Characterising the enzymatic profile of crude tentacle extracts from the South Atlantic jellyfish Olindias sambaquiensis (Cnidaria: Hydrozoa)

Knittel, Paloma Sirigatti; Long, Paul F.; Brammall, Lucas; Marques, Antônio Carlos; Almeida, Michelle; Padilla, Gabriel; Moura-da-Silva, Ana Maria

doi:10.1016/j.toxicon.2016.04.048

Cited by 29 publications

(20 citation statements)

References 49 publications

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“…These extracts did not display hyaluronidase activity. The levels of PLA 2 activity of these scleractinian corals were similar to those previously reported for the hydrozoans M. complanata and M. alcicornis [38], whereas the serine-protease activity levels were similar to those observed in jellyfish and snakes [53]. These results suggest that PLA 2 and serine proteases play an important role in the toxicity of the scleractinian corals.…”

Section: Discussionsupporting

confidence: 87%

“…Serine proteases have also been detected in the venom of the jellyfish Cyanea capillata by transcriptome analysis [52]. The presence of serine protease and PLA 2 in the crude venom from tentacles of the jellyfish Olindias sambaquiensis was experimentally confirmed, showing that the levels of activity of these enzymes were comparable to those observed in venoms of Bothrops snakes [53]. …”

Section: Discussionmentioning

confidence: 99%

“…The profiles of the extracts changed under reducing conditions, suggesting the presence of oligomeric proteins. Based on studies of other cnidarians, enzymes correspond to masses between 25 and 50 kDa [28, 53], whereas cytolysins are found mainly in the region of 20 kDa [28]. Several reports have shown than cnidarian venoms contain an important mixture of peptides with low molecular weights, mostly between 3 and 7 kDa, that act on voltage-gated sodium and potassium channels [29, 54], the presence of these neurotoxins in the cnidarian venoms is important for paralyzing their prey.…”

Section: Discussionmentioning

confidence: 99%

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Composition and biological activities of the aqueous extracts of three scleractinian corals from the Mexican Caribbean: Pseudodiploria strigosa, Porites astreoides and Siderastrea siderea

García-Arredondo

Rojas‐Molina

Ibarra‐Alvarado

et al. 2016

J Venom Anim Toxins Incl Trop Dis

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BackgroundScleractinian corals (stony corals) are the most abundant reef-forming cnidarians found in coral reefs throughout the world. Despite their abundance and ecological importance, information about the diversity of their toxins and their biological activities is very scarce. In this study, the chemical composition and the biological activities of the aqueous extracts of Pseudodiploria strigosa, Porites astreoides and Siderastrea siderea, three scleractinian corals from the Mexican Caribbean, have been assessed for the first time.MethodsToxicity of the extracts was assessed in crickets; the presence of cytolysins was detected by the hemolysis assay; the vasoconstrictor activity was determined by the isolated rat aortic ring assay; the nociceptive activity was evaluated by the formalin test. The presence of phospholipases A2 (PLA2), serine proteases, and hyaluronidases was determined by enzymatic methods. Low-molecular-weight fractions were obtained by gel filtration chromatography and ultrafiltration.ResultsExtracts from the three species were toxic to crickets, induced hemolysis in human and rat erythrocytes, produced vasoconstriction on isolated rat aortic rings, and presented phospholipase A2 and serine-protease activity. Despite the fact that these corals are not considered to be harmless to humans, the extracts generated significant nociceptive responses. The matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry analysis of the low-molecular-weight fractions revealed the presence of peptides within a mass range of 3000 to 6000 Da. These fractions were toxic to crickets and two of them induced a transitory vasoconstrictor effect on isolated rat aortic rings.ConclusionThis study suggests that scleractinian corals produce low-molecular-weight peptides that are lethal to crickets and induce vasoconstriction.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Composition and biological activities of the aqueous extracts of three scleractinian corals from the Mexican Caribbean: Pseudodiploria strigosa, Porites astreoides and Siderastrea siderea

García-Arredondo

Rojas‐Molina

Ibarra‐Alvarado

et al. 2016

J Venom Anim Toxins Incl Trop Dis

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“…The fluorimetric assays were performed using FRET (Fluorescence Resonance Energy Transfer) peptides as described [ 52 ] and modified [ 53 ]. The FRET peptide used was Abz-AGLA-EDDnp (MM 657.65 Da) from GenOne Biotechnologies (Rio de Janeiro, RJ, Brazil).…”

Section: Methodsmentioning

confidence: 99%

Insights into the Mechanisms Involved in Strong Hemorrhage and Dermonecrosis Induced by Atroxlysin-Ia, a PI-Class Snake Venom Metalloproteinase

Freitas-de-Sousa

Colombini

Lopes-Ferreira

et al. 2017

Toxins

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Hemorrhage is the most prominent effect of snake venom metalloproteinases (SVMPs) in human envenomation. The capillary injury is a multifactorial effect caused by hydrolysis of the components of the basement membrane (BM). The PI and PIII classes of SVMPs are abundant in viperid venoms and hydrolyze BM components. However, hemorrhage is associated mostly with PIII-class SVMPs that contain non-catalytic domains responsible for the binding of SVMPs to BM proteins, facilitating enzyme accumulation in the tissue and enhancing its catalytic efficiency. Here we report on Atroxlysin-Ia, a PI-class SVMP that induces hemorrhagic lesions in levels comparable to those induced by Batroxrhagin (PIII-class), and a unique SVMP effect characterized by the rapid onset of dermonecrotic lesions. Atroxlysin-Ia was purified from B. atrox venom, and sequence analyses indicated that it is devoid of non-catalytic domains and unable to bind to BM proteins as collagen IV and laminin in vitro or in vivo. The presence of Atroxlysin-Ia was diffuse in mice skin, and localized mainly in the epidermis with no co-localization with BM components. Nevertheless, the skin lesions induced by Atroxlysin-Ia were comparable to those induced by Batroxrhagin, with induction of leukocyte infiltrates and hemorrhagic areas soon after toxin injection. Detachment of the epidermis was more intense in skin injected with Atroxlysin-Ia. Comparing the catalytic activity of both toxins, Batroxrhagin was more active in the hydrolysis of a peptide substrate while Atroxlysin-Ia hydrolyzed more efficiently fibrin, laminin, collagen IV and nidogen. Thus, the results suggest that Atroxlysin-Ia bypasses the binding step to BM proteins, essential for hemorrhagic lesions induced by PII-and P-III class SVMPs, causing a significantly fast onset of hemorrhage and dermonecrosis, due to its higher proteolytic capacity on BM components.

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“…Based upon the molecular mass and previous published findings, another possible contributor to egg yolk hydrolysis is the small (13~19 kDa) secretory PLA 2 class lipases. PLA 2 -like activity has been extensively reported using 14 C-labelled arachidonic acid in the sn-2 position or 4-nitro-3-octanoyloxybenzoic acid as substrates in various cnidarians, including Cyanea capillata , Cyanea lamarckii (Pe′ron and Le′slieur) and Olindias sambaquiensis [ 22 , 23 , 24 ]. Moreover, when sheep erythrocytes were added into the substrate gel, marked hemolysis occurred at the location where the lipase hydrolyzed the egg yolk substrate ( Figure 2 B).…”

Section: Resultsmentioning

confidence: 99%

Functional Elucidation of Nemopilema nomurai and Cyanea nozakii Nematocyst Venoms’ Lytic Activity Using Mass Spectrometry and Zymography

Yue

et al. 2017

Toxins

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Background: Medusozoans utilize explosively discharging penetrant nematocysts to inject venom into prey. These venoms are composed of highly complex proteins and peptides with extensive bioactivities, as observed in vitro. Diverse enzymatic toxins have been putatively identified in the venom of jellyfish, Nemopilema nomurai and Cyanea nozakii, through examination of their proteomes and transcriptomes. However, functional examination of putative enzymatic components identified in proteomic approaches to elucidate potential bioactivities is critically needed. Methods: In this study, enzymatic toxins were functionally identified using a combined approach consisting of in gel zymography and liquid chromatography tandem mass spectrometry (LC-MS/MS). The potential roles of metalloproteinases and lipases in hemolytic activity were explored using specific inhibitors. Results: Zymography indicated that nematocyst venom possessed protease-, lipase- and hyaluronidase-class activities. Further, proteomic approaches using LC-MS/MS indicated sequence homology of proteolytic bands observed in zymography to extant zinc metalloproteinase-disintegrins and astacin metalloproteinases. Moreover, pre-incubation of the metalloproteinase inhibitor batimastat with N. nomurai nematocyst venom resulted in an approximate 62% reduction of hemolysis compared to venom exposed sheep erythrocytes, suggesting that metalloproteinases contribute to hemolytic activity. Additionally, species within the molecular mass range of 14–18 kDa exhibited both egg yolk and erythrocyte lytic activities in gel overlay assays. Conclusion: For the first time, our findings demonstrate the contribution of jellyfish venom metalloproteinase and suggest the involvement of lipase species to hemolytic activity. Investigations of this relationship will facilitate a better understanding of the constituents and toxicity of jellyfish venom.

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Characterising the enzymatic profile of crude tentacle extracts from the South Atlantic jellyfish Olindias sambaquiensis (Cnidaria: Hydrozoa)

Cited by 29 publications

References 49 publications

Composition and biological activities of the aqueous extracts of three scleractinian corals from the Mexican Caribbean: Pseudodiploria strigosa, Porites astreoides and Siderastrea siderea

Composition and biological activities of the aqueous extracts of three scleractinian corals from the Mexican Caribbean: Pseudodiploria strigosa, Porites astreoides and Siderastrea siderea

Insights into the Mechanisms Involved in Strong Hemorrhage and Dermonecrosis Induced by Atroxlysin-Ia, a PI-Class Snake Venom Metalloproteinase

Functional Elucidation of Nemopilema nomurai and Cyanea nozakii Nematocyst Venoms’ Lytic Activity Using Mass Spectrometry and Zymography

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