New sea anemone toxin RTX-VI selectively modulates voltage-gated sodium channels
Kalina, R.S.; Peigneur, S.; Gladkikh, I.N.; Dmitrenok, P.S.; Kim, N.Y.; Leychenko, E.V.; Monastyrnaya, M.M.; Tytgat, J.; Kozlovskaya, E.P. (2020). New sea anemone toxin RTX-VI selectively modulates voltage-gated sodium channels. Doklady Biochemistry and Biophysics 495(1): 292-295. https://hdl.handle.net/10.1134/S1607672920060071
In: Doklady Biochemistry and Biophysics. MAIK NAUKA/INTERPERIODICA/SPRINGER: New York. ISSN 1607-6729; e-ISSN 1608-3091, meer
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| Trefwoorden |
Radianthus crispa (Hemprich & Ehrenberg in Ehrenberg, 1834) [WoRMS]
Marien/Kust |
| Author keywords |
sea anemone; Heteractis crispa; voltage-gated sodium channels; toxins; electrophysiology |
| Auteurs | | Top |
- Kalina, R.S.
- Peigneur, S., meer
- Gladkikh, I.N.
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- Dmitrenok, P.S.
- Kim, N.Y.
- Leychenko, E.V.
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- Monastyrnaya, M.M.
- Tytgat, J., meer
- Kozlovskaya, E.P.
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| Abstract |
A new neurotoxin RTX-VI that modulates the voltage-gated sodium channels (NaV) was isolated from the ethanolic extract of the sea anemone Heteractis crispa. Its amino acid sequence was determined using the combination of Edman degradation and tandem mass spectrometry. RTX-VI turned out to be an unusual natural analogue of the previously described sea anemone toxin RTX-III. The RTX-VI molecule consists of two disulfide-linked peptide chains and is devoid of Arg13, which is important for the selectivity and affinity of such peptides for the NaV channels. Electrophysiological screening of RTV-VI on NaV channel subtypes showed its selective interaction with the central nervous system (NaV1.2, NaV1.6) and insect (BgNaV1, VdNaV1) sodium channels. |
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