Journals / Natural and Engineering Sciences / 2021 / Cilt: 6 - Sayı: 1

Tetrodotoxin binding protein in the marine puffer fish

Pages
39–52
Publication Date
2021-01-25
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

This protein is discovered to be a dimeric glycoprotein and formed a non-covalent dimer.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Marine pufferfish generally involve a potent neurotoxin, tetrodotoxin (TTX), which might be the leading cause for many human intoxications.
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Key Findings & Data:It blocks nervous impulses’ conduction along nerve fibers and axons during the act, and the LD50 for the mouse is 10 nanograms.
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Conclusion & Impact:This protein is discovered to be a dimeric glycoprotein and formed a non-covalent dimer.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:pufferfish · tetrodotoxin (TTX) · TTX-binding protein

Abstract

Marine pufferfish generally involve a potent neurotoxin, tetrodotoxin (TTX), which might be the leading cause for many human intoxications. It blocks nervous impulses’ conduction along nerve fibers and axons during the act, and the LD50 for the mouse is 10 nanograms. Being much larger than the sodium ion, TTX acts as a cork of a bottle, prevents sodium from flowing until it diffuses slowly. The TTX expanse appears to be species-specific in pufferfish bodies. The toxin is thought to bioaccumulate via the marine food based on the observations that marine pufferfishes that are cultured are not toxic, and non-toxic cultured pufferfishes become toxic when they feed on TTX-containing artificial diets. TTX-bearing animals show incredibly high resistance to TTX, and therefore TTX presumably retains or accumulates as a biological defense substance. These animals carrying TTX can accumulate toxins in their bodies despite not killing themselves is an object of interest. Fort his reason, and it is argued that TTX is wrapped in a particular protein and does not bind directly to the target's side-sodium channel, and therefore does not induce intoxication. The pufferfish TTX-binding protein (PSTBP) was first isolated as a potential TTX-carrier protein from the plasma of the marine pufferfish Takifugu niphobles. This protein is discovered to be a dimeric glycoprotein and formed a non-covalent dimer.

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Cite This Article

TOKUR, B., KORKMAZ, K. (2021). Tetrodotoxin binding protein in the marine puffer fish. Natural and Engineering Sciences, Cilt: 6 - Sayı: 1, 39–52. https://ajindex.com/articles/793155

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References (11)

  1. Akbora, H. D., Kunter, İ., Erçeti̇n, T., Elagöz, A. M., & Çi̇çek, B. A. (2020). Determination of tetrodotoxin (TTX) levels in various tissues of the silver cheeked puffer fish (Lagocephalus sceleratus (Gmelin, 1789)) in Northern Cyprus Sea (Eastern Mediterranean). Toxicon, 175, 1-6.
  2. Arakawa, K. (2001). Resistibility against TTX and PSP. In: Studies on the Toxicity of a Japanese Newt Cynops pyrrhogaster, Doctoral thesis, Nagasaki University, Nagasaki, pp. 50– 53. Arakawa, O., Nishio, S., Noguchi, T., Shida, Y., Onoue, Y. (1995). A new saxitoxin analogue from a xanthid crab Atergatis floridus. Toxicon 33, 1577–1584.
  3. Bane, V., M. Lehane, M. Dikshit, A. O'Riordan, and A. Furey. (2014). Tetrodotoxin: Chemistry, toxicity, source, distribution and detection. Toxins, 6: 693-755.
  4. Chau, R.; Kalaitzis, J.A.; Neilan, B.A. On the origins and biosynthesis of tetrodotoxin. Aquatic Toxicology, 2011, 104, 61–72.
  5. Fournier, T., Medjoubi-N, N., & Porquet, D. (2000). Alpha-1-acid glycoprotein. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 1482(1-2), 157-171.
  6. Fuchi, Y., Tsubone, N., Morisaki, S., Mizokoshi, T., Shuto, M., Fujii, M., Yamada, K., Hayashi, K. (1986).
  7. A survey on toxicity of pufferfishes, Fugu rubripes rubripes (torafugu) and Fugu rubripes chinensis (karasu). Journal of the Food Hygienic Society of Japan, 27, 569–572.
  8. Gao, W., Kanahara, Y., Tatsuno, R., Soyano, K., Nishihara, G.N., Urata, C., Takatani, T., Arakawa, O. (2018). Maturation-associated changes in internal distribution and intra-ovarian microdistribution of tetrodotoxin in the pufferfish Takifugu pardalis. Fisheries Science, 84, 723–732.
  9. Gao, W., Kanahara, Y., Yamada, M., Tatsuno, R., Yoshikawa, H., Doi, H., Takatani, T., Arakawa, O. (2019). Contrasting toxin selectivity between the marine pufferfish Takifugu pardalis and the freshwater pufferfish Pao suvattii. Toxins, 11, 470. Gao, W., Yamada, M., Ohki, R., Nagashima, Y., Tatsuno, R., Ikeda, K.,. & Arakawa, O. (2020). Evaluation of the tetrodotoxin uptake ability of pufferfish Takifugu rubripes tissues according to age using an in vitro tissue slice incubation method. Toxicon, 174, 8-12.
  10. Geffeney, S. L., E. Fujimoto, E. D. III Brodie, E. D. Jr. Brodie, and P.C. Ruben. (2005). Evolutionary diversification of TTX-resistant sodium channels in a predator-prey interaction. Nature, 434: 759–763.
  11. Halstead, B.W., (1988). Poisonous and Venomous Marine Animals of the World, second ed. The Darwin Press Inc., Princeton, pp. 525–