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从 中鉴定出一种新的河豚毒素结合蛋白,过氧化物还原酶 1。

Molecular Characterization of a New Tetrodotoxin-Binding Protein, Peroxiredoxin-1, from .

机构信息

Fisheries Research Institute of Fujian, Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Xiamen 361013, China.

College of Life Sciences, Fujian Normal University, Fuzhou 350108, China.

出版信息

Int J Mol Sci. 2022 Mar 12;23(6):3071. doi: 10.3390/ijms23063071.

DOI:10.3390/ijms23063071
PMID:35328490
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8954737/
Abstract

Pufferfish are considered a culinary delicacy but require careful preparation to avoid ingestion of the highly toxic tetrodotoxin (TTX), which accumulates in certain tissues. In this study, the tissue distribution of peroxiredoxin-1 from was investigated. The peroxiredoxin-1 protein was obtained by in vitro recombinant expression and purification. The recombinant protein had a strong ability to scavenge hydroxyl radicals, protect superhelical DNA plasmids from oxidative damage, and protect L929 cells from HO toxicity through in vitro antioxidant activity. In addition, we verified its ability to bind to tetrodotoxin using surface plasmon resonance techniques. Further, recombinant proteins were found to facilitate the entry of tetrodotoxin into cells. Through these analyses, we identified, for the first time, peroxiredoxin-1 protein from as a potential novel tetrodotoxin-binding protein. Our findings provide a basis for further exploration of the application of peroxiredoxin-1 protein and the molecular mechanisms of tetrodotoxin enrichment in pufferfish.

摘要

河豚鱼被认为是一种美食,但需要小心准备,以避免摄入高度毒性的河豚毒素(TTX),TTX 会在某些组织中积累。在这项研究中,研究了来自 的过氧化物酶-1 的组织分布。过氧化物酶-1 蛋白通过体外重组表达和纯化获得。该重组蛋白具有很强的清除羟自由基的能力,能够保护超螺旋 DNA 质粒免受氧化损伤,并通过体外抗氧化活性保护 L929 细胞免受 HO 毒性。此外,我们使用表面等离子体共振技术验证了其与河豚毒素结合的能力。此外,还发现重组蛋白有助于河豚毒素进入细胞。通过这些分析,我们首次鉴定出 中的过氧化物酶-1 蛋白是一种潜在的新型河豚毒素结合蛋白。我们的研究结果为进一步探索过氧化物酶-1 蛋白的应用和河豚鱼中河豚毒素富集的分子机制提供了依据。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/9e93d05ef818/ijms-23-03071-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/71e18e76ba72/ijms-23-03071-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/dc62a8ebec87/ijms-23-03071-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/052a352c74e1/ijms-23-03071-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/897d162d235d/ijms-23-03071-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/ea926fe61434/ijms-23-03071-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/0c8d71b359f6/ijms-23-03071-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/bc9a303b1967/ijms-23-03071-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/c56694d821f1/ijms-23-03071-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/9e93d05ef818/ijms-23-03071-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/71e18e76ba72/ijms-23-03071-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/dc62a8ebec87/ijms-23-03071-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/052a352c74e1/ijms-23-03071-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/897d162d235d/ijms-23-03071-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/ea926fe61434/ijms-23-03071-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/0c8d71b359f6/ijms-23-03071-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/bc9a303b1967/ijms-23-03071-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/c56694d821f1/ijms-23-03071-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff1e/8954737/9e93d05ef818/ijms-23-03071-g009.jpg

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