Characterization of monomeric and multimeric snake neurotoxins and other bioactive proteins from the venom of the lethal Australian common copperhead (Austrelaps superbus)

Marcon, Francesca; Purtell, Louise; Santos, Jerran; Hains, Peter G.; Escoubas, Pierre; Graudins, Andis; Nicholson, Graham M.

doi:10.1016/j.bcp.2013.02.034

Cited by 8 publications

(3 citation statements)

References 57 publications

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“…Venom phospholipases from various animals have been demonstrated to induce neurotoxicity, platelet activation, allergic reactions, haemolysis, and tissue damage. Unlike snake venom phospholipases which are lethal to their prey [ 69 , 101 ], ant venom phospholipases have not been implicated in causing lethality of prey, however, it is likely that they have synergistic activity with other toxic proteins which cause lethality [ 83 , 102 ].…”

Section: Ant Venom Proteinsmentioning

confidence: 99%

The Biochemical Toxin Arsenal from Ant Venoms

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Aili

Fox

et al. 2016

Toxins

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Ants (Formicidae) represent a taxonomically diverse group of hymenopterans with over 13,000 extant species, the majority of which inject or spray secretions from a venom gland. The evolutionary success of ants is mostly due to their unique eusociality that has permitted them to develop complex collaborative strategies, partly involving their venom secretions, to defend their nest against predators, microbial pathogens, ant competitors, and to hunt prey. Activities of ant venom include paralytic, cytolytic, haemolytic, allergenic, pro-inflammatory, insecticidal, antimicrobial, and pain-producing pharmacologic activities, while non-toxic functions include roles in chemical communication involving trail and sex pheromones, deterrents, and aggregators. While these diverse activities in ant venoms have until now been largely understudied due to the small venom yield from ants, modern analytical and venomic techniques are beginning to reveal the diversity of toxin structure and function. As such, ant venoms are distinct from other venomous animals, not only rich in linear, dimeric and disulfide-bonded peptides and bioactive proteins, but also other volatile and non-volatile compounds such as alkaloids and hydrocarbons. The present review details the unique structures and pharmacologies of known ant venom proteinaceous and alkaloidal toxins and their potential as a source of novel bioinsecticides and therapeutic agents.

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Section: Ant Venom Proteinsmentioning

confidence: 99%

The Biochemical Toxin Arsenal from Ant Venoms

Touchard

Aili

Fox

et al. 2016

Toxins

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“…Neurotoxic components usually induce an inhibition of indirect twitches, leading to a decrease in muscle contraction in a concentration-dependent manner. This assay was used in tandem with SEC to isolate hostoxin-1 from Hoplocephalus stephensi [64], rufoxin from Rhamphiophis oxyrhynchus [65], and SPAN from Austrelaps species [66]. Another method to test neurotoxicity is the evaluation of neurotoxic effects on the sciatic nerve.…”

Section: Bioassay-guided Fractionationmentioning

confidence: 99%

Separation and Analytical Techniques Used in Snake Venomics: A Review Article

et al. 2022

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The deleterious consequences of snake envenomation are due to the extreme protein complexity of snake venoms. Therefore, the identification of their components is crucial for understanding the clinical manifestations of envenomation pathophysiology and for the development of effective antivenoms. In addition, snake venoms are considered as libraries of bioactive molecules that can be used to develop innovative drugs. Numerous separation and analytical techniques are combined to study snake venom composition including chromatographic techniques such as size exclusion and RP-HPLC and electrophoretic techniques. Herein, we present in detail these existing techniques and their applications in snake venom research. In the first part, we discuss the different possible technical combinations that could be used to isolate and purify SV proteins using what is known as bioassay-guided fractionation. In the second part, we describe four different proteomic strategies that could be applied for venomics studies to evaluate whole venom composition, including the mostly used technique: RP-HPLC. Eventually, we show that to date, there is no standard technique used for the separation of all snake venoms. Thus, different combinations might be developed, taking into consideration the main objective of the study, the available resources, and the properties of the target molecules to be isolated.

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“…The best model was selected based on the analysis coming from these programs. The PROCHECK analysis of the best 3D structure model of PLB_Bm shows that 95.7% (468 amino acid residues) were in the favored region and 4.3% (21 amino acid residues) were in the allowed region with no amino acid residue in the outlier region of the Ramachandran plot Bernheimer et al, 1987;Aird et al, 2013Aird et al, , 2017Marcon et al, 2013;Sousa et al, 2013;Viala et al, 2014;Jiménez-Charris et al, 2015;Wiezel et al, 2015;Kovalchuk et al, 2016;Tang et al, 2016Tang et al, , 2019Zainal Abidin et al, 2016;Amorim et al, 2017;Patra et al, 2017;Tan et al, 2017;Vanuopadath et al, 2018;Jones et al, 2019;Méndez et al, 2019;Oliveira et al, 2019 Scorpion Egyptian scorpion Doery and Pearson, 1964;Mohamed et al, 1969 Insects Musca domestica L., Culex pipiens fatigans Khan and Hodgson, 1967;Rao and Subrahmanyam, 1969 Fungi Penicillium notatum Fairbairn, 1948;Saito, 2014 Bacteria Streptomyces sp. strain NA684, Doery and Pearson, 1964;Matsumoto et al, 2013 Mammals Bovine lysosomal phospholipase B-like protein Repo et al, 2014 Rice bran Contardi and Ercoli, 1933 PLBs, phospholipases B.…”

Section: Model Validationmentioning

confidence: 99%

The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B

Ullah

Masood

2020

Front. Mol. Biosci.

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Snake venom phospholipases B (SVPLBs) are the least studied enzymes. They constitute about 1% of Bothrops crude venoms, however, in other snake venoms, it is present in less than 1%. These enzymes are considered the most potent hemolytic agent in the venom. Currently, no structural information is available about these enzymes from snake venom. To better understand its three-dimensional structure and mechanisms of envenomation, the current work describes the first model-based structure report of this enzyme from Bothrops moojeni venom named as B. moojeni phospholipase B (PLB_Bm). The structure model of PLB_Bm was generated using model building software like I-TESSER, MODELLER 9v19, and Swiss-Model. The build PLB_Bm model was validated using validation tools (PROCHECK, ERRAT, and Verif3D). The analysis of the PLB_Bm modeled structure indicates that it contains 491 amino acid residues that form a well-defined four-layer αββα sandwich core and has a typical fold of the N-terminal nucleophile aminohydrolase (Ntn-hydrolase). The overall structure of PLB_Bm contains 18 β-strands and 17 α-helices with many connecting loops. The structure divides into two chains (A and B) after maturation. The A chain is smaller and contains 207 amino acid residues, whereas the B chain is larger and contains 266 amino acid residues. The sequence and structural comparison among homologous snake venom, bacterial, and mammals PLBs indicate that differences in the length and sequence composition may confer variable substrate specificity to these enzymes. Moreover, the surface charge distribution, average volume, and depth of the active site cavity also vary in these enzymes. The present work will provide more information about the structure-function relationship and mechanism of action of these enzymes in snakebite envenomation.

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Characterization of monomeric and multimeric snake neurotoxins and other bioactive proteins from the venom of the lethal Australian common copperhead (Austrelaps superbus)

Cited by 8 publications

References 57 publications

The Biochemical Toxin Arsenal from Ant Venoms

The Biochemical Toxin Arsenal from Ant Venoms

Separation and Analytical Techniques Used in Snake Venomics: A Review Article

The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B

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