2018
DOI: 10.1371/journal.pone.0202981
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Dissecting the mechanism of action of actinoporins. Role of the N-terminal amphipathic α-helix in membrane binding and pore activity of sticholysins I and II

Abstract: Actinoporins sticholysin I and sticholysin II (St I, St II) are proposed to lyse model and biomembranes via toroidal pore formation by their N-terminal domain. Based on the hypothesis that peptide fragments can reproduce the structure and function of this domain, the behavior of peptides containing St I residues 12–31 (StI12-31), St II residues 11–30 (StII11-30), and its TOAC-labeled analogue (N-TOAC-StII11-30) was examined. Molecular modeling showed a good match with experimental structures, indicating amphip… Show more

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Cited by 17 publications
(10 citation statements)
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“…Upon interaction with a lipid membrane containing SM ( b ), their N-terminal α-helix stretch is detached and extended, shortly laying parallel to the membrane ( c ) [ 25 , 26 , 82 , 85 , 87 , 91 , 116 , 140 , 141 , 142 , 143 ]. Then, monomers oligomerize and insert this N-terminal α-helix, now about 30 residues long, within the hydrophobic membrane core ( d ) [ 34 , 144 , 145 , 146 , 147 , 148 , 149 ]. The existence of such an intermediate is one of the most controversial issues, depending on the degree of acceptance of the evidence about the real existence, or not, of pre-pore assemblies [ 132 , 133 , 150 ].…”
Section: Figurementioning
confidence: 99%
“…Upon interaction with a lipid membrane containing SM ( b ), their N-terminal α-helix stretch is detached and extended, shortly laying parallel to the membrane ( c ) [ 25 , 26 , 82 , 85 , 87 , 91 , 116 , 140 , 141 , 142 , 143 ]. Then, monomers oligomerize and insert this N-terminal α-helix, now about 30 residues long, within the hydrophobic membrane core ( d ) [ 34 , 144 , 145 , 146 , 147 , 148 , 149 ]. The existence of such an intermediate is one of the most controversial issues, depending on the degree of acceptance of the evidence about the real existence, or not, of pre-pore assemblies [ 132 , 133 , 150 ].…”
Section: Figurementioning
confidence: 99%
“…Early evidence pointed toward a trimeric or tetrameric oligomer forming toroidal pores (5,10,11), but more recent crystal structures of fragaceatoxin C in lipidic environments showed a nonameric prepore (12) and an octameric pore with the Nt helices forming a funnel-shaped pore (7). The Nt helices by themselves have some pore-forming activity that is similar to that of the entire toxin in the case of sticholysin (13,14), but lower in the case of equinatoxin II (15).…”
Section: Introductionmentioning
confidence: 99%
“…Estas toxinas apresentam apresentam grande semelhanças em suas sequências (93%, segundo de los Rios et al [17]) e atuam pela formação de poros em membranas, sendo o seu suposto receptor a esfingomielina (SM). Todavia, as diversas etapas de ligação à membrana, oligomerização e formação de poros não são completamente compreendidos no nível molecular [18].…”
Section: Efeito Das Toxinas Sti E Stii Em Guvs Contendo Lipídeos Não unclassified
“…St I e St II diferem em treze aminoácidos, dos quais apenas três resíduos não conservados estão localizados na região N-terminal. Como resultado, St II apresenta maior capacidade de interação com membranas (de los Rios et al [17] e Carretero et al [18] demonstram no caso de células sanguineas maior atividade hemolítica do STII do que St I). Portanto, nossos resultados sugerem que a estrutura da membrana determina a ação da toxina ST II na concentração estudada.…”
Section: Efeito Das Toxinas Sti E Stii Em Guvs Contendo Lipídeos Não unclassified
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