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Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents

  • Molecular Toxicology
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Abstract

In this work, a novel M-superfamily conotoxin, designated lt3a, was purified from the crude venom of Conus litteratus. Combined with peptide sequencing, MALDI-TOF mass spectrometry and cDNA cloning techniques, the amino acid sequence of lt3a was supposed to be DγCCγ OQWCDGACDCCS, where O is hydroxyproline and γ is carboxyglutamate. The Cys framework of lt3a (–CC–C–C–CC–) is similar to that of ψ-, μ-, κM-conotoxins, which are representatives of M-conotoxins. Peptide lt3a is categorized into M1 branch based on the number of residues in the last Cys loop. Whole cell patch-clamp study on adult rat dorsal root ganglion neurons indicated that lt3a could enhance tetrodotoxin-sensitive sodium currents. This is a previously unknown function of M-superfamily conotoxins.

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Acknowledgments

This work was supported by the State National High-Tech Development Program (863 Program) from the Ministry of Science and Technology of China (No. 2006AA090504 and No. 2008AA09Z401), National Natural Science Foundation of China (30871921), project of Guangdong Science-Tech Program (No. 2006A36501001), Guangdong Natural Science Foundation (8151027501000083). We thank Jingxing Ou of University of Aberdeen for his comments on this article.

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Correspondence to Anlong Xu.

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L. Wang and J. Liu contributed equally to this work.

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Wang, L., Liu, J., Pi, C. et al. Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents. Arch Toxicol 83, 925–932 (2009). https://doi.org/10.1007/s00204-009-0453-8

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  • DOI: https://doi.org/10.1007/s00204-009-0453-8

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