A novel, non-invasive cnidarian venom extraction device

IF 2.8 Q2 TOXICOLOGY
Toxicon: X Pub Date : 2026-03-01 Epub Date: 2026-01-16 DOI:10.1016/j.toxcx.2025.100240
Phillip J. Robinson , Steven A. Trim , Carol M. Trim
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引用次数: 0

Abstract

Cnidaria represent one of the most ancient venomous lineages with thousands of extant species and their toxins have long been known to signify a source of therapeutic potential. Despite this recognition, cnidarian toxin research has progressed relatively slowly when compared to other taxa. One of the major factors for this slow development pertains to the difficulties involved with obtaining samples, particularly from benthic species which are sessile, where dissected tissues have historically been required. Additionally, the instability of marine venoms has further hindered progression of cnidarian venom research. The research presented aimed to address these issues through the design and development of a novel, non-invasive, venom extraction device that works on a range of cnidarian species. The device functioned underwater at depths ranging from 50 mm down to 5 m whilst scuba diving and was able to successfully obtain venom samples from all 12 species tested. These species were from three taxonomic groups Actiniaria (sea anemones), Scleractinia (corals) and Scyphozoan (Jellyfish) with four species from each. These venom samples revealed the expected phospholipase A2 activity but also the four Scleractinia venoms demonstrated phospholipase A2 inhibitory properties. This is the first description of phospholipase A2 inhibitory activity in cnidarian venoms and further work is required for full characterisation.
一种新型的非侵入性刺胞细胞毒液提取装置
刺胞菌是最古老的有毒谱系之一,有数千种现存物种,它们的毒素长期以来被认为是治疗潜力的来源。尽管认识到这一点,但与其他分类群相比,刺胞毒素的研究进展相对缓慢。造成这种缓慢发展的一个主要因素与获取样本的困难有关,特别是从无底栖生物物种中获取样本的困难,在这些物种中,历史上需要解剖组织。此外,海洋毒液的不稳定性进一步阻碍了刺胞动物毒液研究的进展。该研究旨在通过设计和开发一种新的、非侵入性的毒液提取装置来解决这些问题,该装置适用于一系列刺胞动物物种。该设备在水下50毫米到5米的深度范围内工作,并且能够成功地从所有12种测试物种中获取毒液样本。这些物种分别来自海葵、珊瑚和水母三个分类类群,每个类群各有4种。这些毒液样品显示了预期的磷脂酶A2活性,但四种巩膜菌毒液也显示了磷脂酶A2的抑制特性。这是对刺胞动物毒液中磷脂酶A2抑制活性的首次描述,需要进一步的工作来充分表征。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Toxicon: X
Toxicon: X Pharmacology, Toxicology and Pharmaceutics-Toxicology
CiteScore
6.50
自引率
0.00%
发文量
33
审稿时长
14 weeks
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