메뉴 건너뛰기




Volumn 1828, Issue 5, 2013, Pages 1390-1395

2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes

Author keywords

Isothermal titration calorimetry; Membrane permeabilization; Molecular docking; Surface plasmon resonance

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; CALCEIN; OXYGEN; SPHINGOMYELIN; STICHOLYSIN II; TOXIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 84875154530     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.01.018     Document Type: Article
Times cited : (45)

References (38)
  • 2
    • 0242711311 scopus 로고    scopus 로고
    • Dissecting the actinoporin pore-forming mechanism
    • G. Anderluh, and P. Macek Dissecting the actinoporin pore-forming mechanism Structure 11 2003 1312 1313
    • (2003) Structure , vol.11 , pp. 1312-1313
    • Anderluh, G.1    Macek, P.2
  • 3
    • 0242542032 scopus 로고    scopus 로고
    • Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
    • J.M. Mancheno, J. Martin-Benito, M. Martinez-Ripoll, J.G. Gavilanes, and J.A. Hermoso Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation Structure 11 2003 1319 1328
    • (2003) Structure , vol.11 , pp. 1319-1328
    • Mancheno, J.M.1    Martin-Benito, J.2    Martinez-Ripoll, M.3    Gavilanes, J.G.4    Hermoso, J.A.5
  • 4
    • 0034880806 scopus 로고    scopus 로고
    • Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina
    • A. Athanasiadis, G. Anderluh, P. Macek, and D. Turk Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina Structure 9 2001 341 346
    • (2001) Structure , vol.9 , pp. 341-346
    • Athanasiadis, A.1    Anderluh, G.2    Macek, P.3    Turk, D.4
  • 6
    • 0035004910 scopus 로고    scopus 로고
    • Effects of lipid composition on membrane permeabilization by sticholysin i and II, two cytolysins of the sea anemone Stichodactyla helianthus
    • C.A. Valcarcel, S.M. Dalla, C. Potrich, I. Bernhart, M. Tejuca, D. Martinez, F. Pazos, M.E. Lanio, and G. Menestrina Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus Biophys. J. 80 2001 2761 2774
    • (2001) Biophys. J. , vol.80 , pp. 2761-2774
    • Valcarcel, C.A.1    Dalla, S.M.2    Potrich, C.3    Bernhart, I.4    Tejuca, M.5    Martinez, D.6    Pazos, F.7    Lanio, M.E.8    Menestrina, G.9
  • 7
    • 0032032911 scopus 로고    scopus 로고
    • Mechanism of the leakage induced on lipid model membranes by the hemolytic protein sticholysin II from the sea anemone Stichodactyla helianthus
    • V. de los Rios, J.M. Mancheno, M.E. Lanio, M. Onaderra, and J.G. Gavilanes Mechanism of the leakage induced on lipid model membranes by the hemolytic protein sticholysin II from the sea anemone Stichodactyla helianthus Eur. J. Biochem. 252 1998 284 289
    • (1998) Eur. J. Biochem. , vol.252 , pp. 284-289
    • De Los Rios, V.1    Mancheno, J.M.2    Lanio, M.E.3    Onaderra, M.4    Gavilanes, J.G.5
  • 9
    • 12644291218 scopus 로고    scopus 로고
    • Mechanism of membrane permeabilization by sticholysin I, a cytolysin isolated from the venom of the sea anemone Stichodactyla helianthus
    • M. Tejuca, M.D. Serra, M. Ferreras, M.E. Lanio, and G. Menestrina Mechanism of membrane permeabilization by sticholysin I, a cytolysin isolated from the venom of the sea anemone Stichodactyla helianthus Biochemistry 35 1996 14947 14957
    • (1996) Biochemistry , vol.35 , pp. 14947-14957
    • Tejuca, M.1    Serra, M.D.2    Ferreras, M.3    Lanio, M.E.4    Menestrina, G.5
  • 12
    • 77955868782 scopus 로고    scopus 로고
    • Molecular mechanism of sphingomyelin-specific membrane binding and pore formation by actinoporins
    • B. Bakrac, and G. Anderluh Molecular mechanism of sphingomyelin-specific membrane binding and pore formation by actinoporins Adv. Exp. Med. Biol. 677 2010 106 115
    • (2010) Adv. Exp. Med. Biol. , vol.677 , pp. 106-115
    • Bakrac, B.1    Anderluh, G.2
  • 13
    • 47749109057 scopus 로고    scopus 로고
    • Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence
    • P. Schon, A.J. Garcia-Saez, P. Malovrh, K. Bacia, G. Anderluh, and P. Schwille 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
    • Schon, P.1    Garcia-Saez, A.J.2    Malovrh, P.3    Bacia, K.4    Anderluh, G.5    Schwille, P.6
  • 15
    • 0028964046 scopus 로고
    • Interaction of sphingomyelinase with sphingomyelin analogs modified at the C-1 and C-3 positions of the sphingosine backbone
    • M.D. Lister, Z.S. Ruan, and R. Bittman Interaction of sphingomyelinase with sphingomyelin analogs modified at the C-1 and C-3 positions of the sphingosine backbone Biochim. Biophys. Acta 1256 1995 25 30
    • (1995) Biochim. Biophys. Acta , vol.1256 , pp. 25-30
    • Lister, M.D.1    Ruan, Z.S.2    Bittman, R.3
  • 18
    • 77955656862 scopus 로고    scopus 로고
    • Sphingomyelin analogs with branched N-acyl chains: The position of branching dramatically affects acyl chain order and sterol interactions in bilayer membranes
    • S. Jaikishan, A. Bjorkbom, and J.P. Slotte Sphingomyelin analogs with branched N-acyl chains: the position of branching dramatically affects acyl chain order and sterol interactions in bilayer membranes Biochim. Biophys. Acta 1798 2010 1987 1994
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1987-1994
    • Jaikishan, S.1    Bjorkbom, A.2    Slotte, J.P.3
  • 19
    • 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
    • J. Alegre-Cebollada, G. Clementi, M. Cunietti, C. Porres, M. Onaderra, J.G. Gavilanes, and A.M. Pozo 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 2007 211 221
    • (2007) J. Biotechnol. , vol.127 , 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.7
  • 20
    • 77649253111 scopus 로고    scopus 로고
    • Sterol affinity for bilayer membranes is affected by their ceramide content and the ceramide chain length
    • T.K. Nyholm, P.M. Grandell, B. Westerlund, and J.P. Slotte Sterol affinity for bilayer membranes is affected by their ceramide content and the ceramide chain length Biochim. Biophys. Acta 1798 2010 1008 1013
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1008-1013
    • Nyholm, T.K.1    Grandell, P.M.2    Westerlund, B.3    Slotte, J.P.4
  • 21
    • 37049079283 scopus 로고
    • A novel hydrogel matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands
    • S. Löfås, and B. Johnsson A novel hydrogel matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands J. Chem. Soc., Chem. Commun. 1990 1524 1526
    • (1990) J. Chem. Soc., Chem. Commun. , pp. 1524-1526
    • Löfås, S.1    Johnsson, B.2
  • 22
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94
    • T. Halgren Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94 J. Comput. Chem. 17 1996 490 519
    • (1996) J. Comput. Chem. , vol.17 , pp. 490-519
    • Halgren, T.1
  • 24
    • 33748538349 scopus 로고    scopus 로고
    • Automatic atom type and bond type perception in molecular mechanical calculations
    • J. Wang, W. Wang, P.A. Kollman, and D.A. Case Automatic atom type and bond type perception in molecular mechanical calculations J. Mol. Graph. Model. 25 2006 247 260
    • (2006) J. Mol. Graph. Model. , vol.25 , pp. 247-260
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 25
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • G. Jones, P. Willett, and R.C. Glen Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation J. Mol. Biol. 245 1995 43 53
    • (1995) J. Mol. Biol. , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 26
    • 0000178604 scopus 로고
    • Sphingomyelin-lecithin balance in membranes: Composition, structure, and function relationships
    • M. Shinitzky, CRC Press Boca Raton
    • Y. Barenholz Sphingomyelin-lecithin balance in membranes: composition, structure, and function relationships M. Shinitzky, Physiology of Membrane Fluidity vol. 1 1984 CRC Press Boca Raton 131 174
    • (1984) Physiology of Membrane Fluidity , vol.1 , pp. 131-174
    • Barenholz, Y.1
  • 27
    • 0019336197 scopus 로고
    • Sphingomyelins in bilayers and biological membranes
    • Y. Barenholz, and T.E. Thompson Sphingomyelins in bilayers and biological membranes Biochim. Biophys. Acta 604 1980 129 158
    • (1980) Biochim. Biophys. Acta , vol.604 , pp. 129-158
    • Barenholz, Y.1    Thompson, T.E.2
  • 29
    • 0032840719 scopus 로고    scopus 로고
    • Sphingomyelin-cholesterol interactions in biological and model membranes
    • J.P. Slotte Sphingomyelin-cholesterol interactions in biological and model membranes Chem. Phys. Lipids 102 1999 13 27
    • (1999) Chem. Phys. Lipids , vol.102 , pp. 13-27
    • Slotte, J.P.1
  • 30
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Y.A. Hannun The sphingomyelin cycle and the second messenger function of ceramide J. Biol. Chem. 269 1994 3125 3128
    • (1994) J. Biol. Chem. , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 33
    • 84863658657 scopus 로고    scopus 로고
    • Sticholysin II: A pore-forming toxin as a probe to recognize sphingomyelin in artificial and cellular membranes
    • P.S. Garcia, G. Chieppa, A. Desideri, S. Cannata, E. Romano, P. Luly, and S. Rufini Sticholysin II: a pore-forming toxin as a probe to recognize sphingomyelin in artificial and cellular membranes Toxicon 60 2012 724 733
    • (2012) Toxicon , vol.60 , pp. 724-733
    • Garcia, P.S.1    Chieppa, G.2    Desideri, A.3    Cannata, S.4    Romano, E.5    Luly, P.6    Rufini, S.7
  • 34
    • 0028034850 scopus 로고
    • Interaction of cholesterol with sphingomyelin in monolayers and vesicles
    • R. Bittman, C.R. Kasireddy, P. Mattjus, and J.P. Slotte Interaction of cholesterol with sphingomyelin in monolayers and vesicles Biochemistry 33 1994 11776 11781
    • (1994) Biochemistry , vol.33 , pp. 11776-11781
    • Bittman, R.1    Kasireddy, C.R.2    Mattjus, P.3    Slotte, J.P.4
  • 37
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 38
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.