메뉴 건너뛰기




Volumn 42, Issue 32, 2003, Pages 9804-9812

Interaction of amoebapores and NK-lysin with symmetric phospholipid and asymmetric lipopolysaccharide/phospholipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; ELECTRIC CONDUCTANCE; ENERGY TRANSFER; ESCHERICHIA COLI; FLUORESCENCE; PH EFFECTS; PHOSPHOLIPIDS; PROTEINS; SPECTROSCOPIC ANALYSIS;

EID: 0042026495     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034686u     Document Type: Article
Times cited : (33)

References (41)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms, Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 0029061894 scopus 로고
    • NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity
    • Andersson, M., Gunne, H., Agerberth, B., Boman, A., Bergman, T., Sillard, R., Jornvall, H., Mutt, V., Olsson, B., and Wigzell, H. (1995) NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity, EMBO J. 14, 1615-1625.
    • (1995) EMBO J. , vol.14 , pp. 1615-1625
    • Andersson, M.1    Gunne, H.2    Agerberth, B.3    Boman, A.4    Bergman, T.5    Sillard, R.6    Jornvall, H.7    Mutt, V.8    Olsson, B.9    Wigzell, H.10
  • 3
    • 0031569218 scopus 로고    scopus 로고
    • Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins
    • Pena, S. V., Hanson, D. A., Carr, B. A., Goralski, T. J., and Krensky, A. M. (1997) Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins, J. Immunol. 158, 2680-2688.
    • (1997) J. Immunol. , vol.158 , pp. 2680-2688
    • Pena, S.V.1    Hanson, D.A.2    Carr, B.A.3    Goralski, T.J.4    Krensky, A.M.5
  • 4
    • 0028880453 scopus 로고
    • Ancient weapons: NK-lysin is a mammalian homolog to pore-forming peptides of a protozoan parasite
    • Leippe, M. (1995) Ancient weapons: NK-lysin is a mammalian homolog to pore-forming peptides of a protozoan parasite, Cell 83, 17-18.
    • (1995) Cell , vol.83 , pp. 17-18
    • Leippe, M.1
  • 7
    • 0028073698 scopus 로고
    • Amoebapores, a family of membraneolytic peptides from cytoplasmic granules of Entamoeba histolytica: Isolation, primary structure, and pore formation in bacterial cytoplasmic membranes
    • Leippe, M., Andrä, J., Nickel, R., Tannich, E., and Müller-Eberhard, H. J. (1994) Amoebapores, a family of membraneolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes, Mol. Microbiol. 14, 895-904.
    • (1994) Mol. Microbiol. , vol.14 , pp. 895-904
    • Leippe, M.1    Andrä, J.2    Nickel, R.3    Tannich, E.4    Müller-Eberhard, H.J.5
  • 8
    • 0028072978 scopus 로고
    • Pore-forming peptide of Entamoeba histolytica. Significance of positively charged amino acid residues for its mode of action
    • Andrä, J. and Leippe, M. (1994) Pore-forming peptide of Entamoeba histolytica. Significance of positively charged amino acid residues for its mode of action, FEBS Lett. 354, 97-102.
    • (1994) FEBS Lett. , vol.354 , pp. 97-102
    • Andrä, J.1    Leippe, M.2
  • 9
    • 0029126584 scopus 로고
    • Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
    • Munford, R. S., Sheppard, P. O., and O'Hara, P. J. (1995) Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure, J. Lipid Res. 36, 1653-1663.
    • (1995) J. Lipid Res. , vol.36 , pp. 1653-1663
    • Munford, R.S.1    Sheppard, P.O.2    O'Hara, P.J.3
  • 12
    • 0037391712 scopus 로고    scopus 로고
    • Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes
    • Andrä, J., Herbst, R., and Leippe, M. (2003) Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes, Dev. Comp. Immunol. 27, 291-304.
    • (2003) Dev. Comp. Immunol. , vol.27 , pp. 291-304
    • Andrä, J.1    Herbst, R.2    Leippe, M.3
  • 13
    • 0030950248 scopus 로고    scopus 로고
    • Amoebapores
    • Leippe, M. (1997) Amoebapores, Parasitol. Today 13, 178-183.
    • (1997) Parasitol. Today , vol.13 , pp. 178-183
    • Leippe, M.1
  • 14
    • 0032876977 scopus 로고    scopus 로고
    • Comparative modeling of amoebapores and granulysin based on the NK-lysin structure-structural and functional implications
    • Bruhn, H., and Leippe, M. (1999) Comparative modeling of amoebapores and granulysin based on the NK-lysin structure-structural and functional implications, Biol. Chem. 380, 1001-1007.
    • (1999) Biol. Chem. , vol.380 , pp. 1001-1007
    • Bruhn, H.1    Leippe, M.2
  • 15
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara, M. (1992) Agents that increase the permeability of the outer membrane, Microbiol. Rev. 56, 395-411.
    • (1992) Microbiol. Rev. , vol.56 , pp. 395-411
    • Vaara, M.1
  • 16
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and Vaara, M. (1985) Molecular basis of bacterial outer membrane permeability, Microbial. Rev. 49, 1-32.
    • (1985) Microbial. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 17
    • 0015523228 scopus 로고
    • Mechanism and assembly of the outer membrane of Salmonella typhimurium
    • Osborn, M. J., Gander, J. E., Parisi, E., and Carson, J. (1972) Mechanism and assembly of the outer membrane of Salmonella typhimurium, J. Biol. Chem. 247, 3962-3972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 18
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B. L., Selsted, M. E., Ganz, T., and Lehrer, R. I. (1990) Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes, Proc. Natl. Acad. Sci. U.S.A. 87, 210-214.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 19
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • Wu, M., Maier, E., Benz, R., and Hancock, R. E. (1999) Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli, Biochemistry 38, 7235-7242.
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.4
  • 20
    • 0033648937 scopus 로고    scopus 로고
    • Characterization of molecular properties of pore-forming toxins with planar lipid bilayers
    • Dalla, S. M., and Menestrina, G. (2000) Characterization of molecular properties of pore-forming toxins with planar lipid bilayers, Methods Mol. Biol. 145, 171-188.
    • (2000) Methods Mol. Biol. , vol.145 , pp. 171-188
    • Dalla, S.M.1    Menestrina, G.2
  • 21
    • 0035007963 scopus 로고    scopus 로고
    • Interaction of CAP18-Derived peptides with membranes made from endotoxins or phospholipids
    • Gutsmann, T., Hagge, S. O., Larrick, J. W., Seydel, U., and Wiese, A. (2001) Interaction of CAP18-Derived Peptides with Membranes Made from Endotoxins or Phospholipids, Biophys. J. 80, 2935-2945.
    • (2001) Biophys. J. , vol.80 , pp. 2935-2945
    • Gutsmann, T.1    Hagge, S.O.2    Larrick, J.W.3    Seydel, U.4    Wiese, A.5
  • 22
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal, M., and Mueller, P. (1972) Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties, Proc. Natl. Acad. Sci. U.S.A. 69, 3561-3566.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 23
    • 0024391437 scopus 로고
    • Reconstitution of the lipid matrix of the outer membrane of Gram-negative bacteria as asymmetric planar bilayer
    • Seydel, U., Schröder, G., and Brandenburg, K. (1989) Reconstitution of the lipid matrix of the outer membrane of Gram-negative bacteria as asymmetric planar bilayer, J. Membr. Biol. 109, 95-103.
    • (1989) J. Membr. Biol. , vol.109 , pp. 95-103
    • Seydel, U.1    Schröder, G.2    Brandenburg, K.3
  • 24
    • 0009550916 scopus 로고
    • An ion-channel forming protein produced by Entamoeba histolytica
    • Lynch, E. C., Rosenberg, I. M., and Gitler, C. (1982) An ion-channel forming protein produced by Entamoeba histolytica, EMBO J. 1, 801-804.
    • (1982) EMBO J. , vol.1 , pp. 801-804
    • Lynch, E.C.1    Rosenberg, I.M.2    Gitler, C.3
  • 25
    • 0024308433 scopus 로고
    • Pore-forming protein from Entamoeba histolytica forms voltageand pH-controlled multi-state channels with properties similar those of the barrel-stave aggregates
    • Keller, F., Hanke, W., Trissl, D., and Bakker-Grunwald, T. (1989) Pore-forming protein from Entamoeba histolytica forms voltageand pH-controlled multi-state channels with properties similar those of the barrel-stave aggregates, Biochim. Biophys. Acta 982, 89-93.
    • (1989) Biochim. Biophys. Acta , vol.982 , pp. 89-93
    • Keller, F.1    Hanke, W.2    Trissl, D.3    Bakker-Grunwald, T.4
  • 27
    • 0032738115 scopus 로고    scopus 로고
    • Molecular electroporation: A unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin
    • Miteva, M., Andersson, M., Karshikoff, A., and Otting, G. (1999) Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin, FEBS Lett. 462, 155-158.
    • (1999) FEBS Lett. , vol.462 , pp. 155-158
    • Miteva, M.1    Andersson, M.2    Karshikoff, A.3    Otting, G.4
  • 28
    • 0032520840 scopus 로고    scopus 로고
    • Molecular mechanisms of Polymyxin B-membrane interactions: Direct correlation between surface charge density and self-promoted uptake
    • Wiese, A., Münstermann, M., Gutsmann, T., Lindner, B., Kawahara, K., Zähringer, U., and Seydel, U. (1998) Molecular mechanisms of Polymyxin B-membrane interactions: direct correlation between surface charge density and self-promoted uptake, J. Membr. Biol. 162, 127-138.
    • (1998) J. Membr. Biol. , vol.162 , pp. 127-138
    • Wiese, A.1    Münstermann, M.2    Gutsmann, T.3    Lindner, B.4    Kawahara, K.5    Zähringer, U.6    Seydel, U.7
  • 29
    • 0014531184 scopus 로고
    • A new method for the extraction of R lipopolysaccharides
    • Galanos, C., Lüderitz O., and Westphal, O. (1969) A new method for the extraction of R lipopolysaccharides, Eur. J. Biochem. 9, 245-249.
    • (1969) Eur. J. Biochem. , vol.9 , pp. 245-249
    • Galanos, C.1    Lüderitz, O.2    Westphal, O.3
  • 30
    • 0033230141 scopus 로고    scopus 로고
    • Poreforming peptides of Entamoeba dispar. Similarity and divergence to amoebapores in structure, expression and activity
    • Nickel, R., Ott, C., Dandekar, T., and Leippe, M. (1999) Poreforming peptides of Entamoeba dispar. Similarity and divergence to amoebapores in structure, expression and activity, Eur. J. Biochem. 265, 1002-1007.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 1002-1007
    • Nickel, R.1    Ott, C.2    Dandekar, T.3    Leippe, M.4
  • 31
    • 0037308713 scopus 로고    scopus 로고
    • NK-Lysin and its shortened analog NK-2 exhibit potent activities against trypanosoma cruzi
    • Jacobs, T., Bruhn, H., Gaworski I., Fleischer B., and Leippe, M. (2003) NK-Lysin and Its Shortened Analog NK-2 Exhibit Potent Activities against Trypanosoma cruzi, Antimicrob. Agents Chemother. 47, 607-613.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 607-613
    • Jacobs, T.1    Bruhn, H.2    Gaworski, I.3    Fleischer, B.4    Leippe, M.5
  • 32
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Elman, G. L. (1959) Tissue sulfhydryl groups, Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Elman, G.L.1
  • 33
    • 0033656562 scopus 로고    scopus 로고
    • Electrophysiological measurements on reconstituted outer membranes
    • Wiese, A., and Seydel, U. (1999) Electrophysiological measurements on reconstituted outer membranes, Methods Mol. Biol. 145, 355-370.
    • (1999) Methods Mol. Biol. , vol.145 , pp. 355-370
    • Wiese, A.1    Seydel, U.2
  • 34
    • 0033550049 scopus 로고    scopus 로고
    • Molecular mechanisms of interaction of rabbit CAP18 with outer membranes of Gram-negative bacteria
    • Gutsmann, T., Larrick, J. W., Seydel U., and Wiese, A. (1999) Molecular mechanisms of interaction of rabbit CAP18 with outer membranes of Gram-negative bacteria, Biochemistry 38, 13643-13653.
    • (1999) Biochemistry , vol.38 , pp. 13643-13653
    • Gutsmann, T.1    Larrick, J.W.2    Seydel, U.3    Wiese, A.4
  • 36
    • 0017876757 scopus 로고
    • Voltage-dependent capacitance in lipid bilayers made from monolayers
    • Alvarez, O., and LaTorre, R. (1978) Voltage-dependent capacitance in lipid bilayers made from monolayers. Biophys. J. 21, 1-17.
    • (1978) Biophys. J. , vol.21 , pp. 1-17
    • Alvarez, O.1    LaTorre, R.2
  • 37
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., Hoekstra, D., and Pagano, R. E. (1981) Use of resonance energy transfer to monitor membrane fusion, Biochemistry 20, 4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 38
    • 0033839604 scopus 로고    scopus 로고
    • Mechanisms of action of rabbit CAP18 on monolayers and liposomes made from endotoxins or phospholipids
    • Gutsmann, T., Fix, M., Larrick, J. W., and Wiese, A. (2000) Mechanisms of action of rabbit CAP18 on monolayers and liposomes made from endotoxins or phospholipids, J. Membr. Biol. 176, 223-236.
    • (2000) J. Membr. Biol. , vol.176 , pp. 223-236
    • Gutsmann, T.1    Fix, M.2    Larrick, J.W.3    Wiese, A.4
  • 39
    • 0023867105 scopus 로고
    • Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane
    • Sen, K., Hellman, J., and Nikaido, H. (1988) Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane, J. Biol. Chem. 263, 1182-1187.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1182-1187
    • Sen, K.1    Hellman, J.2    Nikaido, H.3
  • 40
    • 0030961033 scopus 로고    scopus 로고
    • Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica
    • Berninghausen O., and Leippe, M. (1997) Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica, Infect. Immun. 65, 3615-3621.
    • (1997) Infect. Immun. , vol.65 , pp. 3615-3621
    • Berninghausen, O.1    Leippe, M.2
  • 41
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human beta -defensin-3, a novel human inducible peptide antibiotic
    • Harder, J., Bartels, J., Christophers, E., and Schröder, J. M. (2001) Isolation and characterization of human beta -defensin-3, a novel human inducible peptide antibiotic, J. Biol. Chem. 276, 5707-5713.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schröder, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.