A Review of Toxins from Cnidaria

D’Ambra, Isabella; Lauritano, Chiara

doi:10.3390/md18100507

Cited by 60 publications

(75 citation statements)

References 198 publications

(101 reference statements)

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“…Secreted phospholipases A 2 (sPLA 2 ) are venom components widely distributed in organisms of all kingdoms, from cnidarians and insects (bees, wasps and ants) to arachnids and venomous snakes [ 181 , 182 , 183 , 184 ]. Based on their structure-activity, venom PLA2 are classified into distinct types that include enzymes that cause hydrolysis of glycerophospholipids and damage cell membranes, as well as toxins devoid of enzymatic activity that cause neurotoxicity and immunomodulation, inflammation and pain.…”

Section: Cell-penetrating Peptides From Animal Venoms and Toxinsmentioning

confidence: 99%

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Rádis‐Baptista

2021

Toxins

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Cell-penetrating peptides (CPPs) comprise a class of short polypeptides that possess the ability to selectively interact with the cytoplasmic membrane of certain cell types, translocate across plasma membranes and accumulate in the cell cytoplasm, organelles (e.g., the nucleus and mitochondria) and other subcellular compartments. CPPs are either of natural origin or de novo designed and synthesized from segments and patches of larger proteins or designed by algorithms. With such intrinsic properties, along with membrane permeation, translocation and cellular uptake properties, CPPs can intracellularly convey diverse substances and nanomaterials, such as hydrophilic organic compounds and drugs, macromolecules (nucleic acids and proteins), nanoparticles (nanocrystals and polyplexes), metals and radionuclides, which can be covalently attached via CPP N- and C-terminals or through preparation of CPP complexes. A cumulative number of studies on animal toxins, primarily isolated from the venom of arthropods and snakes, have revealed the cell-penetrating activities of venom peptides and toxins, which can be harnessed for application in biomedicine and pharmaceutical biotechnology. In this review, I aimed to collate examples of peptides from animal venoms and toxic secretions that possess the ability to penetrate diverse types of cells. These venom CPPs have been chemically or structurally modified to enhance cell selectivity, bioavailability and a range of target applications. Herein, examples are listed and discussed, including cysteine-stabilized and linear, α-helical peptides, with cationic and amphipathic character, from the venom of insects (e.g., melittin, anoplin, mastoparans), arachnids (latarcin, lycosin, chlorotoxin, maurocalcine/imperatoxin homologs and wasabi receptor toxin), fish (pardaxins), amphibian (bombesin) and snakes (crotamine and cathelicidins).

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Section: Cell-penetrating Peptides From Animal Venoms and Toxinsmentioning

confidence: 99%

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Rádis‐Baptista

2021

Toxins

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“…Sea anemone (Cnidaria, Anthozoa) venom is an important source of bioactive compounds, mainly toxins. These cause severe cardiotoxicity and results in the death of human beings [10]. Tube anemones or cerianthids, posses venom in stinging-cell rich tentacles prey and defend against predators [11].…”

Section: Sea Anemones Toxinsmentioning

confidence: 99%

“…This is isolated from Urticinaeques that produces analgesic activity [53]. The cold-water sea anemone Cnidopus japonicas contain neurotoxins, toxin-like molecules, linear polypeptides (Cys-free), enzymes, which show analgesic effects [60] Sea anemone contains one bioactive peptide named α-AnmTxUeq 12-1 (Ueq 12-1) (fig. 3).…”

Section: Analgesic Activitymentioning

confidence: 99%

“…It also limits the proliferation of endothelial cells proliferation and angiogenesis. It shows trypsin activity inhibition of a Kunitz-type inhibitor that interact with an integrin due to an Arginine Glycin Aspartate (RGD) motif [60]. The anti-angiotensin I converting enzyme activity of box jellyfish, Chiropsalmus quadrigatus Haeckel contanvenom hydrolysate.…”

Section: Anti-angiogenesismentioning

confidence: 99%

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Coelenterate Toxins, Its Pharmaceutical and Therapeutic Effects

Sharma

Upadhyay

2021

Int J Curr Pharm Sci

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Present review article emphasizes species specific coelenterate toxins, its pharmaceutical and therapeutic effects. Most of the coelenterates inflict venom accidently by using nematocysts found on arms. These animals very quickly do massive and multiple inflictions of venom which causes cardiotoxicity that leads to the death of human beings. Coelenterate venom toxin groups differ in their composition and show diverse biological activity i.e. cytolytic or neurotoxic, hemolytic, anti-parasitic activity, α-amylase inhibitor activity, and analgesic activity anti-cancerous and antitumor activity, anti-inflammatory and antimicrobial activity. Coelenterate venom initiates toxic and immunological reactions exert their effects by modifying the properties of the ion channels involved in action potential generation in nerve, heart, and skeletal muscles. This article suggests available information, on coelenterate toxins could be used to develop potential therapeutic interventions for various human diseases and disorders.

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“…These bioreactive compounds are mostly used for defense, competition, and predation [ 5 ], and, due to their potential specificity towards a wide range of molecular targets, they gave rise to a considerable interest for drug discovery purposes [ 6 ]. Venomous animals like snakes, scorpions, and spiders have been receiving attention for their potential biomedical applications and were recently joined by marine invertebrates like cnidarians, annelids, cone snails, and even cephalopods [ 7 , 8 , 9 ].…”

Section: Introductionmentioning

confidence: 99%

Localization and Bioreactivity of Cysteine-Rich Secretions in the Marine Gastropod Nucella lapillus

et al. 2021

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Marine biodiversity has been yielding promising novel bioproducts from venomous animals. Despite the auspices of conotoxins, which originated the paradigmatic painkiller Prialt, the biotechnological potential of gastropod venoms remains to be explored. Marine bioprospecting is expanding towards temperate species like the dogwhelk Nucella lapillus, which is suspected to secrete immobilizing agents through its salivary glands with a relaxing effect on the musculature of its preferential prey, Mytilus sp. This work focused on detecting, localizing, and testing the bioreactivity of cysteine-rich proteins and peptides, whose presence is a signature of animal venoms and poisons. The highest content of thiols was found in crude protein extracts from the digestive gland, which is associated with digestion, followed by the peribuccal mass, where the salivary glands are located. Conversely, the foot and siphon (which the gastropod uses for feeding) are not the main organs involved in toxin secretion. Ex vivo bioassays with Mytilus gill tissue disclosed the differential bioreactivity of crude protein extracts. Secretions from the digestive gland and peribuccal mass caused the most significant molecular damage, with evidence for the induction of apoptosis. These early findings indicate that salivary glands are a promising target for the extraction and characterization of bioactive cysteine-rich proteinaceous toxins from the species.

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A Review of Toxins from Cnidaria

Cited by 60 publications

References 198 publications

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Coelenterate Toxins, Its Pharmaceutical and Therapeutic Effects

Localization and Bioreactivity of Cysteine-Rich Secretions in the Marine Gastropod Nucella lapillus

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