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Toxins (Basel)
2013 Dec 06;512:2420-33. doi: 10.3390/toxins5122420.
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Preliminary results of the in vivo and in vitro characterization of a tentacle venom fraction from the jellyfish Aurelia aurita.
Ponce D
,
López-Vera E
,
Aguilar MB
,
Sánchez-Rodríguez J
.
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The neurotoxic effects produced by a tentacle venom extract and a fraction were analyzed and correlated by in vivo and in vitro approaches. The tentacle venom extract exhibited a wide range of protein components (from 24 to >225 kDa) and produced tetanic reactions, flaccid paralysis, and death when injected into crabs. Two chromatography fractions also produced uncontrolled appendix movements and leg stretching. Further electrophysiological characterization demonstrated that one of these fractions potently inhibited ACh-elicited currents mediated by both vertebrate fetal and adult muscle nicotinic acetylcholine receptors (nAChR) subtypes. Receptor inhibition was concentration-dependent and completely reversible. The calculated IC(50) values were 1.77 μg/μL for fetal and 2.28 μg/μL for adult muscle nAChRs. The bioactive fraction was composed of a major protein component at ~90 kDa and lacked phospholipase A activity. This work represents the first insight into the interaction of jellyfish venom components and muscle nicotinic receptors.
Figure 1. Micrograph of A. aurita nematocysts along fishing tentacles. Atrichous ishorizas (white arrow) measured 6 × 4 µm wide and presented a disperse distribution along the tentacle tissue. Heterotrichous microbasic euryteles (black arrow) were approximately 12 × 9 µm wide and were arranged in clusters. 400× magnification, bar = 50 µm.
Figure 2. Protein content and fractionation of A. aurita TVE. (A) SDS-PAGE protein profile of TVE was performed in 12% polyacrylamide gel stained with Coomassie brilliant blue R-250. M indicates molecular mass standards (Amersham Rainbow Marker high-range, GE Healthcare); Lane 1 corresponds to 20 μg total protein of TVE. (B) Chromatogram of TVE fractionation by C18 reversed-phase column using a gradient of solution B from 5% to 95% (dashed line) at a flow rate of 1 mL/min over 60 min; Baseline indicated with a thin line. (C) SDS-PAGE protein profile of chromatography fractions. Analysis was performed in 10% polyacrylamide gels stained with Coomassie brilliant blue R-250. M indicates molecular mass standards (Kaleidoscope, Bio-Rad); Lanes 1–10 correspond to the eluted peaks equally labeled from HPLC fractionation.
Figure 3. Activity of fraction 4 on fetal muscle nAChR expressed in X. laevis oocytes. Concentration-response effects can be compared through the various panels. Arrows indicate the first current elicited after the 5 min static bath of toxin equilibration. Control membrane depolarisations elicited by 1–5 μM ACh pulses are indicated as 10% of total value (nA); (A) 1.5 μg total protein of fraction 4 inhibited 25% of ACh-elicited currents; (B) 3 μg total protein of fraction 4 blocked 50% of ACh currents; (C) 4.5 μg total protein of fraction 4 caused 96% blocking effect.
Figure 4. Concentration-response curves for fraction 4 on the adult (up-triangle) and fetal (down-triangle) subtypes of mouse muscle nAChR. Curves were generated by plotting current amplitude after toxin application as a percentage of current amplitude prior to toxin application (% response). Each data point represents the average value ± S.E. of the responses from three oocytes.
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