ArticleProtein science : a publication of the Protein Society2017
Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 28 citations in OpenAlex.
- Structural and functional analysis of Hydra Actinoporin-Like Toxin 1 (HALT-1).Scientific reports · 2021Article
- Panorama of the Intracellular Molecular Concert Orchestrated by Actinoporins, Pore-Forming Toxins from Sea Anemones.Toxins · 2021Review
- Membrane Remodeling by the Lytic Fragment of SticholysinII: Implications for the Toroidal Pore Model.Biophysical journal · 2019Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Article
- Multigene Family of Pore-Forming Toxins from Sea AnemoneMarine drugs · 2018Article
- Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation.Scientific reports · 2018Article
- Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone.Biophysical reviews · 2017Review
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12 authors at 4 institutions in 4 countries.
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Abstract
Crystallographic data of the dimeric and octameric forms of fragaceatoxin C (FraC) suggested the key role of a small hydrophobic protein-protein interaction surface for actinoporins oligomerization and pore formation in membranes. However, site-directed mutagenesis studies supporting this hypothesis for others actinoporins are still lacking. Here, we demonstrate that disrupting the key hydrophobic interaction between V60 and F163 (FraC numbering scheme) in the oligomerization interface of FraC, equinatoxin II (EqtII), and sticholysin II (StII) impairs the pore formation activity of these proteins. Our results allow for the extension of the importance of FraC protein-protein interactions in the stabilization of the oligomeric intermediates of StII and EqtII pointing out that all of these proteins follow a similar pathway of membrane disruption. These findings support the hybrid pore proposal as the universal model of actinoporins pore formation. Moreover, we reinforce the relevance of dimer formation, which appears to be a functional intermediate in the assembly pathway of some different pore-forming proteins.
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