Functional and structural variation among sticholysins, pore-forming proteins from the sea anemone stichodactyla helianthus

Esperanza Rivera de Torre, Juan Palacios-Ortega, J. Peter Slotte, José G. Gavilanes, Álvaro Martínez-Del-pozo, Sara García-Linares*

*Corresponding author for this work

Research output: Contribution to journalReviewpeer-review

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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.
Original languageEnglish
Article number8915
JournalInternational Journal of Molecular Sciences
Issue number23
Number of pages24
Publication statusPublished - 2020


  • Actinoporins
  • Cholesterol
  • Cnidaria
  • Leakage
  • Sphingomyelin
  • Venom


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