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Jellyfish venom is a complex mixture of bioactive proteins and peptides stored in specialized stinging cells called nematocytes (Jouiaei et al., 2015). These toxins, which include pore-forming proteins (porins), phospholipases, and neurotoxins, function synergistically to immobilize prey and defend against predators by inducing rapid cellular lysis and systemic toxicity (Yanagihara & Shohet, 2012). In humans, exposure to jellyfish venom can lead to severe clinical conditions such as the Irukandji syndrome, characterized by extreme pain and hypertension, or fatal cardiac arrest in the case of certain box jellyfish species (Tibballs, 2006). While the venom itself is not a traditional therapeutic target, it is the primary target for antivenom therapy and serves as a rich source of molecular templates for drug discovery, particularly in the fields of analgesia and oncology. Pharmacological management focuses on neutralizing the venom components using specific antibodies or mitigating the physiological consequences of the toxins, such as ion imbalance and inflammatory responses (Cegolon et al., 2013). The rapid onset of action and the diversity of toxins within the venom present significant challenges for clinical intervention and the development of universal treatments.
Antivenoms provide passive immunity by using antibodies to bind and neutralize venom proteins, preventing their interaction with host cell membranes (Tibballs, 2006). Other treatments like zinc gluconate may inhibit the pore-forming activity of specific toxins (Yanagihara & Shohet, 2012).
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