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Volumn 278, Issue 12, 2011, Pages 2080-2089

Intrinsic local disorder and a network of charge-charge interactions are key to actinoporin membrane disruption and cytotoxicity

Author keywords

actinoporin; dynamics; electrostatic interactions; NMR structure; sticholysin

Indexed keywords

CYTOLYSIN; STICHOLYSIN II; UNCLASSIFIED DRUG;

EID: 79958156446     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08123.x     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 0026784112 scopus 로고
    • Polypeptide cytolytic toxins from sea anemones (Actiniaria)
    • Macek P, (1992) Polypeptide cytolytic toxins from sea anemones (Actiniaria). FEMS Microbiol Immunol 5, 121-129.
    • (1992) FEMS Microbiol Immunol , vol.5 , pp. 121-129
    • MacEk, P.1
  • 2
    • 0036027362 scopus 로고    scopus 로고
    • Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)
    • DOI 10.1016/S0041-0101(01)00191-X, PII S004101010100191X
    • Anderluh G, &, Macek P, (2002) Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria). Toxicon 40, 111-124. (Pubitemid 33016540)
    • (2002) Toxicon , vol.40 , Issue.2 , pp. 111-124
    • Anderluh, G.1    Macek, P.2
  • 3
    • 39349103788 scopus 로고    scopus 로고
    • Sea anemone actinoporins: The transition from a folded soluble state to a functionally active membrane-bound oligomeric pore
    • DOI 10.2174/138920307783018686
    • Alegre-Cebollada J, Oñaderra M, Gavilanes JG, &, Martínez-del-Pozo AM, (2007) Sea anemone actinoporins: the transition from a folded soluble state to a functionally active membrane-bound oligomeric pore. Curr Protein Pept Sci 8, 558-572. (Pubitemid 351266989)
    • (2007) Current Protein and Peptide Science , vol.8 , Issue.6 , pp. 558-572
    • Alegre-Cebollada, J.1    Onaderra, M.2    Gavilanes, J.G.3    Del Pozo, A.M.4
  • 4
    • 0242664967 scopus 로고    scopus 로고
    • Pore Formation by Equinatoxin II, a Eukaryotic Protein Toxin, Occurs by Induction of Nonlamellar Lipid Structures
    • DOI 10.1074/jbc.M305916200
    • Anderluh G, Dalla Serra M, Viero G, Guella G, Macek P, &, Menestrina G, (2003) Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures. J Biol Chem 278, 45216-45223. (Pubitemid 37432655)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45216-45223
    • Anderluh, G.1    Dalla Serra, M.2    Viero, G.3    Guella, G.4    Macek, P.5    Menestrina, G.6
  • 5
    • 77955868782 scopus 로고    scopus 로고
    • Molecular mechanism of sphingomyelin-specific membrane binding and pore formation by actinoporins
    • Bakrac B, &, Anderluh G, (2010) Molecular mechanism of sphingomyelin-specific membrane binding and pore formation by actinoporins. Adv Exp Med Biol 677, 106-115.
    • (2010) Adv Exp Med Biol , vol.677 , pp. 106-115
    • Bakrac, B.1    Anderluh, G.2
  • 6
    • 0242542032 scopus 로고    scopus 로고
    • Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
    • DOI 10.1016/j.str.2003.09.019
    • Mancheño JM, Martín-Benito J, Martínez-Ripoll M, Gavilanes JG, &, Hermoso JA, (2003) Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation. Structure 11, 1319-1328. (Pubitemid 37412414)
    • (2003) Structure , vol.11 , Issue.11 , pp. 1319-1328
    • Mancheno, J.M.1    Martin-Benito, J.2    Martinez-Ripoll, M.3    Gavilanes, J.G.4    Hermoso, J.A.5
  • 7
    • 0034880806 scopus 로고    scopus 로고
    • Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina
    • DOI 10.1016/S0969-2126(01)00592-5, PII S0969212601005925
    • Athanasiadis A, Anderluh G, Macek P, &, Turk D, (2001) Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina. Structure 9, 341-346. (Pubitemid 32772579)
    • (2001) Structure , vol.9 , Issue.4 , pp. 341-346
    • Athanasiadis, A.1    Anderluh, G.2    Macek, P.3    Turk, D.4
  • 8
    • 0036304122 scopus 로고    scopus 로고
    • Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: Implications for pore formation
    • DOI 10.1006/jmbi.2001.5321
    • Hinds MG, Zhang W, Anderluh G, Hansen PE, &, Norton RS, (2002) Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: implications for pore formation. J Mol Biol 315, 1219-1229. (Pubitemid 34729299)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.5 , pp. 1219-1229
    • Hinds, M.G.1    Zhang, W.2    Anderluh, G.3    Hansen, P.E.4    Norton, R.S.5
  • 12
    • 33845976310 scopus 로고    scopus 로고
    • The equinatoxin N-terminus is transferred across planar lipid membranes and helps to stabilize the transmembrane pore
    • DOI 10.1111/j.1742-4658.2006.05608.x
    • Kristan K, Viero G, Macek P, Dalla Serra M, &, Anderluh G, (2007) The equinatoxin N-terminus is transferred across planar lipid membranes and helps to stabilize the transmembrane pore. FEBS J 274, 539-550. (Pubitemid 46046661)
    • (2007) FEBS Journal , vol.274 , Issue.2 , pp. 539-550
    • Kristan, K.1    Viero, G.2    Macek, P.3    Dalla Serra, M.4    Anderluh, G.5
  • 15
    • 4544352455 scopus 로고    scopus 로고
    • Phenotypic selection and characterization of randomly produced non-haemolytic mutants of the toxic sea anemone protein sticholysin II
    • DOI 10.1016/j.febslet.2004.08.031, PII S0014579304010300
    • Alegre-Cebollada J, Lacadena V, Oñaderra M, Mancheño JM, Gavilanes JG, &, Martínez-del-Pozo AM, (2004) Phenotypic selection and characterization of randomly produced non-haemolytic mutants of the toxic sea anemone protein sticholysin II. FEBS Lett 575, 14-18. (Pubitemid 39237674)
    • (2004) FEBS Letters , vol.575 , Issue.1-3 , pp. 14-18
    • Alegre-Cebollada, J.1    Lacadena, V.2    Onaderra, M.3    Mancheno, J.M.4    Gavilanes, J.G.5    Del Pozo, A.M.6
  • 17
    • 77958474950 scopus 로고    scopus 로고
    • Actinoporins from the sea anemones, tropical Radianthus macrodactylus and northern Oulactis orientalis: Comparative analysis of structure-function relationships
    • Monastyrnaya M, Leychenko E, Isaeva M, Likhatskaya G, Zelepuga E, Kostina E, Trifonov E, Nurminski E, &, Kozlovskaya E, (2010) Actinoporins from the sea anemones, tropical Radianthus macrodactylus and northern Oulactis orientalis: comparative analysis of structure-function relationships. Toxicon 56, 1299-1314.
    • (2010) Toxicon , vol.56 , pp. 1299-1314
    • Monastyrnaya, M.1    Leychenko, E.2    Isaeva, M.3    Likhatskaya, G.4    Zelepuga, E.5    Kostina, E.6    Trifonov, E.7    Nurminski, E.8    Kozlovskaya, E.9
  • 18
    • 77958508102 scopus 로고    scopus 로고
    • Molecular characterization on the genome structure of hemolysin toxin isoforms isolated from sea anemone Actineria villosa and Phyllodiscus semoni
    • Uechi G, Toma H, Arakawa T, &, Sato Y, (2010) Molecular characterization on the genome structure of hemolysin toxin isoforms isolated from sea anemone Actineria villosa and Phyllodiscus semoni. Toxicon 56, 1470-1476.
    • (2010) Toxicon , vol.56 , pp. 1470-1476
    • Uechi, G.1    Toma, H.2    Arakawa, T.3    Sato, Y.4
  • 19
    • 0032999454 scopus 로고    scopus 로고
    • Sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus, is a monomer-tetramer associating protein
    • DOI 10.1016/S0014-5793(99)00846-7, PII S0014579399008467
    • de los Rios V, Mancheño JM, Martinez del Pozo A, Alfonso C, Rivas G, Oñaderra M, &, Gavilanes JG, (1999) Sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus, is a monomer-tetramer associating protein. FEBS Lett 455, 27-30. (Pubitemid 29322775)
    • (1999) FEBS Letters , vol.455 , Issue.1-2 , pp. 27-30
    • De Los Rios, V.1    Mancheno, J.M.2    Martinez Del Pozo, A.3    Alfonso, C.4    Rivas, G.5    Onaderra, M.6    Gavilanes, J.G.7
  • 20
    • 0032710610 scopus 로고    scopus 로고
    • Increased protein backbone conformational entropy upon hydrophobic ligand binding
    • Zidek L, Novotny MV, &, Stone MJ, (1999) Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nat Struct Biol 6, 1118-1121.
    • (1999) Nat Struct Biol , vol.6 , pp. 1118-1121
    • Zidek, L.1    Novotny, M.V.2    Stone, M.J.3
  • 21
    • 33846197988 scopus 로고    scopus 로고
    • Silent mutations at the 5′-end of the cDNA of actinoporins from the sea anemone Stichodactyla helianthus allow their heterologous overproduction in Escherichia coli
    • DOI 10.1016/j.jbiotec.2006.07.006, PII S016816560600592X
    • Alegre-Cebollada J, Clementi G, Cunietti M, Porres C, Oñaderra M, Gavilanes JG, &, Martínez del Pozo A, (2007) Silent mutations at the 5′-end of the cDNA of actinoporins from the sea anemone Stichodactyla helianthus allow their heterologous overproduction in Escherichia coli. J Biotechnol 127, 211-221. (Pubitemid 46107142)
    • (2007) Journal of Biotechnology , vol.127 , Issue.2 , pp. 211-221
    • Alegre-Cebollada, J.1    Clementi, G.2    Cunietti, M.3    Porres, C.4    Onaderra, M.5    Gavilanes, J.G.6    Pozo, A.M.D.7
  • 24
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco, CA.
    • Goddard TD, &, Kneller DG, (2005) SPARKY 3. University of California, San Francisco, CA.
    • (2005) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 25
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert P, (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278, 353-378.
    • (2004) Methods Mol Biol , vol.278 , pp. 353-378
    • Güntert, P.1
  • 26
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu G, Delaglio F, &, Bax A, (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13, 289-302. (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, &, Wüthrich K, (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14, 29-32.
    • (1996) J Mol Graph , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 32
    • 79958099694 scopus 로고    scopus 로고
    • Analytical Ultracentrifugation Facility, Bioservices Center, University of Connecticut, Storrs, CT.
    • Cole J, &, Lary J, (2009) HeteroAnalysis. Analytical Ultracentrifugation Facility, Bioservices Center, University of Connecticut, Storrs, CT.
    • (2009) HeteroAnalysis
    • Cole, J.1    Lary, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.