Polypeptide cytolytic toxins from sea anemones (Actiniaria)

Maček, Peter

doi:10.1016/0378-1097(92)90082-y

Cited by 20 publications

(24 citation statements)

References 29 publications

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“…Four major groups of these cytolysins are found in cnidarians (5,6). Among them, the 19-kDa pore-forming cytolysins are the most predominant (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15).…”

Section: Introductionmentioning

confidence: 99%

“…Four major groups of these cytolysins are found in cnidarians (5,6). Among them, the 19-kDa pore-forming cytolysins are the most predominant (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15). In previous studies, the sea anemone Heteractis magnifica was subjected to the analysis of different cytolysins including magnificalysins Hmg I, Hmg II and Hmg III (14)(15)(16)(17)(18).…”

Section: Introductionmentioning

confidence: 99%

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Characterization, purification and phylogenetic analysis of a cytolysin from the sea anemone Heteractis magnifica of the Indian Ocean

Karthikayalu¹,

Rama²,

Kirubagaran³

et al. 2010

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

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ABSTRACT:It is well established that sea anemones comprise a rich source of cytolytic toxins. The present study reports the isolation and characterization of a cytolysin obtained from the sea anemone Heteractis magnifica collected in the Andaman Islands of the Indian Ocean. The crude extract was screened for hemolytic activity by a blood agar plate method and a 6-mm zone of clearance was observed after incubation. The hemolytic property of the crude extract, tested by the microtiter plate method, revealed positive results at concentrations as low as 120 ng/mL. Furthermore, it was favored by alkaline pH and was stable up to 60°C. On the other hand, the hemolytic effect was abolished by the addition of human serum. Purification steps involved ammonium sulfate precipitation and subsequent desalting by dialysis, followed by anion-and cation-exchange chromatographies. The purified fractions displayed the presence of a 19-kDa cytolysin when analyzed by SDS-PAGE. The conserved region of the cytolysin (with 303 bp) was amplified by RT-PCR and was sequenced. The sequence showed maximum homology (97%) with the already reported cytolysins from other sea anemone species.

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“…Four major groups of these cytolysins are found in cnidarians (5,6). Among them, the 19-kDa pore-forming cytolysins are the most predominant (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15).…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization, purification and phylogenetic analysis of a cytolysin from the sea anemone Heteractis magnifica of the Indian Ocean

Karthikayalu¹,

Rama²,

Kirubagaran³

et al. 2010

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

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“…When stressed the coral release toxins that get trapped in the mucus and function as first line of defense. Moreover, toxin production, a common feature of cnidarians, allows them to produce a variety of peptides and proteins that act as either neurotoxins or cytolysins (3)(4)(5)(6). Toxins are produced by specialized stinging cells, the nematocysts.…”

Section: Introductionmentioning

confidence: 99%

“…Despite the belief that all cnidarians are venomous, the extant biochemical and functional studies have focused only on a few groups and very little research has been done on the toxicology of soft corals. But soft coral stinging nematocysts contain active proteinaceous venoms, while the extra-nematocyst tissues possess many other biologically and pharmacologically active metabolites (1)(2)(3)(4)(5)(6)(7). Hence, the present study was undertaken to identify the cytolytic toxins from the soft coral Sarcophyton trocheliophorum.…”

Section: Introductionmentioning

confidence: 99%

Hemolytic toxin from the soft coral Sarcophyton trocheliophorum: isolation and physiological characterization

Karthikayalu¹,

Rama²,

Kirubagaran³

et al. 2010

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

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ABSTRACT:The unifying characteristic of cnidarians is the production of protein and polypeptide toxins. The present study describes the identification of a hemolytic toxin from the soft coral Sarcophyton trocheliophorum. The crude extract was highly cytotoxic (EC 50 = 50 ng/mL) against human erythrocytes. It was also tested for hemolytic activity by the blood agar plate method, resulting in a hemolytic halo of 12 mm with 50 µg of protein. The stability of the venom under different physiological conditions was analyzed. The venom hemolytic activity was augmented by alkaline and neutral pH whereas it was reduced in acidic pH. The activity was stable up to 60°C. The hemolytic activity was completely abolished by the addition of serum and reduced significantly during frequent freezing-thawing cycles. Toxin purification was performed by ammonium sulfate precipitation and subsequently desalted by dialysis against 10 mM sodium phosphate buffer (pH 7.2), followed by anion exchange chromatography on DEAE cellulose column and gel filtration chromatography using Sephadex G-50 matrix. The purified active fractions possessed a prominent protein of approximately 45 kDa, as revealed by SDS-PAGE.

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“…Cytolysins that act on cell membranes (pore-forming toxins) have also been described (3,4). All these types of peptides have been isolated from different species such as Anemonia sulcata (5), Stoichactis helianthus (6), Actinia equina (7), Bunodosoma granulifera (2,8,9) and Bunodosoma caissarum (10,11).…”

Section: Introductionmentioning

confidence: 99%

Identification of hemolytic and neuroactive fractions in the venom of the sea anemone Bunodosoma cangicum

Lagos

Durán

Červeñanský

et al. 2001

Braz J Med Biol Res

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Sea anemones are a rich source of biologically active substances. In crayfish muscle fibers, Bunodosoma cangicum whole venom selectively blocks the I K(Ca) currents. In the present study, we report for the first time powerful hemolytic and neuroactive effects present in two different fractions obtained by gel-filtration chromatography from whole venom of B. cangicum. A cytolytic fraction (Bcg-2) with components of molecular mass ranging from 8 to 18 kDa elicited hemolysis of mouse erythrocytes with an EC 50 = 14 µg/ml and a maximum dose of 22 µg/ml. The effects of the neuroactive fraction, Bcg-3 (2 to 5 kDa), were studied on isolated crab nerves. This fraction prolonged the compound action potentials by increasing their duration and rise time in a dose-dependent manner. This effect was evident after the washout of the preparation, suggesting the existence of a reversible substance that was initially masking the effects of an irreversible one. In order to elucidate the target of Bcg-3 action, the fraction was applied to a tetraethylammonium-pretreated preparation. An additional increase in action potential duration was observed, suggesting a blockade of a different population of K + channels or of tetraethylammonium-insensitive channels. Also, tetrodotoxin could not block the action potentials in a Bcg-3-pretreated preparation, suggesting a possible interaction of Bcg-3 with Na + channels. The present data suggest that B. cangicum venom contains at least two bioactive fractions whose activity on cell membranes seems to differ from the I K(Ca) blockade described previously.

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Polypeptide cytolytic toxins from sea anemones (Actiniaria)

Cited by 20 publications

References 29 publications

Characterization, purification and phylogenetic analysis of a cytolysin from the sea anemone Heteractis magnifica of the Indian Ocean

Characterization, purification and phylogenetic analysis of a cytolysin from the sea anemone Heteractis magnifica of the Indian Ocean

Hemolytic toxin from the soft coral Sarcophyton trocheliophorum: isolation and physiological characterization

Identification of hemolytic and neuroactive fractions in the venom of the sea anemone Bunodosoma cangicum

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