메뉴 건너뛰기




Volumn 1667, Issue 2, 2004, Pages 148-156

Antibacterial activity and pore-forming properties of ceratotoxins: A mechanism of action based on the barrel stave model

Author keywords

helical peptide; Conductance; Ion channel; Lipid bilayer

Indexed keywords

CERATOTOXIN A; CERATOTOXIN A1 17; CERATOTOXIN A1 29; CERATOTOXIN A17 36; CERATOTOXIN C; CERATOTOXIN C1 32; CERATOTOXIN D; CERATOTOXIN D1 36; ION CHANNEL; UNCLASSIFIED DRUG;

EID: 9644281662     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2004.09.011     Document Type: Article
Times cited : (39)

References (30)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 0016311447 scopus 로고
    • A molecular model of membrane excitability
    • G. Baumann, and P. Mueller A molecular model of membrane excitability J. Supramol. Struct. 2 1974 538 557
    • (1974) J. Supramol. Struct. , vol.2 , pp. 538-557
    • Baumann, G.1    Mueller, P.2
  • 3
    • 0016183539 scopus 로고
    • Statistical analysis of alamethicin channels in black lipid membranes
    • G. Boheim Statistical analysis of alamethicin channels in black lipid membranes J. Membr. Biol. 19 1974 277 303
    • (1974) J. Membr. Biol. , vol.19 , pp. 277-303
    • Boheim, G.1
  • 4
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? a case study on melittin pores
    • L. Yang, T.A. Harroun, T.M. Weiss, L. Ding, and H.W. Huang Barrel-stave model or toroidal model? A case study on melittin pores Biophys. J. 81 2001 1475 1485
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 5
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta 1462 1999 55 70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 7
    • 0029858808 scopus 로고    scopus 로고
    • Molecular characterization of ceratotoxin C, a novel antibacterial female-specific peptide of the ceratotoxin family from the medfly Ceratitis capitata
    • M. Rosetto, A.G. Manetti, P.C. Giordano, L. Marri, R. Amons, C.T. Baldari, D. Marchini, and R. Dallai Molecular characterization of ceratotoxin C, a novel antibacterial female-specific peptide of the ceratotoxin family from the medfly Ceratitis capitata Eur. J. Biochem. 241 1996 330 337
    • (1996) Eur. J. Biochem. , vol.241 , pp. 330-337
    • Rosetto, M.1    Manetti, A.G.2    Giordano, P.C.3    Marri, L.4    Amons, R.5    Baldari, C.T.6    Marchini, D.7    Dallai, R.8
  • 8
    • 0027631267 scopus 로고
    • Purification and primary structure of ceratotoxin a and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta:Diptera)
    • D. Marchini, P.C. Giordano, R. Amons, L.F. Bernini, and R. Dallai Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta:Diptera) Insect Biochem. Mol. Biol. 23 1993 591 598
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 591-598
    • Marchini, D.1    Giordano, P.C.2    Amons, R.3    Bernini, L.F.4    Dallai, R.5
  • 9
    • 0031410160 scopus 로고    scopus 로고
    • The genes encoding the antibacterial sex-specific peptides ceratotoxins are clustered in the genome of the medfly Ceratitis capitata
    • M. Rosetto, T. De Filippis, A.G. Manetti, D. Marchini, C.T. Baldari, and R. Dallai The genes encoding the antibacterial sex-specific peptides ceratotoxins are clustered in the genome of the medfly Ceratitis capitata Insect Biochem. Mol. Biol. 27 1997 1039 1046
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 1039-1046
    • Rosetto, M.1    De Filippis, T.2    Manetti, A.G.3    Marchini, D.4    Baldari, C.T.5    Dallai, R.6
  • 10
    • 0029893090 scopus 로고    scopus 로고
    • The novel antibacterial peptide ceratotoxin a alters permeability of the inner and outer membrane of Escherichia coli K-12
    • L. Marri, R. Dallai, and D. Marchini The novel antibacterial peptide ceratotoxin A alters permeability of the inner and outer membrane of Escherichia coli K-12 Curr. Microbiol. 33 1996 40 43
    • (1996) Curr. Microbiol. , vol.33 , pp. 40-43
    • Marri, L.1    Dallai, R.2    Marchini, D.3
  • 11
    • 1042290509 scopus 로고    scopus 로고
    • The antibacterial peptide ceratotoxin a displays alamethicin-like behavior in lipid bilayers
    • N. Saint, L. Marri, D. Marchini, and G. Molle The antibacterial peptide ceratotoxin A displays alamethicin-like behavior in lipid bilayers Peptides 24 2003 1779 1784
    • (2003) Peptides , vol.24 , pp. 1779-1784
    • Saint, N.1    Marri, L.2    Marchini, D.3    Molle, G.4
  • 12
    • 0030957967 scopus 로고    scopus 로고
    • Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder
    • A.M. Cole, P. Weis, and G. Diamond Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder J. Biol. Chem. 272 1997 12008 12013
    • (1997) J. Biol. Chem. , vol.272 , pp. 12008-12013
    • Cole, A.M.1    Weis, P.2    Diamond, G.3
  • 13
    • 0037206144 scopus 로고    scopus 로고
    • Antibacterial peptide pleurocidin forms ion channels in planar lipid bilayers
    • N. Saint, H. Cadiou, Y. Bessin, and G. Molle Antibacterial peptide pleurocidin forms ion channels in planar lipid bilayers Biochim. Biophys. Acta 1564 2002 359 364
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 359-364
    • Saint, N.1    Cadiou, H.2    Bessin, Y.3    Molle, G.4
  • 16
    • 0036142518 scopus 로고    scopus 로고
    • Bacteria associated with the oesophageal bulb of the medfly Ceratitis capitata (Diptera:Tephritidae)
    • D. Marchini, M. Rosetto, R. Dallai, and L. Marri Bacteria associated with the oesophageal bulb of the medfly Ceratitis capitata (Diptera:Tephritidae) Curr. Microbiol. 44 2002 120 124
    • (2002) Curr. Microbiol. , vol.44 , pp. 120-124
    • Marchini, D.1    Rosetto, M.2    Dallai, R.3    Marri, L.4
  • 17
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • M. Montal, and P. Mueller Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties Proc. Natl. Acad. Sci. U. S. A. 69 1972 3561 3566
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 18
    • 0019166405 scopus 로고
    • The synthesis of antibacterial proteins in isolated fat body from Cecropia silkmoth pupae
    • I. Faye, and G.R. Wyatt The synthesis of antibacterial proteins in isolated fat body from Cecropia silkmoth pupae Experientia 36 1980 1325 1326
    • (1980) Experientia , vol.36 , pp. 1325-1326
    • Faye, I.1    Wyatt, G.R.2
  • 19
    • 0024841875 scopus 로고
    • Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids
    • H.G. Boman, D. Wade, I.A. Boman, B. Wahlin, and R.B. Merrifield Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids FEBS Lett. 259 1989 103 106
    • (1989) FEBS Lett. , vol.259 , pp. 103-106
    • Boman, H.G.1    Wade, D.2    Boman, I.A.3    Wahlin, B.4    Merrifield, R.B.5
  • 20
    • 0020686109 scopus 로고
    • Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia
    • D. Hultmark, A. Engstrom, K. Andersson, H. Steiner, H. Bennich, and H.G. Boman Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia EMBO J. 2 1983 571 576
    • (1983) EMBO J. , vol.2 , pp. 571-576
    • Hultmark, D.1    Engstrom, A.2    Andersson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 22
    • 0020586620 scopus 로고
    • Alamethicin-induced current-voltage curve asymmetry in lipid bilayers
    • I. Vodyanoy, J.E. Hall, and T.M. Balasubramanian Alamethicin-induced current-voltage curve asymmetry in lipid bilayers Biophys. J. 42 1983 71 82
    • (1983) Biophys. J. , vol.42 , pp. 71-82
    • Vodyanoy, I.1    Hall, J.E.2    Balasubramanian, T.M.3
  • 23
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues
    • H. Duclohier, and H. Wroblewski Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues J. Membr. Biol. 184 2001 1 12
    • (2001) J. Membr. Biol. , vol.184 , pp. 1-12
    • Duclohier, H.1    Wroblewski, H.2
  • 24
    • 0035967534 scopus 로고    scopus 로고
    • The effect of cyclization of magainin 2 and melittin analogues on structure, function, and model membrane interactions: Implication to their mode of action
    • T. Unger, Z. Oren, and Y. Shai The effect of cyclization of magainin 2 and melittin analogues on structure, function, and model membrane interactions: implication to their mode of action Biochemistry 40 2001 6388 6397
    • (2001) Biochemistry , vol.40 , pp. 6388-6397
    • Unger, T.1    Oren, Z.2    Shai, Y.3
  • 25
    • 0037457824 scopus 로고    scopus 로고
    • Exploring peptide membrane interaction using surface plasmon resonance: Differentiation between pore formation versus membrane disruption by lytic peptides
    • N. Papo, and Y. Shai Exploring peptide membrane interaction using surface plasmon resonance: Differentiation between pore formation versus membrane disruption by lytic peptides Biochemistry 42 2003 458 466
    • (2003) Biochemistry , vol.42 , pp. 458-466
    • Papo, N.1    Shai, Y.2
  • 26
    • 0036467404 scopus 로고    scopus 로고
    • General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides
    • M. Dathe, J. Meyer, M. Beyermann, B. Maul, C. Hoischen, and M. Bienert General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides Biochim. Biophys. Acta 1558 2002 171 186
    • (2002) Biochim. Biophys. Acta , vol.1558 , pp. 171-186
    • Dathe, M.1    Meyer, J.2    Beyermann, M.3    Maul, B.4    Hoischen, C.5    Bienert, M.6
  • 27
    • 0033737012 scopus 로고    scopus 로고
    • The topology of lysine-containing amphipathic peptides in bilayers by circular dichroism, solid-state NMR, and molecular modeling
    • B. Vogt, P. Ducarme, S. Schinzel, R. Brasseur, and B. Bechinger The topology of lysine-containing amphipathic peptides in bilayers by circular dichroism, solid-state NMR, and molecular modeling Biophys. J. 79 2000 2644 2656
    • (2000) Biophys. J. , vol.79 , pp. 2644-2656
    • Vogt, B.1    Ducarme, P.2    Schinzel, S.3    Brasseur, R.4    Bechinger, B.5
  • 28
    • 0033594986 scopus 로고    scopus 로고
    • Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides
    • L. Zhang, R. Benz, and R.E. Hancock Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides Biochemistry 38 1999 8102 8111
    • (1999) Biochemistry , vol.38 , pp. 8102-8111
    • Zhang, L.1    Benz, R.2    Hancock, R.E.3
  • 29
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • Y. Shai, and Z. Oren From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides Peptides 22 2001 1629 1641
    • (2001) Peptides , vol.22 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 30
    • 0030807804 scopus 로고    scopus 로고
    • Lateral diffusion and conductance properties of a fluorescein-labelled alamethicin in planar lipid bilayers
    • O. Helluin, J.Y. Dugast, G. Molle, A.R. Mackie, S. Ladha, and H. Duclohier Lateral diffusion and conductance properties of a fluorescein-labelled alamethicin in planar lipid bilayers Biochim. Biophys. Acta 1330 1997 284 292
    • (1997) Biochim. Biophys. Acta , vol.1330 , pp. 284-292
    • Helluin, O.1    Dugast, J.Y.2    Molle, G.3    MacKie, A.R.4    Ladha, S.5    Duclohier, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.