New Sea Anemone Toxin RTX-VI Selectively Modulates Voltage-Gated Sodium Channels

A new neurotoxin RTX-VI that modulates the voltage-gated sodium channels (Na V ) 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 u...

Full description

Saved in:
Bibliographic Details
Published inDoklady. Biochemistry and biophysics Vol. 495; no. 1; pp. 292 - 295
Main Authors 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.
Format Journal Article
LanguageEnglish
Published Moscow Pleiades Publishing 01.11.2020
Subjects
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Life Sciences
Molecular Biology
electrophysiology
sea anemone
voltage-gated sodium channels
toxins
Heteractis crispa
Online AccessGet full text

Cover

More Information
Summary:A new neurotoxin RTX-VI that modulates the voltage-gated sodium channels (Na V ) 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 Na V channels. Electrophysiological screening of RTV-VI on Na V channel subtypes showed its selective interaction with the central nervous system (Na V 1.2, Na V 1.6) and insect (BgNa V 1, VdNa V 1) sodium channels.
ISSN:1607-6729
1608-3091
DOI:10.1134/S1607672920060071