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Volumn 1798, Issue 2, 2010, Pages 244-251

Solid-state NMR study of membrane interactions of the pore-forming cytolysin, equinatoxin II

Author keywords

Equinatoxin II; Lipid domain; Membrane toxin; Phospholipid bilayer; Protein lipid interaction; Solid state NMR

Indexed keywords

CHOLESTEROL; DIMYRISTOYLPHOSPHATIDYLCHOLINE; EQUINATOXIN; EQUINATOXIN II; SPHINGOMYELIN; UNCLASSIFIED DRUG;

EID: 74249085736     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.10.012     Document Type: Article
Times cited : (23)

References (34)
  • 1
    • 0023895943 scopus 로고
    • Isolation and characterization of three lethal and hemolytic toxins from the sea anemone Actinia equina L
    • Maček P., and Lebez D. Isolation and characterization of three lethal and hemolytic toxins from the sea anemone Actinia equina L. Toxicon 26 (1988) 441-451
    • (1988) Toxicon , vol.26 , pp. 441-451
    • Maček, P.1    Lebez, D.2
  • 7
    • 0037379727 scopus 로고    scopus 로고
    • Effects of the eukaryotic pore-forming cytolysin equinatoxin II on lipid membranes and the role of sphingomyelin
    • Bonev B.B., Lam Y.H., Anderluh G., Watts A., Norton R.S., and Separovic F. Effects of the eukaryotic pore-forming cytolysin equinatoxin II on lipid membranes and the role of sphingomyelin. Biophys. J. 84 (2003) 2382-2392
    • (2003) Biophys. J. , vol.84 , pp. 2382-2392
    • Bonev, B.B.1    Lam, Y.H.2    Anderluh, G.3    Watts, A.4    Norton, R.S.5    Separovic, F.6
  • 8
    • 0242664967 scopus 로고    scopus 로고
    • Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures
    • Anderluh G., Dalla Serra M., Viero G., Guella G., Maček P., and Menestrina G. Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures. J. Biol. Chem. 278 (2003) 45216-45223
    • (2003) J. Biol. Chem. , vol.278 , pp. 45216-45223
    • Anderluh, G.1    Dalla Serra, M.2    Viero, G.3    Guella, G.4    Maček, P.5    Menestrina, G.6
  • 9
    • 0344443818 scopus 로고    scopus 로고
    • Solid-state NMR structure determination
    • Drechsler A., and Separovic F. Solid-state NMR structure determination. IUBMB Life 55 (2003) 515-523
    • (2003) IUBMB Life , vol.55 , pp. 515-523
    • Drechsler, A.1    Separovic, F.2
  • 10
    • 0026768029 scopus 로고
    • Melittin-induced changes in lipid multilayers. A solid-state NMR study
    • Smith R., Separovic F., Bennett F.C., and Cornell B.A. Melittin-induced changes in lipid multilayers. A solid-state NMR study. Biophys. J. 63 (1992) 469-474
    • (1992) Biophys. J. , vol.63 , pp. 469-474
    • Smith, R.1    Separovic, F.2    Bennett, F.C.3    Cornell, B.A.4
  • 11
    • 0029981549 scopus 로고    scopus 로고
    • Nuclear magnetic resonance investigation of hydrocarbon chain packing in bilayers of polyunsaturated phospholipids
    • Holte L.L., Separovic F., and Gawrisch K. Nuclear magnetic resonance investigation of hydrocarbon chain packing in bilayers of polyunsaturated phospholipids. Lipids 31 (1996) 199-203
    • (1996) Lipids , vol.31 , pp. 199-203
    • Holte, L.L.1    Separovic, F.2    Gawrisch, K.3
  • 12
    • 0021099797 scopus 로고
    • 31P nuclear magnetic resonance studies of the association of basic proteins with multilayers of diacyl phosphatidylserine
    • 31P nuclear magnetic resonance studies of the association of basic proteins with multilayers of diacyl phosphatidylserine. Biochim. Biophys. Acta 732 (1983) 492-498
    • (1983) Biochim. Biophys. Acta , vol.732 , pp. 492-498
    • Smith, R.1    Cornell, B.A.2    Keniry MA Separovic, F.3
  • 13
    • 47749109057 scopus 로고    scopus 로고
    • Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence
    • Schön P., García-Sáez A.J., Malovrh P., Bacia K., Anderluh G., and Schwille P. Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence. Biophys. J. 95 (2008) 691-698
    • (2008) Biophys. J. , vol.95 , pp. 691-698
    • Schön, P.1    García-Sáez, A.J.2    Malovrh, P.3    Bacia, K.4    Anderluh, G.5    Schwille, P.6
  • 15
    • 0014195281 scopus 로고
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
    • Shapiro A.L., Vinuela E., and Maizel J.V. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Res. Commun. 28 (1967) 815-820
    • (1967) Biochem. Biophys. Res. Commun. , vol.28 , pp. 815-820
    • Shapiro, A.L.1    Vinuela, E.2    Maizel, J.V.3
  • 16
    • 0000745176 scopus 로고
    • Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • Davis J.H., Jeffrey K.R., Bloom M., and Valic M.I. Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains. Chem. Phys. Lett. 42 (1976) 390-394
    • (1976) Chem. Phys. Lett. , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4
  • 17
    • 0017372433 scopus 로고
    • Orientation and flexibility of the choline head group in phosphatidylcholine bilayers
    • Seelig J., Gally G.U., and Wohlgemuth R. Orientation and flexibility of the choline head group in phosphatidylcholine bilayers. Biochim. Biophys. Acta 467 (1977) 109-119
    • (1977) Biochim. Biophys. Acta , vol.467 , pp. 109-119
    • Seelig, J.1    Gally, G.U.2    Wohlgemuth, R.3
  • 18
    • 0017902280 scopus 로고
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes. Biochim. Biophys. Acta 575 (1978) 105-140
    • (1978) Biochim. Biophys. Acta , vol.575 , pp. 105-140
    • Seelig, J.1
  • 19
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis P.R., and de Kruijff B. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta 559 (1979) 399-420
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    de Kruijff, B.2
  • 20
    • 17844376024 scopus 로고    scopus 로고
    • NMR methods for studying membrane-active antimicrobial peptides
    • Strandberg E., and Ulrich A.S. NMR methods for studying membrane-active antimicrobial peptides. Concepts Magn. Res. 23A (2004) 89-120
    • (2004) Concepts Magn. Res. , vol.23 A , pp. 89-120
    • Strandberg, E.1    Ulrich, A.S.2
  • 21
    • 0025965346 scopus 로고
    • Phosphorus-31 two-dimensional solid-state exchange NMR. Application to model membrane and biological systems
    • Fenske D.B., and Jarrell H.C. Phosphorus-31 two-dimensional solid-state exchange NMR. Application to model membrane and biological systems. Biophys. J. 59 (1991) 55-69
    • (1991) Biophys. J. , vol.59 , pp. 55-69
    • Fenske, D.B.1    Jarrell, H.C.2
  • 22
    • 0018982584 scopus 로고
    • Lipid conformation in model membranes
    • Seelig J., and Seelig A. Lipid conformation in model membranes. Quart. Rev. Biophys. 13 (1980) 19-61
    • (1980) Quart. Rev. Biophys. , vol.13 , pp. 19-61
    • Seelig, J.1    Seelig, A.2
  • 23
    • 0015213769 scopus 로고
    • Effects of cholesterol and cholesterol derivatives on hydrocarbon chain mobility in lipids
    • Oldfield E., and Chapman D. Effects of cholesterol and cholesterol derivatives on hydrocarbon chain mobility in lipids. Biochem. Biophys. Res. Commun. 43 (1971) 610-616
    • (1971) Biochem. Biophys. Res. Commun. , vol.43 , pp. 610-616
    • Oldfield, E.1    Chapman, D.2
  • 26
    • 0014221481 scopus 로고
    • The stability and structure of mixed lipid monolayers and bilayers. I. Properties of lipid and lipoprotein monolayers on OsO4 solutions and the role of cholesterol, retinol, and tocopherol in stabilizing lecithin monolayers
    • Dreher K.D., Schulman J.H., Anderson O.R., and Roels O.A. The stability and structure of mixed lipid monolayers and bilayers. I. Properties of lipid and lipoprotein monolayers on OsO4 solutions and the role of cholesterol, retinol, and tocopherol in stabilizing lecithin monolayers. J. Ultrastruct. Res. 19 (1967) 586-599
    • (1967) J. Ultrastruct. Res. , vol.19 , pp. 586-599
    • Dreher, K.D.1    Schulman, J.H.2    Anderson, O.R.3    Roels, O.A.4
  • 27
    • 33749445059 scopus 로고    scopus 로고
    • Domain-formation in DOPC/SM bilayers studied by pfg-NMR: Effect of sterol structure
    • Shahedi V., Orädd G., and Lindblom G. Domain-formation in DOPC/SM bilayers studied by pfg-NMR: Effect of sterol structure. Biophys. J. 91 (2006) 2501-2507
    • (2006) Biophys. J. , vol.91 , pp. 2501-2507
    • Shahedi, V.1    Orädd, G.2    Lindblom, G.3
  • 29
    • 0030069976 scopus 로고    scopus 로고
    • Comparative effects of cholesterol and cholesterol sulfate on hydration and ordering of dimyristoylphosphatidylcholine membranes
    • Faure C., Tranchant J.F., and Dufourc E.J. Comparative effects of cholesterol and cholesterol sulfate on hydration and ordering of dimyristoylphosphatidylcholine membranes. Biophys. J. 70 (1996) 1380-1390
    • (1996) Biophys. J. , vol.70 , pp. 1380-1390
    • Faure, C.1    Tranchant, J.F.2    Dufourc, E.J.3
  • 30
    • 0027398335 scopus 로고
    • Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes
    • Belmonte G., Pederzolli C., Maček P., and Menestrina G. Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes. J. Membr. Biol. 131 (1993) 11-22
    • (1993) J. Membr. Biol. , vol.131 , pp. 11-22
    • Belmonte, G.1    Pederzolli, C.2    Maček, P.3    Menestrina, G.4
  • 31
    • 0041461861 scopus 로고    scopus 로고
    • Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy
    • Kahya N., Scherfeld D., Bacia K., Poolman B., and Schwille P. Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy. J. Biol. Chem. 278 (2003) 28109-28115
    • (2003) J. Biol. Chem. , vol.278 , pp. 28109-28115
    • Kahya, N.1    Scherfeld, D.2    Bacia, K.3    Poolman, B.4    Schwille, P.5
  • 32
    • 4143091360 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy relates rafts in model and native membranes
    • Bacia K., Scherfeld D., Kahya N., and Schwille P. Fluorescence correlation spectroscopy relates rafts in model and native membranes. Biophys. J. 87 (2004) 1034-1043
    • (2004) Biophys. J. , vol.87 , pp. 1034-1043
    • Bacia, K.1    Scherfeld, D.2    Kahya, N.3    Schwille, P.4
  • 33
    • 52049091255 scopus 로고    scopus 로고
    • The effects of lipids on the structure of the eukaryotic cytolysin equinatoxin II: a synchrotron radiation circular dichroism spectroscopic study
    • Miles A.J., Drechsler A., Kristan K., Anderluh G., Norton R.S., Wallace B.A., and Separovic F. The effects of lipids on the structure of the eukaryotic cytolysin equinatoxin II: a synchrotron radiation circular dichroism spectroscopic study. Biochim. Biophys. Acta 1178 (2008) 2091-2096
    • (2008) Biochim. Biophys. Acta , vol.1178 , pp. 2091-2096
    • Miles, A.J.1    Drechsler, A.2    Kristan, K.3    Anderluh, G.4    Norton, R.S.5    Wallace, B.A.6    Separovic, F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.