The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface
Actinoporins are α-pore forming proteins with therapeutic potential, produced by sea anemones. Sticholysin II (StnII) from Stichodactyla helianthus is one of its most extensively characterized members. These proteins remain stably folded in water, but upon interaction with lipid bilayers, they oligo...
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| Format: | Article |
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MDPI AG
2015-03-01
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| Series: | Marine Drugs |
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| Online Access: | http://www.mdpi.com/1660-3397/13/4/1647 |
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| author | Sara García-Linares Ida Alm Terhi Maula José G. Gavilanes Johan Peter Slotte Álvaro Martínez-del-Pozo |
| author_facet | Sara García-Linares Ida Alm Terhi Maula José G. Gavilanes Johan Peter Slotte Álvaro Martínez-del-Pozo |
| author_sort | Sara García-Linares |
| collection | DOAJ |
| description | Actinoporins are α-pore forming proteins with therapeutic potential, produced by sea anemones. Sticholysin II (StnII) from Stichodactyla helianthus is one of its most extensively characterized members. These proteins remain stably folded in water, but upon interaction with lipid bilayers, they oligomerize to form a pore. This event is triggered by the presence of sphingomyelin (SM), but cholesterol (Chol) facilitates pore formation. Membrane attachment and pore formation require changes involving long-distance rearrangements of residues located at the protein-membrane interface. The influence of Chol on membrane recognition, oligomerization, and/or pore formation is now studied using StnII variants, which are characterized in terms of their ability to interact with model membranes in the presence or absence of Chol. The results obtained frame Chol not only as an important partner for SM for functional membrane recognition but also as a molecule which significantly reduces the structural requirements for the mentioned conformational rearrangements to occur. However, given that the DOPC:SM:Chol vesicles employed display phase coexistence and have domain boundaries, the observed effects could be also due to the presence of these different phases on the membrane. In addition, it is also shown that the Arg51 guanidinium group is strictly required for membrane recognition, independently of the presence of Chol. |
| first_indexed | 2024-04-11T11:54:38Z |
| format | Article |
| id | doaj.art-c6c27f765759470a8410fc4e8a84a2b2 |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-04-11T11:54:38Z |
| publishDate | 2015-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-c6c27f765759470a8410fc4e8a84a2b22022-12-22T04:25:12ZengMDPI AGMarine Drugs1660-33972015-03-011341647166510.3390/md13041647md13041647The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane InterfaceSara García-Linares0Ida Alm1Terhi Maula2José G. Gavilanes3Johan Peter Slotte4Álvaro Martínez-del-Pozo5Department of Biochemistry and Molecular Biology I, Complutense University, 28040 Madrid, SpainBiochemistry, Department of Biosciences, Åbo Akademi University, 20520 Turku, FinlandBiochemistry, Department of Biosciences, Åbo Akademi University, 20520 Turku, FinlandDepartment of Biochemistry and Molecular Biology I, Complutense University, 28040 Madrid, SpainBiochemistry, Department of Biosciences, Åbo Akademi University, 20520 Turku, FinlandDepartment of Biochemistry and Molecular Biology I, Complutense University, 28040 Madrid, SpainActinoporins are α-pore forming proteins with therapeutic potential, produced by sea anemones. Sticholysin II (StnII) from Stichodactyla helianthus is one of its most extensively characterized members. These proteins remain stably folded in water, but upon interaction with lipid bilayers, they oligomerize to form a pore. This event is triggered by the presence of sphingomyelin (SM), but cholesterol (Chol) facilitates pore formation. Membrane attachment and pore formation require changes involving long-distance rearrangements of residues located at the protein-membrane interface. The influence of Chol on membrane recognition, oligomerization, and/or pore formation is now studied using StnII variants, which are characterized in terms of their ability to interact with model membranes in the presence or absence of Chol. The results obtained frame Chol not only as an important partner for SM for functional membrane recognition but also as a molecule which significantly reduces the structural requirements for the mentioned conformational rearrangements to occur. However, given that the DOPC:SM:Chol vesicles employed display phase coexistence and have domain boundaries, the observed effects could be also due to the presence of these different phases on the membrane. In addition, it is also shown that the Arg51 guanidinium group is strictly required for membrane recognition, independently of the presence of Chol.http://www.mdpi.com/1660-3397/13/4/1647actinoporinequinatoxinsphingomyelinpore-forming toxinsphingomyelin |
| spellingShingle | Sara García-Linares Ida Alm Terhi Maula José G. Gavilanes Johan Peter Slotte Álvaro Martínez-del-Pozo The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface Marine Drugs actinoporin equinatoxin sphingomyelin pore-forming toxin sphingomyelin |
| title | The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface |
| title_full | The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface |
| title_fullStr | The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface |
| title_full_unstemmed | The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface |
| title_short | The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface |
| title_sort | effect of cholesterol on the long range network of interactions established among sea anemone sticholysin ii residues at the water membrane interface |
| topic | actinoporin equinatoxin sphingomyelin pore-forming toxin sphingomyelin |
| url | http://www.mdpi.com/1660-3397/13/4/1647 |
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