2021•Natural and Engineering SciencesOpen access

Tetrodotoxin binding protein in the marine puffer fish

Bahar Tokur, Koray Korkmaz

Open full text 4 citations

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.

Open-access reader

About this research paper

What this paper is about

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.

Why it matters

OpenAlex reports 4 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available 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.

Key concepts: Tetrodotoxin, Sodium channel, Neurotoxin, Toxin, Chemistry, Biophysics, Sodium, Cell biology

Related papers

Back to paper searchBrowse research topicsOriginal source
Tetrodotoxin binding protein in the marine puffer fish — Research Paper | ScholarLens