Lipid interactions of an actinoporin pore-forming oligomer.
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
20 04 2021
20 04 2021
Historique:
received:
02
10
2020
revised:
16
01
2021
accepted:
11
02
2021
pubmed:
23
2
2021
medline:
1
6
2021
entrez:
22
2
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33617834
pii: S0006-3495(21)00152-1
doi: 10.1016/j.bpj.2021.02.015
pmc: PMC8105734
pii:
doi:
Substances chimiques
Lipid Bilayers
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1357-1366Subventions
Organisme : NIMHD NIH HHS
ID : G12 MD007603
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103712
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM116961
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM117146
Pays : United States
Informations de copyright
Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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