Differential binding and activity of the pore-forming toxin sticholysin II in 
model membranes containing diverse ceramide-derived lipids

Soto, Carmen; Del Valle, Anaixis; Valiente, Pedro A.; Ros, Uris; Lanio, María E.; Hernández, Ana M.; Alvarez, Carlos

doi:10.1016/j.biochi.2017.04.003

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Differential binding and activity of the pore-forming toxin sticholysin II in model membranes containing diverse ceramide-derived lipids

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Soto, C., Del Valle, A., Valiente, P. A., Ros, U., Lanio, M. E., Hernández, A. M., et al. (2017). Differential binding and activity of the pore-forming toxin sticholysin II in model membranes containing diverse ceramide-derived lipids. Biochimie, 138, 20-31. doi:10.1016/j.biochi.2017.04.003.

Cite as: https://hdl.handle.net/21.11116/0000-000F-C4F9-B

Abstract

Sticholysin II is a pore-forming toxin produced by the sea anemone Stichodactyla helianthus that belongs to the actinoporin protein family. The high affinity of actinoporins for sphingomyelin (SM)-containing membranes has been well documented. However, the molecular determinants that define this affinity have not been fully clarified. Here, we have examined the binding and permeabilizing activity of StII to different single and mixed lipidic systems by combining lipid monolayers, liposomes, and permeabilizing assays. This study characterizes the contribution of ceramide-derived compounds for StII-membrane interaction. Molecular dynamics simulations revealed a differential binding mode of StII with the polar head group of SM and PC. The electrostatic interaction energies were the major energetic contributors to the better affinity of StII for SM compared to PC, while the van der Waals interaction energies were the major driving forces of the better affinity of StII for SM respect to Cer. Furthermore, the presence of sugar residues in glycosphingolipids modulated binding and pore-formation by actinoporins probably by hindering StII to reach relevant structural motifs in membrane for binding or inducing a non-competent adsorption to membrane. Our results demonstrate that StII-membrane interaction, leading to pore formation, may critically respond to changes in lipid head group properties, and the access to SM interfacial structural motif.