Partial purification and characterization of a hemolysin (CAH1) from Hawaiian box jellyfish ( Carybdea alata ) venom

Chung, John J.; Ratnapala, L. A.; Cooke, Ian M.; Yanagihara, Angel A.

doi:10.1016/s0041-0101(00)00237-3

Cited by 102 publications

(66 citation statements)

References 14 publications

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“…Furthermore, as demonstrated here and in a previous study (3), the CfTX proteins have a propensity to oligomerize into high molecular mass quaternary structures, implying that although each toxin is individually The functional role(s) of the C-terminal domain in CfTX-like toxins is less clear, but due to its structural similarity (albeit weaker) to Domain II of 3d-Cry toxins, it may be involved in receptor binding and/or toxin specificity. Earlier experimental studies found that purified CaTX-A bound to specific carbohydrates (40), which implicates these carbohydrates as potential sugar moieties in toxin-binding receptors. However, further functional studies are still necessary to establish which domain(s) are involved in receptor binding and whether the carbohydrate-binding affinity of CfTX-like toxins influences target specificity.…”

Section: Discussionmentioning

confidence: 92%

Chironex fleckeri (Box Jellyfish) Venom Proteins

Brinkman

Konstantakopoulos

McInerney

et al. 2014

Journal of Biological Chemistry

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Background: Box jellyfish produce a unique family of toxic venom proteins. Results: The toxins are structurally similar, yet two subgroups confer different cytolytic activities in red blood cells and cardiovascular effects in rats. Conclusion: Diversification within the toxin family may influence toxin function/specificity. Significance: Characterization of the toxins provides new insight into their potential roles in human envenoming.

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Section: Discussionmentioning

confidence: 92%

Chironex fleckeri (Box Jellyfish) Venom Proteins

Brinkman

Konstantakopoulos

McInerney

et al. 2014

Journal of Biological Chemistry

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“…Haemolytic activity was found to be reduced when the crude venom from Carybdea alata was pre incubated at temperatures above 25C (Chung et al, 2001). Other, non published data, from one of us (JS) has demonstrated a similar loss of lethality when Carukia barnesi venom is heated above 43 C.…”

Section: Discussionmentioning

confidence: 73%

Successful use of heat as first aid for tropical Australian jellyfish stings

Little

Fitzpatrick

Seymour

2016

Toxicon

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a b s t r a c tCurrently the Australian Resuscitation Council (ARC) recommends dousing with vinegar followed by ice as first aid for jellyfish stings in tropical Australia, with limited evidence to support this recommendation (Li et al., 2013). We report our successful experience in using hot water immersion as first aid in treating two people stung by venomous tropical Australian jellyfish, one by Chironex fleckeri and one by Carukia barnesi.© 2016 Elsevier Ltd. All rights reserved. Clinical recordA 35 yo M cinematographer was filming documentary on Irukandji jellyfish at Palm Cove, Queensland. He was coming to the shore holding a camera housing, and removed his glove to lift the housing out of the water. As he placed his left hand underwater he contacted a jellyfish, where the tentacle ran from ½ way down the extensor surface of his forearm, running around the web space of his L hand across his palm and then between the ring and middle finger, and ending dorsally at the wrist joint. It was estimated to be 30 cm of tentacle, which was typical for Carukia barnesi.Within 5 minutes his entire forearm and hand was immersed in hot water (as hot as he could tolerate) in a plastic container. This was left there for about 20 minutes, with the water being replaced several times as soon as the water cooled.He was taken to the ED at Cairns Hospital, was observed for 5 hours and did not require any analgesia medication.The jellyfish, wrapped around the victims arm, was captured and later identified as Carukia barnesi.A 40yo M biologist was at Palm Cove collecting Box jellyfish (Chironex fleckeri). Whilst collecting one animal, he was stung across both hands and fingers on both the dorsal and palmer aspects by a Chironex fleckeri box jellyfish with a bell 25cm diameter. He had immediate severe pain, which the patient described 'brought him to tears'. He immediately rubbed his hands in wet sand and within 5 minutes he placed both hands in a plastic container of hot water (as hot as he could tolerate) for about 10 minutes. He had almost immediate relief of pain, and the severe pain recurred as the water temperature cooled and had the hot water replaced about four times. After ten minutes the pain had settled and was minimal, although he had marked swelling of his hands that settled over 48 hours. He required no analgesia medication. He had no permanent scarring.

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“…Divalent cations could inhibit hemolysis by stabilizing the erythrocyte membrane; alternatively, they could combine with the toxin, thus preventing the binding of the peptide to the membrane (Malovrh et al 1999). Inhibition of hemolysis by carbohydrates has been reported for other hemolytic toxins, which is suggestive of a carbohydrate protection mechanism for erythrocyte membranes (Chung et al 2001). The binding of cholesterol and the capacity to form pores in host cell membranes are major characteristics of hemolytic peptides (Raghuraman and Chattopadhyay 2005).…”

Section: Discussionmentioning

confidence: 91%

“…Aliquots of extract (300 μl, 75 μg protein total) were incubated for 30 min at 37°C with different concentrations of DTT or trypsin; the total volume was brought up to 1 ml with PBS, pH 7.2. Then, 100 μl of the pre-incubated materials, corresponding to 1.5 HU (10.71 μg/ml), was mixed with 100 μl of a 4% w/v RBC suspension and 500 μl of PBS (pH 7.2); after incubation at 37°C for 30 min, the samples were assayed for hemolytic activity (Chung et al 2001). …”

Section: Effect Of Temperature On Hemolytic Activitymentioning

confidence: 99%

A hemolytic peptide from the mycophilic fungus Sepedonium chrysospermum (Bull.) Fr.

Sanguineti

Cosulich

Salis

et al. 2011

Appl Microbiol Biotechnol

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The hemolytic activity of an extract of the mycoparasite Sepedonium chrysospermum (teleomorph Hypomyces chrysospermus) was detected and characterized. Extraction of the fungal biomass by methanol yielded a fraction in which the hemolytic activity against human red blood cells corresponded to a peptide with a molecular mass of 7,653.72 Da and an isoelectric point of approximately 5.8. The peptide was temperature resistant, and the hemolysis was only partially inhibited, even after a 30-min pre-incubation at 100°C. Its hemolytic activity was unaffected by treatment with proteolytic enzymes such as trypsin. Among the divalent cations assayed, Hg(2+) was the strongest inhibitor of hemolysis. The reducing agent, dithiothreitol, and the membrane lipid, cholesterol, demonstrated concentration-dependent inhibitory activities. Finally, hemolytic activity triggered by the peptide was analyzed by scanning electron microscopy, and a pore-forming activity was detected.

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Partial purification and characterization of a hemolysin (CAH1) from Hawaiian box jellyfish ( Carybdea alata ) venom

Cited by 102 publications

References 14 publications

Chironex fleckeri (Box Jellyfish) Venom Proteins

Chironex fleckeri (Box Jellyfish) Venom Proteins

Successful use of heat as first aid for tropical Australian jellyfish stings

A hemolytic peptide from the mycophilic fungus Sepedonium chrysospermum (Bull.) Fr.

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