Phosphodiesterase (Pde)mentioning

confidence: 99%

Section: Phosphodiesterase (Pde)mentioning

confidence: 99%

A current perspective on snake venom composition and constituent protein families

Tasoulis

2022

Arch Toxicol

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“…Others substrates were tested in PDEs studies to characterize their enzymatic activity, such as bis ( p -nitrophenyl) phosphate (0.4 mM [ 20 ], 1 mM [ 17 ] and 5 mM [ 21 ]), adenosine triphosphate (ATP, 0.05 mM), nicotinamide adenine dinucleotide (NAD, 0.05 mM), adenosine diphosphate (ADP, 0.05 mM), nicotinamide guanine dinucleotide (NGD, 0.05 mM), and adenosine monophosphate (AMP, 0.05 mM) [ 22 ], among others [ 18 , 19 ]. Although our study did not aim to characterize the enzymatic kinetics of Cdc PDE, using λDNA as substrate, we observed that the amount of substrate used in the cited studies is much higher than in our study (6 × 10 −13 mM), and even though the hydrolysis was observed.…”

Section: Resultsmentioning

confidence: 99%

“…Moreover, functional previous studies demonstrated that the Cdc PDE was able to inhibit ADP-induced platelet aggregation and to cause a cytotoxic effect to human keratinocytes [ 17 ]. Knowing that Cdc PDE is classified as a nuclease, able to degrade DNA (i.e., DNAse [ 18 , 19 ], this study aimed to verify if the rattlesnake-derived molecule could degrade cell-free DNA from NETs ( Figure 1 ).…”

Section: Introductionmentioning

confidence: 99%

A Promising Biomolecule Able to Degrade Neutrophil Extracellular Traps: CdcPDE, a Rattlesnake Phosphodiesterase

Oliveira

Costa

Veras

et al. 2023

Toxins

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Neutrophil extracellular traps (NETs) are an important mechanism for defense against pathogens. Their overproduction can be harmful since excessive NET formation promotes inflammation and tissue damage in several diseases. Nucleases are capable to degrade NET on basis of their DNA hydrolysis activity, including the CdcPDE, a nuclease isolated from Crotalus durissus collilineatus snake venom. Here, we report a new finding about CdcPDE activity, demonstrating its efficiency in degrading cell-free DNA from NETs, being a potential candidate to assist in therapies targeting inflammatory diseases.

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“…Phosphodiesterases are enzymes that hydrolyze cyclic nucleotides and play a role in regulating intracellular levels of cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP) and, therefore, cell function [ 86 , 87 ]. Its presence in the venom was detected by proteome [ 8 ].…”

Section: High Molecular Weight Compounds and How They Could Interfere...mentioning

confidence: 99%

Understanding the complexity of Tityus serrulatus venom: A focus on high molecular weight components

Oliveira,

Alano-da-Silva,

Ferreira

et al. 2024

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

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Tityus serrulatus scorpion is responsible for a significant number of envenomings in Brazil, ranging from mild to severe, and in some cases, leading to fatalities. While supportive care is the primary treatment modality, moderate and severe cases require antivenom administration despite potential limitations and adverse effects. The remarkable proliferation of T. serrulatus scorpions, attributed to their biology and asexual reproduction, contributes to a high incidence of envenomation. T. serrulatus scorpion venom predominantly consists of short proteins acting as neurotoxins (α and β), that primarily target ion channels. Nevertheless, high molecular weight compounds, including metalloproteases, serine proteases, phospholipases, and hyaluronidases, are also present in the venom. These compounds play a crucial role in envenomation, influencing the severity of symptoms and the spread of venom. This review endeavors to comprehensively understand the T. serrulatus scorpion venom by elucidating the primary high molecular weight compounds and exploring their potential contributions to envenomation. Understanding these compounds' mechanisms of action can aid in developing more effective treatments and prevention strategies, ultimately mitigating the impact of scorpion envenomation on public health in Brazil.

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State-of-the-art review of snake venom phosphodiesterases (svPDEs)

Cited by 3 publications

References 83 publications

A current perspective on snake venom composition and constituent protein families

A current perspective on snake venom composition and constituent protein families

A Promising Biomolecule Able to Degrade Neutrophil Extracellular Traps: CdcPDE, a Rattlesnake Phosphodiesterase

Understanding the complexity of Tityus serrulatus venom: A focus on high molecular weight components

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