Platypus venom: source of novel compounds

2009 ◽  
Vol 57 (4) ◽  
pp. 203 ◽  
Author(s):  
Jennifer M. S. Koh ◽  
Paramjit S. Bansal ◽  
Allan M. Torres ◽  
Philip W. Kuchel
Keyword(s):  
Nerve Growth Factor ◽  
Natriuretic Peptides ◽  
Venom Gland ◽  
Anatomical Feature ◽  
Isomerase Activity ◽  
Novel Proteins ◽  
Pharmaceutical Applications ◽  
Ornithorhynchus Anatinus ◽  
Animal Venoms ◽  
Proteins And Peptides

An anatomical feature of the platypus (Ornithorhynchus anatinus) that is seen in only one other mammal, the echidna, is that the male has a crural glandular system that produces venom that is used for defence and territorial–breeding functions; whether the echidna is similarly venomous is not yet established. Platypus venom contains many novel proteins and peptides that are different from those in reptilian venom. It also causes pain and symptoms that are not experienced by any other kind of envenomation. Five types of proteins and peptides have been isolated and identified from platypus venom, namely: defensin-like peptides (DLPs); Ornithorhynchus venom C-type natriuretic peptides (OvCNPs); Ornithorhynchus nerve growth factor; hyaluronidase; and l-to-d-peptide isomerase. The structures of DLPs and OvCNPs have already been studied and they are very similar to β-defensin-12 and mammalian C-type natriuretic peptides, respectively. A special mammalian l-to-d-peptide isomerase that is responsible for interconverting the l- and d-peptide isomers is also found in platypus venom. Isomerase activity has recently been discovered in platypus tissues other than the venom gland. It is possible that similar kinds of enzymes might exist in other mammals and play important, as yet unknown, biological roles. Considering the fact that some animal venoms have already been widely used in pharmaceutical applications, research into platypus venom may lead to the discovery of new molecules and potent drugs that are useful biomedical tools.

Animal Venoms have Potential to Treat Cancer

2019 ◽  
Vol 18 (30) ◽  
pp. 2555-2566 ◽  
Author(s):  
Bhaswati Chatterjee
Keyword(s):  
Cancer Therapeutics ◽  
Sea Anemones ◽  
Anticancer Activities ◽  
Inhibition Of Proliferation ◽  
Cycle Arrest ◽  
Venomous Animals ◽  
Anti Cancer ◽  
Cancerous Cells ◽  
Animal Venoms ◽  
Proteins And Peptides

The resistance to chemotherapeutics by the cancerous cells has made its treatment more complicated. Animal venoms have emerged as an alternative strategy for anti-cancer therapeutics. Animal venoms are cocktails of complex bioactive chemicals mainly disulfide-rich proteins and peptides with diverse pharmacological actions. The components of venoms are specific, stable, and potent and have the ability to modify their molecular targets thus making them good therapeutics candidates. The isolation of cancer-specific components from animal venoms is one of the exciting strategies in anti-cancer research. This review highlights the identified venom peptides and proteins from different venomous animals like snakes, scorpions, spiders, bees, wasps, snails, toads, frogs and sea anemones and their anticancer activities including inhibition of proliferation of cancer cells, their invasion, cell cycle arrest, induction of apoptosis and the identification of involved signaling pathways.

scholarly journals Synthesis and functionalization of glucan dendrimer, and its application as a drug delivery system carrier

Amylase ◽  
2021 ◽  
Vol 5 (1) ◽  
pp. 50-61
Author(s):  
Michiyo Yanase ◽  
Takashi Kuriki
Keyword(s):  
Glucuronic Acid ◽  
Molecular Surface ◽  
Branching Enzyme ◽  
Sucrose Phosphorylase ◽  
Pharmaceutical Applications ◽  
Natural Polysaccharide ◽  
Suitable Form ◽  
Glucan Phosphorylase ◽  
Sugar Chains ◽  
Proteins And Peptides

Abstract Glycogen is a natural polysaccharide with a dendrimer structure, in which glucose is frequently branched and polymerized. Functionalizing the numerous non-reducing ends on the molecular surface of glycogen could be expected to enable its use in various fields. We developed a method for enzymatically synthesizing a suitable form of glycogen from sucrose by using sucrose phosphorylase and branching enzyme, both of which belong to the α-amylase family, as well as glucan phosphorylase. We refer to this enzymatically synthesized glycogen as the glucan dendrimer (GD). We then selectively modified the non-reducing ends on the surface of GD particles by using the reaction of glucan phosphorylase with various hexose 1-phosphates. Modifying the non-reducing ends of GD with glucuronic acid or glucosamine added negative and positive charges to the GD particles. In addition, we found that glucuronic acid and/or glucosamine residues at the non-reducing ends can be used to covalently conjugate functional substances, such as sugar chains, proteins, and peptides to the surface of GD particles. GD and modification of its non-reducing ends represent versatile platforms for pharmaceutical applications of polysaccharides.

scholarly journals Identification and characterization of novel proteins from Arizona bark scorpion venom that inhibit Nav1.8, a voltage-gated sodium channel regulator of pain signaling

2021 ◽  
Author(s):  
Tarek Mohamed Abd El-Aziz ◽  
Yucheng Xiao ◽  
Jake Kline ◽  
Harold Gridley ◽  
Alyse Heaston ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Venom Gland ◽  
Reversed Phase ◽  
Scorpion Venom ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated ◽  
Novel Proteins ◽  
Centruroides Sculpturatus ◽  
Current Mass ◽  
Venom Proteins

The voltage-gated sodium channel Nav1.8 is linked to neuropathic and inflammatory pain, high-lighting the potential to serve as a drug target. However, the biophysical mechanisms that regu-late Nav1.8 activation and inactivation gating are not completely understood. Progress has been hindered by a lack of biochemical tools for examining Nav1.8 gating mechanisms. Arizona bark scorpion (Centruroides sculpturatus) venom proteins inhibit Nav1.8 and block pain in grasshopper mice (Onychomys torridus). These proteins provide tools for examining Nav1.8 structure-activity relationships. To identify proteins that inhibit Nav1.8 activity, venom samples were fractioned using liquid chromatography (reversed phase and ion exchange). A recombinant Nav1.8 clone expressed in ND7/23 cells was used to identify subfractions that inhibited Nav1.8 Na+ current. Mass spectrometry-based bottom-up proteomic analyses identified unique peptides from inhibi-tory subfractions. A search of the peptides against the AZ bark scorpion venom gland transcrip-tome revealed four novel proteins between 40 and 60% conserved with venom proteins from scorpions in four genera (Centruroides, Parabuthus, Androctonus, and Tityus). Ranging from 63 to 82 amino acids, each primary structure includes 8 cysteines and a CXCE motif where X = an aro-matic residue (tryptophan, tyrosine or phenylalanine). Electrophysiology data demonstrated that the inhibitory effects of bioactive subfractions can be removed by hyperpolarizing the channels, suggesting that proteins may function as gating modifiers as opposed to pore blockers.

scholarly journals Comparison of Methods for Measuring Protein Concentration in Venom Samples

Animals ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 448 ◽  
Author(s):  
Aleksandra Bocian ◽  
Sonja Sławek ◽  
Marcin Jaromin ◽  
Konrad K. Hus ◽  
Justyna Buczkowicz ◽  
...  
Keyword(s):  
Protein Concentration ◽  
Complex Mixture ◽  
Venom Protein ◽  
Agkistrodon Contortrix ◽  
Venom Composition ◽  
Natural Mixture ◽  
Pharmacological Potential ◽  
Animal Venoms ◽  
High Diversity ◽  
Proteins And Peptides

Snake venom is an extremely interesting natural mixture of proteins and peptides, characterized by both high diversity and high pharmacological potential. Much attention has been paid to the study of venom composition of different species and also detailed analysis of the properties of individual components. Since proteins and peptides are the active ingredients in venom, rapidly developing proteomic techniques are used to analyze them. During such analyses, one of the routine operations is to measure the protein concentration in the sample. The aim of this study was to compare five methods used to measure protein content in venoms of two snake species: the Viperids representative, Agkistrodon contortrix, and the Elapids representative, Naja ashei. The study showed that for A. contortrix venom, the concentration of venom protein measured by four methods is very similar and only the NanoDrop method clearly stands out from the rest. However, in the case of N. ashei venom, each technique yields significantly different results. We hope that this report will help to draw attention to the problem of measuring protein concentration, especially in such a complex mixture as animal venoms.

scholarly journals Proteo-Transcriptomic Characterization of the Venom from the Endoparasitoid Wasp Pimpla turionellae with Aspects on Its Biology and Evolution

Toxins ◽  
2019 ◽  
Vol 11 (12) ◽  
pp. 721 ◽  
Author(s):  
Rabia Özbek ◽  
Natalie Wielsch ◽  
Heiko Vogel ◽  
Günter Lochnit ◽  
Frank Foerster ◽  
...  
Keyword(s):  
Transcriptome Assembly ◽  
Parasitoid Wasp ◽  
Venom Gland ◽  
Hymenopteran Species ◽  
Robber Flies ◽  
And Function ◽  
Wasp Venoms ◽  
Venom Proteins ◽  
Proteins And Peptides

Within mega-diverse Hymenoptera, non-aculeate parasitic wasps represent 75% of all hymenopteran species. Their ovipositor dual-functionally injects venom and employs eggs into (endoparasitoids) or onto (ectoparasitoids) diverse host species. Few endoparasitoid wasps such as Pimpla turionellae paralyze the host and suppress its immune responses, such as encapsulation and melanization, to guarantee their offspring’s survival. Here, the venom and its possible biology and function of P. turionellae are characterized in comparison to the few existing proteo-transcriptomic analyses on parasitoid wasp venoms. Multiple transcriptome assembly and custom-tailored search and annotation strategies were applied to identify parasitoid venom proteins. To avoid false-positive hits, only transcripts were finally discussed that survived strict filter settings, including the presence in the proteome and higher expression in the venom gland. P. turionella features a venom that is mostly composed of known, typical parasitoid enzymes, cysteine-rich peptides, and other proteins and peptides. Several venom proteins were identified and named, such as pimplin2, 3, and 4. However, the specification of many novel candidates remains difficult, and annotations ambiguous. Interestingly, we do not find pimplin, a paralytic factor in Pimpla hypochondriaca, but instead a new cysteine inhibitor knot (ICK) family (pimplin2), which is highly similar to known, neurotoxic asilid1 sequences from robber flies.

Platypus Venom: a Review

2007 ◽  
Vol 29 (1) ◽  
pp. 57 ◽  
Author(s):  
Camilla Whittington ◽  
Katherine Belov
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Natriuretic Peptide ◽  
Mating Season ◽  
Sea Anemones ◽  
Nerve Growth ◽  
Evolutionary Lineage ◽  
Ornithorhynchus Anatinus ◽  
Important Position ◽  
Insight Into

Platypuses (Ornithorhynchus anatinus) and other monotremes occupy an important position as an early offshoot from the evolutionary lineage leading from reptiles to mammals. One of the most intriguing characteristics of these mammals is that the males produce venom during the mating season. O. anatinus venom contains defensin-like peptide, C-type natriuretic peptide and nerve growth factor, as well as other unidentified fractions. These components of O. anatinus venom display similarity to components of the venom of other species such as sea anemones, snakes and shrews. Here we review available literature on O. anatinus venom and venom in other species. Further research into O. anatinus venom will offer some insight into the evolution and functions of venom components.

L-to-D-peptide isomerase in male echidna venom

2010 ◽  
Vol 58 (5) ◽  
pp. 284 ◽  
Author(s):  
Jennifer M. S. Koh ◽  
Leesa Haynes ◽  
Katherine Belov ◽  
Philip W. Kuchel
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
High Performance ◽  
Hind Limb ◽  
Reproductive Behaviour ◽  
Reverse Phase ◽  
Isomerase Activity ◽  
Rp Hplc ◽  
Synthetic Hexapeptide ◽  
Proteins And Peptides

The monotremes (the echidnas and the platypus) display both mammalian and reptilian features. Male monotremes have a bilateral crural gland that is connected via a duct to a spur on each hind limb. Male echidnas appear not to use their spurs as weapons in aggressive acts, but the crural system may have a role in reproductive behaviour because it appears only to be active during the breeding season. The secretions produced by the echidna’s crural gland have not hitherto been biochemically or pharmacologically characterised. We used reverse-phase high-performance liquid chromatography (RP-HPLC) to separate the components of echidna venom and compared the chromatograms with those from platypus venom. The echidna venom appears to contain fewer proteins and peptides than platypus venom; however, it appears to have defensin-like peptides that behave similarly on RP-HPLC to those in platypus venom. Like platypus venom, echidna venom has peptidyl aminoacyl l/d-peptide isomerase activity. An RP-HPLC-based assay showed that the second amino acid residue, of a probe synthetic hexapeptide, was converted into the d-form, when incubated with echidna venom.

scholarly journals An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant Paraponera clavata

Toxins ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 324
Author(s):  
Samira R. Aili ◽  
Axel Touchard ◽  
Regan Hayward ◽  
Samuel D. Robinson ◽  
Sandy S. Pineda ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Venom Gland ◽  
Sequence Database ◽  
Liquid Chromatography Mass Spectrometry ◽  
Ant Venom ◽  
Proteomic Investigation ◽  
Paraponera Clavata ◽  
And Function ◽  
Venom Proteins ◽  
Proteins And Peptides

A critical hurdle in ant venom proteomic investigations is the lack of databases to comprehensively and specifically identify the sequence and function of venom proteins and peptides. To resolve this, we used venom gland transcriptomics to generate a sequence database that was used to assign the tandem mass spectrometry (MS) fragmentation spectra of venom peptides and proteins to specific transcripts. This was performed alongside a shotgun liquid chromatography–mass spectrometry (LC-MS/MS) analysis of the venom to confirm that these assigned transcripts were expressed as proteins. Through the combined transcriptomic and proteomic investigation of Paraponera clavata venom, we identified four times the number of proteins previously identified using 2D-PAGE alone. In addition to this, by mining the transcriptomic data, we identified several novel peptide sequences for future pharmacological investigations, some of which conform with inhibitor cysteine knot motifs. These types of peptides have the potential to be developed into pharmaceutical or bioinsecticide peptides.

scholarly journals Phylogenetic analyses suggest centipede venom arsenals were repeatedly stocked by horizontal gene transfer

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Eivind A. B. Undheim ◽  
Ronald A. Jenner
Keyword(s):  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Phylogenetic Analyses ◽  
Gene Families ◽  
Venom Gland ◽  
Bacterial Gene ◽  
Multiple Gene ◽  
Genomic Analyses ◽  
Endogenous Proteins ◽  
Animal Venoms

AbstractVenoms have evolved over a hundred times in animals. Venom toxins are thought to evolve mostly by recruitment of endogenous proteins with physiological functions. Here we report phylogenetic analyses of venom proteome-annotated venom gland transcriptome data, assisted by genomic analyses, to show that centipede venoms have recruited at least five gene families from bacterial and fungal donors, involving at least eight horizontal gene transfer events. These results establish centipedes as currently the only known animals with venoms used in predation and defence that contain multiple gene families derived from horizontal gene transfer. The results also provide the first evidence for the implication of horizontal gene transfer in the evolutionary origin of venom in an animal lineage. Three of the bacterial gene families encode virulence factors, suggesting that horizontal gene transfer can provide a fast track channel for the evolution of novelty by the exaptation of bacterial weapons into animal venoms.

scholarly journals Identification and Characterization of Novel Proteins from Arizona Bark Scorpion Venom That Inhibit Nav1.8, a Voltage-Gated Sodium Channel Regulator of Pain Signaling

Toxins ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 501
Author(s):  
Tarek Mohamed Abd El-Aziz ◽  
Yucheng Xiao ◽  
Jake Kline ◽  
Harold Gridley ◽  
Alyse Heaston ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Venom Gland ◽  
Reversed Phase ◽  
Scorpion Venom ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated ◽  
Novel Proteins ◽  
Centruroides Sculpturatus ◽  
Current Mass ◽  
Venom Proteins

The voltage-gated sodium channel Nav1.8 is linked to neuropathic and inflammatory pain, highlighting the potential to serve as a drug target. However, the biophysical mechanisms that regulate Nav1.8 activation and inactivation gating are not completely understood. Progress has been hindered by a lack of biochemical tools for examining Nav1.8 gating mechanisms. Arizona bark scorpion (Centruroides sculpturatus) venom proteins inhibit Nav1.8 and block pain in grasshopper mice (Onychomys torridus). These proteins provide tools for examining Nav1.8 structure–activity relationships. To identify proteins that inhibit Nav1.8 activity, venom samples were fractioned using liquid chromatography (reversed-phase and ion exchange). A recombinant Nav1.8 clone expressed in ND7/23 cells was used to identify subfractions that inhibited Nav1.8 Na+ current. Mass-spectrometry-based bottom-up proteomic analyses identified unique peptides from inhibitory subfractions. A search of the peptides against the AZ bark scorpion venom gland transcriptome revealed four novel proteins between 40 and 60% conserved with venom proteins from scorpions in four genera (Centruroides, Parabuthus, Androctonus, and Tityus). Ranging from 63 to 82 amino acids, each primary structure includes eight cysteines and a “CXCE” motif, where X = an aromatic residue (tryptophan, tyrosine, or phenylalanine). Electrophysiology data demonstrated that the inhibitory effects of bioactive subfractions can be removed by hyperpolarizing the channels, suggesting that proteins may function as gating modifiers as opposed to pore blockers.

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