Over het archief
Het OWA, het open archief van het Waterbouwkundig Laboratorium heeft tot doel alle vrij toegankelijke onderzoeksresultaten van dit instituut in digitale vorm aan te bieden. Op die manier wil het de zichtbaarheid, verspreiding en gebruik van deze onderzoeksresultaten, alsook de wetenschappelijke communicatie maximaal bevorderen.
Dit archief wordt uitgebouwd en beheerd volgens de principes van de Open Access Movement, en het daaruit ontstane Open Archives Initiative.
Basisinformatie over ‘Open Access to scholarly information'.
| one publication added to basket [338045] |
New insights into the type II toxins from the sea anemone Heteractis crispa
Kalina, R.S.; Peigneur, S.; Zelepuga, E.A.; Dmitrenok, P.S.; Kvetkina, A.N.; Kim, N.Y.; Leychenko, E.V.; Tytgat, J.; Kozlovskaya, E.P.; Monastyrnaya, M.M.; Gladkikh, I.N. (2020). New insights into the type II toxins from the sea anemone Heteractis crispa. Toxins 12(1): 44. https://hdl.handle.net/10.3390/toxins12010044
In: Toxins. Multidisciplinary Digital Publishing Institute (MDPI): Basel. e-ISSN 2072-6651, meer
|   |
| Trefwoorden |
Radianthus crispa (Hemprich & Ehrenberg in Ehrenberg, 1834) [WoRMS]
Marien/Kust |
| Author keywords |
sea anemone; type II toxins; voltage-gated sodium channels; electrophysiology |
| Auteurs | | Top |
- Kalina, R.S.
- Peigneur, S., meer
- Zelepuga, E.A.
- Dmitrenok, P.S.
|
- Kvetkina, A.N.
- Kim, N.Y.
- Leychenko, E.V.
- Tytgat, J., meer
|
- Kozlovskaya, E.P.
- Monastyrnaya, M.M.
- Gladkikh, I.N.
|
| Abstract |
Toxins modulating NaV channels are the most abundant and studied peptide components of sea anemone venom. Three type-II toxins, δ-SHTX-Hcr1f (= RpII), RTX-III, and RTX-VI, were isolated from the sea anemone Heteractis crispa. RTX-VI has been found to be an unusual analog of RTX-III. The electrophysiological effects of Heteractis toxins on nine NaV subtypes were investigated for the first time. Heteractis toxins mainly affect the inactivation of the mammalian NaV channels expressed in the central nervous system (NaV1.1–NaV1.3, NaV1.6) as well as insect and arachnid channels (BgNaV1, VdNaV1). The absence of Arg13 in the RTX-VI structure does not prevent toxin binding with the channel but it has changed its pharmacological profile and potency. According to computer modeling data, the δ-SHTX-Hcr1f binds within the extracellular region of the rNaV1.2 voltage-sensing domain IV and pore-forming domain I through a network of strong interactions, and an additional fixation of the toxin at the channel binding site is carried out through the phospholipid environment. Our data suggest that Heteractis toxins could be used as molecular tools for NaV channel studies or insecticides rather than as pharmacological agents. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
