Journal article
Lipid interactions of an actinoporin pore-forming oligomer
Biophysical journal, v 120(8), pp 1357-1366
20 Apr 2021
PMID: 33617834
Abstract
The actinoporins are cytolytic toxins produced by sea anemones. Upon encountering a membrane, preferably containing sphingomyelin, they oligomerize and insert their N-terminal helix into the membrane, forming a pore. Whether sphingomyelin is specifically recognized by the protein or simply induces phase coexistence in the membrane has been debated. Here, we perform multi-microsecond molecular dynamics simulations of an octamer of fragaceatoxin C, a member of the actinoporin family, in lipid bilayers containing either pure 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) or a 1:1 mixture of DOPC and palmitoyl sphingomyelin (PSM). The complex is highly stable in both environments, with only slight fraying of the inserted helices near their N-termini. Analyzing the structural parameters of the mixed membrane in the course of the simulation, we see signs of a phase transition for PSM in the inner leaflet of the bilayer. In both leaflets, cross-interactions between lipids of different type decrease over time. Surprisingly, the aromatic loop thought to be responsible for sphingomyelin recognition interacts more with DOPC than PSM by the end of the simulation. These results support the notion that the key membrane property that actinoporins recognize is lipid phase coexistence.
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Details
- Title
- Lipid interactions of an actinoporin pore-forming oligomer
- Creators
- Aliasghar Sepehri - City College of New YorkBinod Nepal - City College of New YorkThemis Lazaridis - City College of New York
- Publication Details
- Biophysical journal, v 120(8), pp 1357-1366
- Publisher
- Elsevier
- Grant note
- G12 MD007603 / NIMHD NIH HHS R01 GM117146 / NIGMS NIH HHS P41 GM103712 / NIGMS NIH HHS R01 GM116961 / NIGMS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:000642100000010
- Scopus ID
- 2-s2.0-85101999725
- Other Identifier
- 991021955154504721
InCites Highlights
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- Web of Science research areas
- Biophysics