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Volumn 49, Issue 7, 2005, Pages 2583-2588

Different anti-Candida activities of two human lactoferrin-derived peptides, Lfpep and kaliocin-1

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOTERICIN B; ANTIINFECTIVE AGENT; BREVININ 1SA; FLUCONAZOLE; KALIOCIN 1; LACTOFERRICIN H; LACTOFERRIN; PROPIDIUM IODIDE; PROTEIN LFPEP; SYNTHETIC PEPTIDE; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 21444435350     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.49.7.2583-2588.2005     Document Type: Article
Times cited : (63)

References (36)
  • 1
    • 0032697965 scopus 로고    scopus 로고
    • Permeabilizing action of an antimicrobial lactoferricin-derived peptide on bacterial and artificial membranes
    • Aguilera, O., H. Ostolaza, L. M. Quirós, and J. F. Fierro. 1999. Permeabilizing action of an antimicrobial lactoferricin-derived peptide on bacterial and artificial membranes. FEBS Lett. 462:273-277.
    • (1999) FEBS Lett. , vol.462 , pp. 273-277
    • Aguilera, O.1    Ostolaza, H.2    Quirós, L.M.3    Fierro, J.F.4
  • 2
    • 0342715103 scopus 로고    scopus 로고
    • P-type ATPases mediate sodium and potassium effluxes in Schwanniomyces occidentalis
    • Bañuelos, M. A., and A. Rodríguez-Navarro. 1998. P-type ATPases mediate sodium and potassium effluxes in Schwanniomyces occidentalis. J. Biol. Chem. 273:1640-1646.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1640-1646
    • Bañuelos, M.A.1    Rodríguez-Navarro, A.2
  • 5
    • 0027428420 scopus 로고
    • Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis
    • Britigan, B. E., M. B. Hayek, B. N. Doebbeling, and R. B. Fick Jr. 1993. Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis. Infect. Immun. 61:5049-5055.
    • (1993) Infect. Immun. , vol.61 , pp. 5049-5055
    • Britigan, B.E.1    Hayek, M.B.2    Doebbeling, B.N.3    Fick Jr., R.B.4
  • 6
    • 0031842041 scopus 로고
    • Activity of protegrins against yeast-phase Candida albicans
    • Cho, Y., J. S. Turner, N. N. Dinh, and R. I. Lehrer. 1988. Activity of protegrins against yeast-phase Candida albicans. Infect. Immun. 66:2486-2493.
    • (1988) Infect. Immun. , vol.66 , pp. 2486-2493
    • Cho, Y.1    Turner, J.S.2    Dinh, N.N.3    Lehrer, R.I.4
  • 7
    • 0032714837 scopus 로고    scopus 로고
    • Peptides with antimicrobial activity of the brevinin-1 family isolated from skin secretions of the southern leopard frog, Rana sphenocephala
    • Conlon, J. M., T. Halverson, J. Dulka, J. E. Platz, and F. C. Knop. 1999. Peptides with antimicrobial activity of the brevinin-1 family isolated from skin secretions of the southern leopard frog, Rana sphenocephala. J. Pept. Res. 54:522-527.
    • (1999) J. Pept. Res. , vol.54 , pp. 522-527
    • Conlon, J.M.1    Halverson, T.2    Dulka, J.3    Platz, J.E.4    Knop, F.C.5
  • 8
    • 0242364776 scopus 로고    scopus 로고
    • Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii
    • Conlon, J. M., Á. Sonnevend, M. Patel, C. Davidson, P. F. Nielsen, T. Pál, and L. A. Rollins-Smith. 2003. Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii. J. Pept. Res. 62:207-213.
    • (2003) J. Pept. Res. , vol.62 , pp. 207-213
    • Conlon, J.M.1    Sonnevend, Á.2    Patel, M.3    Davidson, C.4    Nielsen, P.F.5    Pál, T.6    Rollins-Smith, L.A.7
  • 9
    • 0141918814 scopus 로고    scopus 로고
    • Antimicrobial peptides in defence of the oral and respiratory tracts
    • Devine, D. A. 2003. Antimicrobial peptides in defence of the oral and respiratory tracts. Mol. Immunol. 40:431-443.
    • (2003) Mol. Immunol. , vol.40 , pp. 431-443
    • Devine, D.A.1
  • 10
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • Dimarcq, J. L., P. Bulet, C. Hetru, and J. Hoffmann. 1998. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers 47:465-477.
    • (1998) Biopolymers , vol.47 , pp. 465-477
    • Dimarcq, J.L.1    Bulet, P.2    Hetru, C.3    Hoffmann, J.4
  • 11
    • 0141918811 scopus 로고    scopus 로고
    • Lactoferrin - A multifunctional protein with antimicrobial properties
    • Farnaud, S., and R. W. Evans. 2003. Lactoferrin - a multifunctional protein with antimicrobial properties. Mol. Immunol. 40:395-405.
    • (2003) Mol. Immunol. , vol.40 , pp. 395-405
    • Farnaud, S.1    Evans, R.W.2
  • 12
    • 0030071417 scopus 로고    scopus 로고
    • Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides
    • Fehlbaum, P., P. Bulet, S. Chernysh, J. P. Briand, J. P. Roussel, L. Letellier, C. Hetru, and J. A. Hoffmann. 1996. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc. Natl. Acad. Sci. USA 93:1221-1225.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1221-1225
    • Fehlbaum, P.1    Bulet, P.2    Chernysh, S.3    Briand, J.P.4    Roussel, J.P.5    Letellier, L.6    Hetru, C.7    Hoffmann, J.A.8
  • 13
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman, M. J., G. M. Anderson, E. D. Stolzenberg, U. P. Kari, M. Zasloff, and J. M. Wilson. 1997. Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88:553-560.
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 15
    • 0347983810 scopus 로고    scopus 로고
    • The global epidemiology of invasive Candida infections - Is the tide turning?
    • Hobson, R. P. 2003. The global epidemiology of invasive Candida infections - is the tide turning? J. Hosp. Infect. 55:159-168.
    • (2003) J. Hosp. Infect. , vol.55 , pp. 159-168
    • Hobson, R.P.1
  • 16
    • 0034910676 scopus 로고    scopus 로고
    • Antifungal resistance among Candida species
    • Klepser, M. E. 2001. Antifungal resistance among Candida species. Pharmacotherapy 21:124-132.
    • (2001) Pharmacotherapy , vol.21 , pp. 124-132
    • Klepser, M.E.1
  • 17
    • 0033516461 scopus 로고    scopus 로고
    • Salivary histatin 5 induces non-lytic release of ATP from Candida albicans leading to cell death
    • Koshlukova, S. E., T. L. Lloyd, M. W. B. Araujo, and M. Edgerton. 1999. Salivary histatin 5 induces non-lytic release of ATP from Candida albicans leading to cell death. J. Biol. Chem. 274:18872-18879.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18872-18879
    • Koshlukova, S.E.1    Lloyd, T.L.2    Araujo, M.W.B.3    Edgerton, M.4
  • 18
    • 0032707616 scopus 로고    scopus 로고
    • Synergistic fungistatic effects of lactoferrin in combination with antifungal drugs against clinical Candida isolates
    • Kuipers, M. E., H. G. de Vries, M. C. Eikelboom, D. K. Meijer, and P. J. Swart. 1999. Synergistic fungistatic effects of lactoferrin in combination with antifungal drugs against clinical Candida isolates. Antimicrob. Agents Chemother. 43:2635-2641.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 2635-2641
    • Kuipers, M.E.1    De Vries, H.G.2    Eikelboom, M.C.3    Meijer, D.K.4    Swart, P.J.5
  • 19
    • 0021847049 scopus 로고
    • Correlation of binding of rabbit granulocyte peptides to Candida albicans with candidacidal activity
    • Lehrer, R. I., D. Szklarek, T. Ganz, and M. E. Selsted. 1985. Correlation of binding of rabbit granulocyte peptides to Candida albicans with candidacidal activity. Infect. Immun. 49:207-211.
    • (1985) Infect. Immun. , vol.49 , pp. 207-211
    • Lehrer, R.I.1    Szklarek, D.2    Ganz, T.3    Selsted, M.E.4
  • 22
    • 0027096816 scopus 로고
    • Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa
    • Morikawa, N., K. Hagiwara, and T. Nakajima. 1992. Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa. Biochem. Biophys. Res. Commun. 189:184-190.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 184-190
    • Morikawa, N.1    Hagiwara, K.2    Nakajima, T.3
  • 24
    • 0035112330 scopus 로고    scopus 로고
    • Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria
    • Nibbering, P. H., E. Ravensbergen, M. M. Welling, L. A. van Berkel, P. H. C. van Berkel, E. K. J. Pauwels, and J. H. Nuijens. 2001. Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria. Infect. Immun. 69:1469-1476.
    • (2001) Infect. Immun. , vol.69 , pp. 1469-1476
    • Nibbering, P.H.1    Ravensbergen, E.2    Welling, M.M.3    Van Berkel, L.A.4    Van Berkel, P.H.C.5    Pauwels, E.K.J.6    Nuijens, J.H.7
  • 25
    • 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
  • 27
    • 0035185146 scopus 로고    scopus 로고
    • P-113D, an antimicrobial peptide active against Pseudomonas aeruginosa, retains activity in the presence of sputum from cystic fibrosis patients
    • Sajjan, U. S., L. T. Tran, N. Sole, C. Rovaldi, A. Akiyama, P. M. Friden, J. F. Forstner, and D. M. Rothstein. 2001. P-113D, an antimicrobial peptide active against Pseudomonas aeruginosa, retains activity in the presence of sputum from cystic fibrosis patients. Antimicrob. Agents Chemother. 45:3437-3444.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 3437-3444
    • Sajjan, U.S.1    Tran, L.T.2    Sole, N.3    Rovaldi, C.4    Akiyama, A.5    Friden, P.M.6    Forstner, J.F.7    Rothstein, D.M.8
  • 28
    • 0034128892 scopus 로고    scopus 로고
    • In vitro assessment of antifungal therapeutic potential of salivary histatin-5, two variants of histatin-5, and salivary mucin (MUC) domain 1
    • Situ, H., and L. A. Bobek. 2000. In vitro assessment of antifungal therapeutic potential of salivary histatin-5, two variants of histatin-5, and salivary mucin (MUC) domain 1. Antimicrob. Agents Chemother. 44:1485-1493.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1485-1493
    • Situ, H.1    Bobek, L.A.2
  • 30
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 31
    • 0028828203 scopus 로고
    • Giardicidal activity of lactoferrin and N-terminal peptides
    • Turchany, J. M., S. B. Aley, and F. D. Gillin. 1995. Giardicidal activity of lactoferrin and N-terminal peptides. Infect. Immun. 63:4550-4552.
    • (1995) Infect. Immun. , vol.63 , pp. 4550-4552
    • Turchany, J.M.1    Aley, S.B.2    Gillin, F.D.3
  • 33
    • 0037303162 scopus 로고    scopus 로고
    • Potassium-efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane
    • Viejo-Díaz, M., M. T. Andrés, J. Pérez-Gil, M. Sánchez, and J. F. Fierro. 2003. Potassium-efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane. Biochemistry (Moscow) 68:217-227.
    • (2003) Biochemistry (Moscow) , vol.68 , pp. 217-227
    • Viejo-Díaz, M.1    Andrés, M.T.2    Pérez-Gil, J.3    Sánchez, M.4    Fierro, J.F.5
  • 34
    • 18344408431 scopus 로고    scopus 로고
    • Modulation of in vitro fungicidal activity of human lactoferrin against Candida albicans by extracellular cation concentration and target cell metabolic activity
    • Viejo-Díaz, M., M. T. Andrés, and J. F. Fierro. 2004. Modulation of in vitro fungicidal activity of human lactoferrin against Candida albicans by extracellular cation concentration and target cell metabolic activity. Antimicrob. Agents Chemother. 48:1242-1248.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1242-1248
    • Viejo-Díaz, M.1    Andrés, M.T.2    Fierro, J.F.3
  • 35
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M. R., and N. Y. Yount. 2003. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55:27-55.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 36
    • 2442515355 scopus 로고    scopus 로고
    • Multidimensional signatures in antimicrobial peptides
    • Yount, N. Y., and M. R. Yeaman. 2004. Multidimensional signatures in antimicrobial peptides. Proc. Natl. Acad. Sci. USA 101:7363-7368.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7363-7368
    • Yount, N.Y.1    Yeaman, M.R.2


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