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Volumn 50, Issue 8, 2006, Pages 2797-2805

Synthetic histidine-rich peptides inhibit Candida species and other fungi in vitro: Role of endocytosis and treatment implications

Author keywords

[No Author keywords available]

Indexed keywords

4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; ANTIFUNGAL AGENT; BAFILOMYCIN A1; HISTATIN; HISTATIN 5; HISTIDINE; LYSINE; NUCLEIC ACID;

EID: 33746917547     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.00411-06     Document Type: Article
Times cited : (34)

References (45)
  • 1
    • 0035215744 scopus 로고    scopus 로고
    • Genetically engineered human salivary histatin genes are functional in Candida albicans: Development of a new system for studying histatin candidacidal activity
    • Baev, D., X. Li, and M. Edgerton. 2001. Genetically engineered human salivary histatin genes are functional in Candida albicans: development of a new system for studying histatin candidacidal activity. Microbiology 147:3323-3334.
    • (2001) Microbiology , vol.147 , pp. 3323-3334
    • Baev, D.1    Li, X.2    Edgerton, M.3
  • 2
    • 0038444053 scopus 로고    scopus 로고
    • Killing of Candida albicans by human salivary histatin 5 is modulated, but not determined, by the potassium channel TOK1
    • Baev, D., A. Rivetta, X. S. Li, S. Vylkova, E. Bashi, C. L. Slayman, and M. Edgerton. 2003. Killing of Candida albicans by human salivary histatin 5 is modulated, but not determined, by the potassium channel TOK1. Infect. Immun. 71:3251-3260.
    • (2003) Infect. Immun. , vol.71 , pp. 3251-3260
    • Baev, D.1    Rivetta, A.2    Li, X.S.3    Vylkova, S.4    Bashi, E.5    Slayman, C.L.6    Edgerton, M.7
  • 3
    • 11244278605 scopus 로고    scopus 로고
    • The TRK1 potassium transporter is the critical effector for killing of Candida albicans by the cationic protein, histatin 5
    • Baev, D., A. Rivetta, S. Vylkova, J. N. Sun, G. F. Zeng, C. L. Slayman, and M. Edgerton. 2004. The TRK1 potassium transporter is the critical effector for killing of Candida albicans by the cationic protein, histatin 5. J. Biol. Chem. 279:55060-55072.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55060-55072
    • Baev, D.1    Rivetta, A.2    Vylkova, S.3    Sun, J.N.4    Zeng, G.F.5    Slayman, C.L.6    Edgerton, M.7
  • 5
    • 0037040244 scopus 로고    scopus 로고
    • Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site
    • Bowman, B. J., and E. J. Bowman. 2002. Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site. J. Biol. Chem. 277:3965-3972.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3965-3972
    • Bowman, B.J.1    Bowman, E.J.2
  • 6
    • 4043065767 scopus 로고    scopus 로고
    • The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae
    • Bowman, E. J., L. A. Graham, T. H. Stevens, and B. J. Bowman. 2004. The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae. J. Biol. Chem. 279:33131-33138.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33131-33138
    • Bowman, E.J.1    Graham, L.A.2    Stevens, T.H.3    Bowman, B.J.4
  • 7
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman, E. J., A. Siebers, and K. Altendorf. 1988. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. USA 85:7972-7976.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 8
    • 0037085731 scopus 로고    scopus 로고
    • Optimal transfection with the HK polymer depends on its degree of branching and the pH of endocytic vesicles
    • Chen, Q. R., L. Zhang, P. W. Luther, and A. J. Mixson. 2002. Optimal transfection with the HK polymer depends on its degree of branching and the pH of endocytic vesicles. Nucleic Acids Res. 30:1338-1345.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1338-1345
    • Chen, Q.R.1    Zhang, L.2    Luther, P.W.3    Mixson, A.J.4
  • 9
    • 0035869214 scopus 로고    scopus 로고
    • Branched co-polymers of histidine and lysine are efficient carriers of plasmids
    • Chen, Q. R., L. Zhang, S. A. Stass, and A. J. Mixson. 2001. Branched co-polymers of histidine and lysine are efficient carriers of plasmids. Nucleic Acids Res. 29:1334-1340.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1334-1340
    • Chen, Q.R.1    Zhang, L.2    Stass, S.A.3    Mixson, A.J.4
  • 10
    • 0033759241 scopus 로고    scopus 로고
    • Co-polymer of histidine and lysine markedly enhances transfection efficiency of liposomes
    • Chen, Q. R., L. Zhang, S. A. Stass, and A. J. Mixson. 2000. Co-polymer of histidine and lysine markedly enhances transfection efficiency of liposomes. Gene Ther. 7:1698-1705.
    • (2000) Gene Ther. , vol.7 , pp. 1698-1705
    • Chen, Q.R.1    Zhang, L.2    Stass, S.A.3    Mixson, A.J.4
  • 12
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • Dathe, M., and T. Wieprecht. 1999. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462:71-87.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 13
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R. M., and H. J. Vogel. 1999. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462:11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 15
    • 0014095983 scopus 로고
    • The use of computed optical rotatory dispersion curves for the evaluation of protein conformation
    • Greenfield, N., B. Davidson, and G. D. Fasman. 1967. The use of computed optical rotatory dispersion curves for the evaluation of protein conformation. Biochemistry 6:1630-1637.
    • (1967) Biochemistry , vol.6 , pp. 1630-1637
    • Greenfield, N.1    Davidson, B.2    Fasman, G.D.3
  • 17
    • 0032916291 scopus 로고    scopus 로고
    • Host defence (cationic) peptides: What is their future clinical potential?
    • Hancock, R. E. 1999. Host defence (cationic) peptides: what is their future clinical potential? Drugs 57:469-473.
    • (1999) Drugs , vol.57 , pp. 469-473
    • Hancock, R.E.1
  • 18
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R. E., and R. Lehrer. 1998. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16:82-88.
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 19
    • 0035937109 scopus 로고    scopus 로고
    • Characterization of histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation
    • Helmerhorst, E. J., W. van't Hof, P. Breeuwer, E. C. Veerman, T. Abee, R. F. Troxler, A. V. Amerongen, and F. G. Oppenheim. 2001. Characterization of histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation. J. Biol. Chem. 276:5643-5649.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5643-5649
    • Helmerhorst, E.J.1    Van't Hof, W.2    Breeuwer, P.3    Veerman, E.C.4    Abee, T.5    Troxler, R.F.6    Amerongen, A.V.7    Oppenheim, F.G.8
  • 20
    • 0033538328 scopus 로고    scopus 로고
    • Direct detection of a histidine-histidine side chain hydrogen bond important for folding of apomyoglobin
    • Henig, M., and B. Geierstanger. 1999. Direct detection of a histidine-histidine side chain hydrogen bond important for folding of apomyoglobin. J. Am. Chem. Soc. 121:5123-5126.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5123-5126
    • Henig, M.1    Geierstanger, B.2
  • 22
    • 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
  • 23
    • 0032738066 scopus 로고    scopus 로고
    • Simulation studies of the interaction of antimicrobial peptides and lipid bilayers
    • La Rocca, P., P. C. Biggin, D. P. Tieleman, and M. S. Sansom. 1999. Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. Biochim. Biophys. Acta 1462:185-200.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 185-200
    • La Rocca, P.1    Biggin, P.C.2    Tieleman, D.P.3    Sansom, M.S.4
  • 24
    • 26644469058 scopus 로고    scopus 로고
    • Modified branched peptides with a histidine-rich tail enhance in vitro gene transfection
    • Leng, Q., and A. J. Mixson. 2005. Modified branched peptides with a histidine-rich tail enhance in vitro gene transfection. Nucleic Acids Res. 33:e40.
    • (2005) Nucleic Acids Res. , vol.33
    • Leng, Q.1    Mixson, A.J.2
  • 26
    • 0042208078 scopus 로고    scopus 로고
    • Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5
    • Li, X. S., M. S. Reddy, D. Baev, and M. Edgerton. 2003. Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5. J. Biol. Chem. 278:28553-28561.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28553-28561
    • Li, X.S.1    Reddy, M.S.2    Baev, D.3    Edgerton, M.4
  • 28
    • 27744525788 scopus 로고    scopus 로고
    • Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery
    • Massodi, I., G. L. Bidwell III, and D. Raucher. 2005. Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery. J. Control Release 108:396-408.
    • (2005) J. Control Release , vol.108 , pp. 396-408
    • Massodi, I.1    Bidwell III, G.L.2    Raucher, D.3
  • 29
    • 0033948397 scopus 로고    scopus 로고
    • IB-367, a protegrin peptide with in vitro and in vivo activities against the microflora associated with oral mucositis
    • Mosca, D. A., M. A. Hurst, W. So, B. S. Viajar, C. A. Fujii, and T. J. Falla. 2000. IB-367, a protegrin peptide with in vitro and in vivo activities against the microflora associated with oral mucositis. Antimicrob. Agents Chemother. 44:1803-1808.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1803-1808
    • Mosca, D.A.1    Hurst, M.A.2    So, W.3    Viajar, B.S.4    Fujii, C.A.5    Falla, T.J.6
  • 30
  • 31
    • 84984084377 scopus 로고
    • Some optical properties of poly-L-bennyl-L-histidine and poly-L-histidine
    • Norland, K. S., G. D. Gasman, E. Katchalsky, and E. R. Blout. 1963. Some optical properties of poly-L-bennyl-L-histidine and poly-L-histidine. Biopolymers 1:277-294.
    • (1963) Biopolymers , vol.1 , pp. 277-294
    • Norland, K.S.1    Gasman, G.D.2    Katchalsky, E.3    Blout, E.R.4
  • 32
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans
    • Oppenheim, F. G., T. Xu, F. M. McMillian, S. M. Levitz, R. D. Diamond, G. D. Offner, and R. F. Troxler. 1988. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J. Biol. Chem. 263:7472-7477.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3    Levitz, S.M.4    Diamond, R.D.5    Offner, G.D.6    Troxler, R.F.7
  • 35
    • 0036701581 scopus 로고    scopus 로고
    • Insights from yeast endosomes
    • Pelham, H. R. 2002. Insights from yeast endosomes. Curr. Opin. Cell Biol. 14:454-462.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 454-462
    • Pelham, H.R.1
  • 38
    • 0027430001 scopus 로고
    • Three clathrin-dependent budding steps and cell polarity
    • Riezman, H. 1993. Three clathrin-dependent budding steps and cell polarity. Trends Cell Biol. 3:330-332.
    • (1993) Trends Cell Biol. , vol.3 , pp. 330-332
    • Riezman, H.1
  • 39
    • 26444593299 scopus 로고    scopus 로고
    • Invasive candidiasis in immunocompromised hospitalized patients
    • Sims, C. R., L. Ostrosky-Zeichner, and J. H. Rex. 2005. Invasive candidiasis in immunocompromised hospitalized patients. Arch. Med. Res. 36:660-671.
    • (2005) Arch. Med. Res. , vol.36 , pp. 660-671
    • Sims, C.R.1    Ostrosky-Zeichner, L.2    Rex, J.H.3
  • 40
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity
    • Sitaram, N., and R. Nagaraj. 1999. Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity. Biochim. Biophys. Acta 1462:29-54.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 41
    • 0030623934 scopus 로고    scopus 로고
    • Designer assays for antimicrobial peptides. Disputing the "one-size-fits-all" theory
    • Steinberg, D. A., and R. I. Lehrer. 1997. Designer assays for antimicrobial peptides. Disputing the "one-size-fits-all" theory. Methods Mol. Biol. 78:169-186.
    • (1997) Methods Mol. Biol. , vol.78 , pp. 169-186
    • Steinberg, D.A.1    Lehrer, R.I.2
  • 42
    • 0032319580 scopus 로고    scopus 로고
    • Human salivary histatins: Promising antifungal therapeutic agents
    • Tsai, H., and L. A. Bobek. 1998. Human salivary histatins: promising antifungal therapeutic agents. Crit. Rev. Oral Biol. Med. 9:480-497.
    • (1998) Crit. Rev. Oral Biol. Med. , vol.9 , pp. 480-497
    • Tsai, H.1    Bobek, L.A.2
  • 43
    • 28844433952 scopus 로고    scopus 로고
    • Subunit a of the yeast V-ATPase participates in binding of bafilomycin
    • Wang, Y., T. Inoue, and M. Forgac. 2005. Subunit a of the yeast V-ATPase participates in binding of bafilomycin. J. Biol. Chem. 280:40481-40488.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40481-40488
    • Wang, Y.1    Inoue, T.2    Forgac, M.3
  • 44
  • 45
    • 1342287828 scopus 로고    scopus 로고
    • DNA delivery to cells in culture using peptides
    • Zhang, L., N. Ambulos, and A. J. Mixson. 2004. DNA delivery to cells in culture using peptides. Methods Mol. Biol. 245:33-52.
    • (2004) Methods Mol. Biol. , vol.245 , pp. 33-52
    • Zhang, L.1    Ambulos, N.2    Mixson, A.J.3


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