Wed, Nov 4, 2026 2:00 PM - 3:00 PM GMT
Welcome to the Biochemistry Focus webinar series, organised by the Biochemical Society and Portland Press.
Pore-forming toxins disrupt cellular membranes by assembling into oligomeric transmembrane complexes. Among them, actinoporins, a family of α-pore-forming toxins from cnidarians, have emerged as a powerful model for studying protein-lipid interactions during pore formation. These small proteins specifically target sphingomyelin-containing membranes, with cholesterol further enhancing their activity. Recent structural evidence demonstrates that lipids are not merely passive substrates but serve as integral structural components of the pore itself.
In this webinar, Dr Šolinc will present recent findings on the actinoporin-like protein Fav from the coral Orbicella faveolata. Their data reveals that funnel-shaped pores are associated with numerous lipids, particularly in the upper membrane leaflet, where up to 15 lipids per subunit can be resolved. These lipids play different roles, from initial membrane binding to structural lipids positioned between protomers that stabilise the oligomeric assembly. By varying lipid composition, they isolated pores with different stoichiometries, all sharing a conserved protomer fold and lipid arrangement, demonstrating that membrane thickness and lipid composition directly influence pore stoichiometry.
Don’t miss the chance to discuss these results in the broader context of actinoporin research, including recent high-resolution structures of FraC and StnII pores, the molecular basis of sphingomyelin specificity driven by hydrogen bonding and cation–π interactions, and the emerging view that actinoporin pores are best understood as protein–lipid complexes rather than purely proteinaceous assemblies.
Invited Speaker:
- Dr Gašper Šolinc, National Institute of Chemistry, Slovenia
