RT Journal Article
T1 Functional and Structural Variation amongSticholysins, Pore-Forming Proteins from the SeaAnemone Stichodactyla helianthus
A1 Rivera de la Torre, Esperanza
A1 Palacios Ortega, Juan
A1 Slotte, J. Peter
A1 Gavilanes, José G.
A1 Martínez del Pozo, Álvaro
A1 García Linares, Sara
AB Venoms constitute complex mixtures of many different molecules arising from evolution in processes driven by continuous prey–predator interactions. One of the most common compounds in these venomous cocktails are pore-forming proteins, a family of toxins whose activity relies on the disruption of the plasmatic membranes by forming pores. The venom of sea anemones, belonging to the oldest lineage of venomous animals, contains a large amount of a characteristic group of pore-forming proteins known as actinoporins. They bind specifically to sphingomyelin-containing membranes and suffer a conformational metamorphosis that drives them to make pores. This event usually leads cells to death by osmotic shock. Sticholysins are the actinoporins produced by Stichodactyla helianthus. Three different isotoxins are known: Sticholysins I, II, and III. They share very similar amino acid sequence and three-dimensional structure but display different behavior in terms of lytic activity and ability to interact with cholesterol, an important lipid component of vertebrate membranes. In addition, sticholysins can act in synergy when exerting their toxin action. The subtle, but important, molecular nuances that explain their different behavior are described and discussed throughout the text. Improving our knowledge about sticholysins behavior is important for eventually developing them into biotechnological tools.
PB MDPI
SN 1661-6596
YR 2020
FD 2020-11
LK https://hdl.handle.net/20.500.14352/6579
UL https://hdl.handle.net/20.500.14352/6579
LA eng
NO UCM-Banco Santander
DS Docta Complutense
RD 1 may 2024