메뉴 건너뛰기




Volumn 66, Issue 6, 1998, Pages 2434-2440

Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; BIS(1,3 DIBUTYLBARBITURIC ACID)TRIMETHINE OXONOL; CARBONYL CYANIDE CHLOROPHENYLHYDRAZONE; ESCHERICHIA COLI LIPOPOLYSACCHARIDE; FLUORESCENT DYE; HUMAN LACTOFERRIN PEPTIDE 1; HUMAN LACTOFERRIN PEPTIDE 2; HUMAN LACTOFERRIN PEPTIDE 6; HUMAN LACTOFERRIN PEPTIDE 7; LACTOFERRIN; PROPIDIUM IODIDE; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 0031839843     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.66.6.2434-2440.1998     Document Type: Article
Times cited : (109)

References (39)
  • 3
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • Arnold, R. R., R. M. Cole, and J. R. McGhee. 1977. A bactericidal effect for human lactoferrin. Science 197:263-265.
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, R.M.2    McGhee, J.R.3
  • 5
    • 0022643302 scopus 로고
    • Bactericidal effect of lactoferrin on Legionella pneumophila
    • Bortner, C. A., R. D. Miller, and R. R. Arnold. 1986. Bactericidal effect of lactoferrin on Legionella pneumophila. Infect. Immun. 51:373-377.
    • (1986) Infect. Immun. , vol.51 , pp. 373-377
    • Bortner, C.A.1    Miller, R.D.2    Arnold, R.R.3
  • 6
    • 0018899060 scopus 로고
    • Lactoferrin in human milk: Its role in iron absorption and protection against enteric infection in the new-born infant
    • Brock, J. H. 1980. Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the new-born infant. Arch. Dis. Child. 55:417-421.
    • (1980) Arch. Dis. Child. , vol.55 , pp. 417-421
    • Brock, J.H.1
  • 7
    • 0015497562 scopus 로고
    • Iron-binding proteins in milk and resistance to Escherichia coli infection in infants
    • Bullen, J. J., H. J. Rogers, and L. Leigh. 1972. Iron-binding proteins in milk and resistance to Escherichia coli infection in infants. Br. Med. J. 1:69-75.
    • (1972) Br. Med. J. , vol.1 , pp. 69-75
    • Bullen, J.J.1    Rogers, H.J.2    Leigh, L.3
  • 8
    • 2642632040 scopus 로고    scopus 로고
    • A helical region on human lactoferrin - Its role in antimicrobial pathogencsis
    • G. Spik, D. Legrand, J. Mazurier, J.-P. Perraudin, and A. Pierce (ed.), in press. Plenum Publishing Corporation, New York, N.Y.
    • Chapple, D. S., D. J. Mason, C. L. Joannou, J. K. Shergill, E. W. Odell, V. Gant, and R. W. Evans. A helical region on human lactoferrin - its role in antimicrobial pathogencsis. In G. Spik, D. Legrand, J. Mazurier, J.-P. Perraudin, and A. Pierce (ed.), Advances in lactoferrin research, in press. Plenum Publishing Corporation, New York, N.Y.
    • Advances in Lactoferrin Research
    • Chapple, D.S.1    Mason, D.J.2    Joannou, C.L.3    Shergill, J.K.4    Odell, E.W.5    Gant, V.6    Evans, R.W.7
  • 9
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen, B., J. Fink, R. B. Merrifield, and D. Mauzerall. 1988. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. USA 85:5072-5076.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 11
    • 0024438756 scopus 로고
    • Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers
    • Duclohier, H., G. Molle, and G. Spach. 1989. Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. Biophys. J. 56:1017-1021.
    • (1989) Biophys. J. , vol.56 , pp. 1017-1021
    • Duclohier, H.1    Molle, G.2    Spach, G.3
  • 12
    • 0029620277 scopus 로고
    • Lactoferrin-lipopolysaccharide interaction: Involvement of the 28-34 loop region of human lactoferrin in the high affinity bindine to Escherichia coli 055B5 lipopolysaccharide
    • Elass-Rochard, E., A. Roseanu, D. Legrand, M. Trif, V. Salmon, C. Motas, J. Montreuil, and D. Spik. 1995. Lactoferrin-lipopolysaccharide interaction: involvement of the 28-34 loop region of human lactoferrin in the high affinity bindine to Escherichia coli 055B5 lipopolysaccharide. Biochem. J. 312:839-845.
    • (1995) Biochem. J. , vol.312 , pp. 839-845
    • Elass-Rochard, E.1    Roseanu, A.2    Legrand, D.3    Trif, M.4    Salmon, V.5    Motas, C.6    Montreuil, J.7    Spik, D.8
  • 13
    • 0026095436 scopus 로고
    • Killing of Gram-negative bacteria by lactoferrin and lysozyme
    • Ellison, R. T., III, and T. J. Giehl. 1991. Killing of Gram-negative bacteria by lactoferrin and lysozyme. J. Clin. Invest. 88:1080-1091.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1080-1091
    • Ellison III, R.T.1    Giehl, T.J.2
  • 14
    • 0023815539 scopus 로고
    • Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin
    • Ellison, R. T., III, T. J. Giehl, and F. M. LaForce. 1988. Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect. Immun. 56:2774-2780.
    • (1988) Infect. Immun. , vol.56 , pp. 2774-2780
    • Ellison III, R.T.1    Giehl, T.J.2    Laforce, F.M.3
  • 15
    • 0028273860 scopus 로고
    • Lactoferrin hinds to porins OmpF and OmpC in Escherichia coli
    • Erdei, J., A. Forsgren, and A. S. Naidu. 1994. Lactoferrin hinds to porins OmpF and OmpC in Escherichia coli. Infect. Immun. 62:1236-1240.
    • (1994) Infect. Immun. , vol.62 , pp. 1236-1240
    • Erdei, J.1    Forsgren, A.2    Naidu, A.S.3
  • 17
    • 2642686938 scopus 로고
    • The application of flow cytometry to the study of bacterial responses to antibiotics
    • Gant, V. A., G. Warnes, I. Phillips, and G. F. Savage. 1993. The application of flow cytometry to the study of bacterial responses to antibiotics. J. Med. Microbiol. 23:83-88.
    • (1993) J. Med. Microbiol. , vol.23 , pp. 83-88
    • Gant, V.A.1    Warnes, G.2    Phillips, I.3    Savage, G.F.4
  • 19
    • 0014050060 scopus 로고
    • Sequence analysis of melittin from tryptic and peptic degradation products
    • Habermann, E., and J. Jentsch. 1967. Sequence analysis of melittin from tryptic and peptic degradation products. Hoppe-Seyler's Z. Physiol. Chem. 348:37-50.
    • (1967) Hoppe-Seyler's Z. Physiol. Chem. , vol.348 , pp. 37-50
    • Habermann, E.1    Jentsch, J.2
  • 20
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock, R. E. W. 1997. Peptide antibiotics. Lancet 349:418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.W.1
  • 21
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from the hemolymph of immunised pupae of Hyalphora cecropia
    • Hultmark, D., H. Steiner, T. Rasmuson, and H. G. Boman. 1980. Insect immunity. Purification and properties of three inducible bactericidal proteins from the hemolymph of immunised pupae of Hyalphora cecropia. Eur. J. Biochem. 106:7-16.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 22
    • 0001618922 scopus 로고
    • Isolation of an iron-containing red protein from human milk
    • Johansson, B. 1960. Isolation of an iron-containing red protein from human milk. Acta Chem. Scand. 14:510-512.
    • (1960) Acta Chem. Scand. , vol.14 , pp. 510-512
    • Johansson, B.1
  • 23
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B. L., M. E. Selsted, T. Ganz, and R. I. Lehrer. 1990. Antimicrobial defensin peptides form voltage dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl. Acad. Sci. USA 87:210-214.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 24
    • 0023736956 scopus 로고
    • Killing of Actinobacillus actinomycetemcomitans by human lactoferrin
    • Kalmar, J. R., and R. R. Arnold. 1988. Killing of Actinobacillus actinomycetemcomitans by human lactoferrin. Infect. Immun. 56:2552-2557.
    • (1988) Infect. Immun. , vol.56 , pp. 2552-2557
    • Kalmar, J.R.1    Arnold, R.R.2
  • 25
    • 0029860472 scopus 로고    scopus 로고
    • Structure-biological activity relationship of 11-residue highly basic peptide segment of bovine lactoferrin
    • Kang, J. H., M. K. Lee, K. L. Kim, and K. S. Hahan. 1996. Structure-biological activity relationship of 11-residue highly basic peptide segment of bovine lactoferrin. Int. J. Peptide Protein Res. 48:357-363.
    • (1996) Int. J. Peptide Protein Res. , vol.48 , pp. 357-363
    • Kang, J.H.1    Lee, M.K.2    Kim, K.L.3    Hahan, K.S.4
  • 26
    • 0026576379 scopus 로고
    • Rapid assessment of bacterial viability and vitality by rhodamine 123 and flow-cytometry
    • Kaprelyants, A. S., and D. B. Kell. 1992. Rapid assessment of bacterial viability and vitality by rhodamine 123 and flow-cytometry. J. Appl. Bacteriol. 72:410-422.
    • (1992) J. Appl. Bacteriol. , vol.72 , pp. 410-422
    • Kaprelyants, A.S.1    Kell, D.B.2
  • 27
    • 0029885779 scopus 로고    scopus 로고
    • Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance
    • Kuziemko, G. M., M. Stroh, and R. C. Stevens. 1996. Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance. Biochemistry 35:6375-6384.
    • (1996) Biochemistry , vol.35 , pp. 6375-6384
    • Kuziemko, G.M.1    Stroh, M.2    Stevens, R.C.3
  • 28
    • 0027978954 scopus 로고
    • Delineation of glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin
    • Mann, D. M., E. Romm, and M. Migliorini. 1994. Delineation of glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin. J. Biol. Chem. 269:23661-23667.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23661-23667
    • Mann, D.M.1    Romm, E.2    Migliorini, M.3
  • 30
    • 0028033780 scopus 로고
    • Rapid estimation of bacterial antibiotic susceptibility
    • Mason, D. J., R. Allman, J. M. Stark, and D. Lloyd. 1994. Rapid estimation of bacterial antibiotic susceptibility. J. Microsc. 176:8-16.
    • (1994) J. Microsc. , vol.176 , pp. 8-16
    • Mason, D.J.1    Allman, R.2    Stark, J.M.3    Lloyd, D.4
  • 31
    • 0009665799 scopus 로고
    • An iron-binding protein common to many external secretions
    • Masson, P. L., J. F. Heremans, and C. Dive. 1966. An iron-binding protein common to many external secretions. Clin. Chim. Acta 14:735-739.
    • (1966) Clin. Chim. Acta , vol.14 , pp. 735-739
    • Masson, P.L.1    Heremans, J.F.2    Dive, C.3
  • 32
    • 0014574791 scopus 로고
    • Lactoferrin, an iron-binding protein in neutrophilic leukocytes
    • Masson, P. L., J. F. Heremans, and E. Schonne. 1969. Lactoferrin, an iron-binding protein in neutrophilic leukocytes. J. Exp. Med. 130:643-658.
    • (1969) J. Exp. Med. , vol.130 , pp. 643-658
    • Masson, P.L.1    Heremans, J.F.2    Schonne, E.3
  • 34
    • 0029930976 scopus 로고    scopus 로고
    • Antibacterial activity of peptides homologous to a loop region in human lactoferrin
    • Odell, E. W., R. Sarra, M. Foxworthy, D. S. Chapple, and R. W. Evans. 1996. Antibacterial activity of peptides homologous to a loop region in human lactoferrin. FEBS Lett. 382:175-178.
    • (1996) FEBS Lett. , vol.382 , pp. 175-178
    • Odell, E.W.1    Sarra, R.2    Foxworthy, M.3    Chapple, D.S.4    Evans, R.W.5
  • 35
    • 0014428034 scopus 로고
    • Inhibition of bacteria by lactoferrin and other iron-chelating agents
    • Oram, J. D., and B. Reiter. 1968. Inhibition of bacteria by lactoferrin and other iron-chelating agents. Biochim. Biophys. Acta 170:351-365.
    • (1968) Biochim. Biophys. Acta , vol.170 , pp. 351-365
    • Oram, J.D.1    Reiter, B.2
  • 36
    • 0025066842 scopus 로고
    • Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins
    • Skerlavaj, B., D. Romeo, and R. Gennaro. 1990. Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins. Infect. Immun. 58:3724-3730.
    • (1990) Infect. Immun. , vol.58 , pp. 3724-3730
    • Skerlavaj, B.1    Romeo, D.2    Gennaro, R.3
  • 37
    • 0020079526 scopus 로고
    • The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities
    • Terwilliger, T. C., L. Weissman, and D. Eisenberg. 1982. The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities. Biophys. J. 37:353-361.
    • (1982) Biophys. J. , vol.37 , pp. 353-361
    • Terwilliger, T.C.1    Weissman, L.2    Eisenberg, D.3
  • 38
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi, K., M. Tomita, T. J. Giehl, and R. T. Ellison III. 1993. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61:719-728.
    • (1993) Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison III, R.T.4
  • 39
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. 1987. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84:5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.