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Volumn 53, Issue 5, 2004, Pages 750-758

In vitro synergic antifungal effect of MUC7 12-mer with histatin-5 12-mer or miconazole

Author keywords

Antimicrobial peptides; Chequerboard assay; Combination; Haemolysis; Salivary mucin

Indexed keywords

ALANYLLYSYLARGINYLHISTIDYLHISTIDYLGLYCYLTYROSILYLLYSYLARGINYLLYSYLPHENYLALANYLHISTIDINE; AMPHOTERICIN B; ARGINYLLYSYLSERYLTYROSILYLLYSYLCYSTYLHISTIDINYLLYSYLARGINYLCYSTYLARGININE; HISTATIN; MICONAZOLE; MUCIN 7; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 2442719004     PISSN: 03057453     EISSN: None     Source Type: Journal    
DOI: 10.1093/jac/dkh181     Document Type: Article
Times cited : (46)

References (46)
  • 1
    • 0031969879 scopus 로고    scopus 로고
    • Clinical, cellular, and molecular factors that contribute to antifungal drug resistance
    • White, T. C., Marr, K. A. & Bowden, R. A. (1998). Clinical, cellular, and molecular factors that contribute to antifungal drug resistance. Clinical Microbiology Reviews 11, 382-402.
    • (1998) Clinical Microbiology Reviews , vol.11 , pp. 382-402
    • White, T.C.1    Marr, K.A.2    Bowden, R.A.3
  • 3
    • 2442638337 scopus 로고    scopus 로고
    • Antifungal prophylaxis: An ounce of prevention is worth three grams of amphotericin B
    • [Online] (16 March 2004, date last accessed)
    • Ostrosky-Zeichner, L. & Rex, J. H. (2002). Antifungal prophylaxis: an ounce of prevention is worth three grams of amphotericin B. [Online] http://www.medscape.com (16 March 2004, date last accessed).
    • (2002)
    • Ostrosky-Zeichner, L.1    Rex, J.H.2
  • 4
    • 0031742198 scopus 로고    scopus 로고
    • Antifungal agents. Part I. Amphotericin B preparations and flucytosine
    • Patel, R. (1998). Antifungal agents. Part I. Amphotericin B preparations and flucytosine. Mayo Clinic Proceedings 73, 1205-25.
    • (1998) Mayo Clinic Proceedings , vol.73 , pp. 1205-1225
    • Patel, R.1
  • 5
    • 0033106434 scopus 로고    scopus 로고
    • The changing face of nosocomial candidemia: Epidemiology, resistance, and drug therapy
    • quiz 534-35
    • Lewis, R. E. & Klepser, M. E. (1999). The changing face of nosocomial candidemia: epidemiology, resistance, and drug therapy. American Journal of Health System Pharmacy 56, 525-33; quiz 534-35.
    • (1999) American Journal of Health System Pharmacy , vol.56 , pp. 525-533
    • Lewis, R.E.1    Klepser, M.E.2
  • 6
    • 0037098680 scopus 로고    scopus 로고
    • Antifungal chemotherapy: Advances and perspectives
    • Groll, A. H. & Walsh, T. J. (2002). Antifungal chemotherapy: advances and perspectives. Swiss Medical Weekly 132, 303-11.
    • (2002) Swiss Medical Weekly , vol.132 , pp. 303-311
    • Groll, A.H.1    Walsh, T.J.2
  • 7
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock, R. E. (1997). Peptide antibiotics. Lancet 349, 418-22.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 9
    • 0036895275 scopus 로고    scopus 로고
    • Synthetic peptides that exert antimicrobial activities in whole blood and blood-derived matrices
    • Yeaman, M. R., Gank, K. D., Bayer, A. S. et al, (2002). Synthetic peptides that exert antimicrobial activities in whole blood and blood-derived matrices. Antimicrobial Agents and Chemotherapy 46, 3883-91.
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , pp. 3883-3891
    • Yeaman, M.R.1    Gank, K.D.2    Bayer, A.S.3
  • 10
    • 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., Xu, T., McMillian, F. M. et al. (1988). Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. Journal of Biological Chemistry 263, 7472-7.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3
  • 11
    • 0025733707 scopus 로고
    • Anticandidal activity of major human salivary histatins
    • Xu, T., Levitz, S. M., Diamond, R. D. et al. (11991). Anticandidal activity of major human salivary histatins. Infection and Immunity 59, 2549-54.
    • (1991) Infection and Immunity , vol.59 , pp. 2549-2554
    • Xu, T.1    Levitz, S.M.2    Diamond, R.D.3
  • 12
    • 0030670607 scopus 로고    scopus 로고
    • Human salivary histatin-5 exerts potent fungicidal activity against Cryptococcus neoformans
    • Tsai, H. & Bobek, L. A. (1997). Human salivary histatin-5 exerts potent fungicidal activity against Cryptococcus neoformans. Biochimica et Biophysica Acta 1336, 367-9.
    • (1997) Biochimica et Biophysica Acta , vol.1336 , pp. 367-369
    • Tsai, H.1    Bobek, L.A.2
  • 13
    • 0032979798 scopus 로고    scopus 로고
    • Amphotericin B- and fluconazole-resistant Candida spp., Aspergillus fumigatus, and other newly emerging pathogenic fungi are susceptible to basic antifungal peptides
    • Helmerhorst, E. J., Reijnders, I. M., van't Hof, W. et al. (1999). Amphotericin B- and fluconazole-resistant Candida spp., Aspergillus fumigatus, and other newly emerging pathogenic fungi are susceptible to basic antifungal peptides. Antimicrobial Agents and Chemotherapy 43, 702-4.
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , pp. 702-704
    • Helmerhorst, E.J.1    Reijnders, I.M.2    van't Hof, W.3
  • 14
    • 0035032562 scopus 로고    scopus 로고
    • Anticandida activity is retained in P-113, a 12-amino-acid fragment of histatin 5
    • Rothstein, D. M., Spacciapoli, P., Tran, L. T. et al. (2001). Anticandida activity is retained in P-113, a 12-amino-acid fragment of histatin 5. Antimicrobial Agents and Chemotherapy 45, 1367-73.
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , pp. 1367-1373
    • Rothstein, D.M.1    Spacciapoli, P.2    Tran, L.T.3
  • 15
    • 0032319580 scopus 로고    scopus 로고
    • Human salivary histatins: Promising antifungal therapeutic agents
    • Tsai, H., & Bobek, L. A. (1998). Human salivary histatins: promising antifungal therapeutic agents. Critical Reviews in Oral Biology and Medicine 9, 480-97.
    • (1998) Critical Reviews in Oral Biology and Medicine , vol.9 , pp. 480-497
    • Tsai, H.1    Bobek, L.A.2
  • 16
    • 0033784572 scopus 로고    scopus 로고
    • Divergent solid-phase synthesis and candidacidal activity of MUC7 D1, a 51-residue histidine-rich N-terminal domain of human salivary mucin MUC7
    • Satyanarayana, J., Situ, H., Narasimhamurthy, S. et al. (2000). Divergent solid-phase synthesis and candidacidal activity of MUC7 D1, a 51-residue histidine-rich N-terminal domain of human salivary mucin MUC7. Journal of Peptide Research 56, 275-82.
    • (2000) Journal of Peptide Research , vol.56 , pp. 275-282
    • Satyanarayana, J.1    Situ, H.2    Narasimhamurthy, S.3
  • 17
    • 0141952263 scopus 로고    scopus 로고
    • Human salivary MUC7 mucin peptides: Effect of size, charge, and cysteine residues on antifungal activity
    • Bobek, L. A., Mashhoon, S. & Situ, H. (2002). Human salivary MUC7 mucin peptides: effect of size, charge, and cysteine residues on antifungal activity. Journal of Dental Research 81, 236.
    • (2002) Journal of Dental Research , vol.81 , pp. 236
    • Bobek, L.A.1    Mashhoon, S.2    Situ, H.3
  • 18
    • 0037311494 scopus 로고    scopus 로고
    • MUC7 20-mer: Investigation of antimicrobial activity, secondary structure and possible mechanism of antifungal action
    • Bobek, L. A. & Situ, H. (2003). MUC7 20-mer: investigation of antimicrobial activity, secondary structure and possible mechanism of antifungal action. Antimicrobial Agents and Chemotherapy 47, 645-52.
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , pp. 645-652
    • Bobek, L.A.1    Situ, H.2
  • 19
    • 0032952474 scopus 로고    scopus 로고
    • A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides
    • Helmerhorst, E. J., Reijnders, I. M., van't Hof, W. et al. (1999). A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides. FEBS Letters 449, 105-10.
    • (1999) FEBS Letters , vol.449 , pp. 105-110
    • Helmerhorst, E.J.1    Reijnders, I.M.2    van't Hof, W.3
  • 20
    • 0034128892 scopus 로고    scopus 로고
    • In vitro assessment of antifungal therapeutic potential of salivary histatin-5, two variants of histatin-5, and salivary mucin (MUC7) domain 1
    • Situ, H. & Bobek, L. A. (2000). In vitro assessment of antifungal therapeutic potential of salivary histatin-5, two variants of histatin-5, and salivary mucin (MUC7) domain 1. Antimicrobial Agents and Chemotherapy 44, 1485-93.
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , pp. 1485-1493
    • Situ, H.1    Bobek, L.A.2
  • 21
    • 0030953570 scopus 로고    scopus 로고
    • Antifungal agents in the 1990s. Current status and future developments
    • Kauffman, C. A. & Carver, P. L. (1997). Antifungal agents in the 1990s. Current status and future developments. Drugs 53, 539-49.
    • (1997) Drugs , vol.53 , pp. 539-549
    • Kauffman, C.A.1    Carver, P.L.2
  • 22
    • 0029843859 scopus 로고    scopus 로고
    • Group of peptides that act synergistically with hydrophobic antibiotics against gram-negative enteric bacteria
    • Vaara, M. & Porro, M. (1996). Group of peptides that act synergistically with hydrophobic antibiotics against gram-negative enteric bacteria. Antimicrobial Agents and Chemotherapy 40, 1801-5.
    • (1996) Antimicrobial Agents and Chemotherapy , vol.40 , pp. 1801-1805
    • Vaara, M.1    Porro, M.2
  • 23
    • 0034521229 scopus 로고    scopus 로고
    • Synergistic effects of low doses of histatin 5 and its analogues on amphotericin B anti-mycotic activity
    • van't Hof, W., Reijnders, I. M., Helmerhorst, E. J. et al. (2000). Synergistic effects of low doses of histatin 5 and its analogues on amphotericin B anti-mycotic activity. Antonie Van Leeuwenhoek 78, 163-9.
    • (2000) Antonie van Leeuwenhoek , vol.78 , pp. 163-169
    • van't Hof, W.1    Reijnders, I.M.2    Helmerhorst, E.J.3
  • 24
    • 0031039601 scopus 로고    scopus 로고
    • Pneumocandin L-743,872 enhances the activities of amphotericin B and fluconazole against Cryptococcus neoformans in vitro
    • Franzot, S. P. & Casadevall, A. (1997). Pneumocandin L-743,872 enhances the activities of amphotericin B and fluconazole against Cryptococcus neoformans in vitro. Antimicrobial Agents and Chemotherapy 41, 331-6.
    • (1997) Antimicrobial Agents and Chemotherapy , vol.41 , pp. 331-336
    • Franzot, S.P.1    Casadevall, A.2
  • 25
    • 0345593755 scopus 로고    scopus 로고
    • In vitro antifungal activity and cytotoxicity of a novel membrane-active peptide
    • Hong, S. Y., Oh, J. E. & Lee, K. H. (1999). In vitro antifungal activity and cytotoxicity of a novel membrane-active peptide. Antimicrobial Agents and Chemotherapy 43, 1704-7.
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , pp. 1704-1707
    • Hong, S.Y.1    Oh, J.E.2    Lee, K.H.3
  • 26
    • 0035083899 scopus 로고    scopus 로고
    • A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils
    • Ueta, E., Tanida, T. & Osaki, T. (2001). A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils. Journal of Peptide Research 57, 240-9.
    • (2001) Journal of Peptide Research , vol.57 , pp. 240-249
    • Ueta, E.1    Tanida, T.2    Osaki, T.3
  • 27
    • 0037228719 scopus 로고    scopus 로고
    • Synergistic activity of the N-terminal peptide of human lactoferrin and fluconazole against Candida species
    • Lupetti, A., Paulusma-Annema, A., Welling, M. M. et al. (2003). Synergistic activity of the N-terminal peptide of human lactoferrin and fluconazole against Candida species. Antimicrobial Agents and Chemotherapy 47, 262-7.
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , pp. 262-267
    • Lupetti, A.1    Paulusma-Annema, A.2    Welling, M.M.3
  • 28
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan, H. & Hancock, R. E. (2001). Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrobial Agents and Chemotherapy 45, 1558-60.
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.2
  • 29
    • 0141919277 scopus 로고    scopus 로고
    • Human salivary MUC7 mucin peptides: Effect of size, charge and cysteine residues on antifungal activity
    • Situ, H., Wei, G., Smith, C. J. et al. (2003). Human salivary MUC7 mucin peptides: effect of size, charge and cysteine residues on antifungal activity. Biochemical Journal 375, 175-82.
    • (2003) Biochemical Journal , vol.375 , pp. 175-182
    • Situ, H.1    Wei, G.2    Smith, C.J.3
  • 30
    • 0030984095 scopus 로고    scopus 로고
    • Synthetic histatin analogues with broad-spectrum antimicrobial activity
    • Helmerhorst, E. J., Van't Hof, W., Veerman, E. C. et al. (1997). Synthetic histatin analogues with broad-spectrum antimicrobial activity. Biochemical Journal 326, 39-45.
    • (1997) Biochemical Journal , vol.326 , pp. 39-45
    • Helmerhorst, E.J.1    Van't Hof, W.2    Veerman, E.C.3
  • 31
    • 0035366506 scopus 로고    scopus 로고
    • Effects of histatin 5 and derived peptides on Candida albicans
    • Ruissen, A. L., Groenink, J., Helmerhorst, E. J. et al. (2001). Effects of histatin 5 and derived peptides on Candida albicans. Biochemical Journal 356, 361-8.
    • (2001) Biochemical Journal , vol.356 , pp. 361-368
    • Ruissen, A.L.1    Groenink, J.2    Helmerhorst, E.J.3
  • 32
    • 0002515716 scopus 로고    scopus 로고
    • Antimicrobial combinations
    • 4th edn (Lorian, V., Ed), Williams & Wilkins, Baltimore, MD, USA
    • Eliopoulos, G. M. & Moellering, T. C. (1996). Antimicrobial combinations. In Antibiotics in Laboratory Medicine, 4th edn (Lorian, V., Ed), pp. 330-96. Williams & Wilkins, Baltimore, MD, USA.
    • (1996) Antibiotics in Laboratory Medicine , pp. 330-396
    • Eliopoulos, G.M.1    Moellering, T.C.2
  • 33
    • 0038601510 scopus 로고    scopus 로고
    • Synergy, antagonism, and what the chequerboard puts between them
    • Odds, F. C. (2003). Synergy, antagonism, and what the chequerboard puts between them. Journal of Antimicrobial Chemotherapy 52, 1.
    • (2003) Journal of Antimicrobial Chemotherapy , vol.52 , pp. 1
    • Odds, F.C.1
  • 34
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R. E. & Lehrer, R. (1998). Cationic peptides: a new source of antibiotics. Trends in Biotechnology 16, 82-8.
    • (1998) Trends in Biotechnology , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 35
    • 0032528858 scopus 로고    scopus 로고
    • Identification and characterization of the antimicrobial peptide corresponding to C-terminal beta-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor
    • Lee, K. H., Hong, S. Y., Oh, J. E. et al. (1998). Identification and characterization of the antimicrobial peptide corresponding to C-terminal beta-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor. Biochemical Journal 334, 99-105.
    • (1998) Biochemical Journal , vol.334 , pp. 99-105
    • Lee, K.H.1    Hong, S.Y.2    Oh, J.E.3
  • 36
    • 0034425782 scopus 로고    scopus 로고
    • Candidacidal activities of human lactoferrin peptides derived from the N terminus
    • Lupetti, A., Paulusma-Annema, A., Welling, M. M. et al. (2000). Candidacidal activities of human lactoferrin peptides derived from the N terminus. Antimicrobial Agents and Chemotherapy 44, 3257-63.
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , pp. 3257-3263
    • Lupetti, A.1    Paulusma-Annema, A.2    Welling, M.M.3
  • 37
    • 0036445391 scopus 로고    scopus 로고
    • Antimicrobial activity and stability to proteolysis of small linear cationic peptides with D-amino acid substitutions
    • Hamamoto, K., Kida, Y., Zhang, Y. et al. (2002). Antimicrobial activity and stability to proteolysis of small linear cationic peptides with D-amino acid substitutions. Microbiology and Immunology 46, 741-9.
    • (2002) Microbiology and Immunology , vol.46 , pp. 741-749
    • Hamamoto, K.1    Kida, Y.2    Zhang, Y.3
  • 38
    • 0032493760 scopus 로고    scopus 로고
    • Candidacidal activity of salivary histatins. Identification of a histatin 5-binding protein on Candida albicans
    • Edgerton, M., Koshlukova, S. E., Lo, T. E. et al. (1998). Candidacidal activity of salivary histatins. Identification of a histatin 5-binding protein on Candida albicans. Journal of Biological Chemistry 273, 20438-47.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 20438-20447
    • Edgerton, M.1    Koshlukova, S.E.2    Lo, T.E.3
  • 39
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • Tossi, A., Sandri, L. & Giangaspero, A. (2000). Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55, 4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 40
    • 0034824532 scopus 로고    scopus 로고
    • The effect of charge increase on the specificity and activity of a short antimicrobial peptide
    • Hong, S. Y., Park, T. G. & Lee, K. H. (2001). The effect of charge increase on the specificity and activity of a short antimicrobial peptide. Peptides 22, 1669-74.
    • (2001) Peptides , vol.22 , pp. 1669-1674
    • Hong, S.Y.1    Park, T.G.2    Lee, K.H.3
  • 41
    • 0030896419 scopus 로고    scopus 로고
    • Cellular charge of Cryptococcus neoformans: Contributions from the capsular polysaccharide, melanin, and monoclonal antibody binding
    • Nosanchuk, J. D. & Casadevall, A. (1997). Cellular charge of Cryptococcus neoformans: contributions from the capsular polysaccharide, melanin, and monoclonal antibody binding. Infection and Immunity 65, 1836-41.
    • (1997) Infection and Immunity , vol.65 , pp. 1836-1841
    • Nosanchuk, J.D.1    Casadevall, A.2
  • 42
    • 0036166413 scopus 로고    scopus 로고
    • Antimicrobial peptides: Therapeutic potential for the treatment of Candida infections
    • Nibbering, P. H., Danesi, R., van't Wout, J. W. et al. (2002). Antimicrobial peptides: therapeutic potential for the treatment of Candida infections. Expert Opinion on Investigational Drugs 11, 309-18.
    • (2002) Expert Opinion on Investigational Drugs , vol.11 , pp. 309-318
    • Nibbering, P.H.1    Danesi, R.2    van't Wout, J.W.3
  • 43
    • 0033548487 scopus 로고    scopus 로고
    • The cellular target of histatin 5 on Candida albicans is the energized mitochondrion
    • Helmerhorst, E. J., Breeuwer, P., van't Hof, W. et al. (1999). The cellular target of histatin 5 on Candida albicans is the energized mitochondrion. Journal of Biological Chemistry 274, 7286-91.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 7286-7291
    • Helmerhorst, E.J.1    Breeuwer, P.2    van't Hof, W.3
  • 44
    • 0030863427 scopus 로고    scopus 로고
    • Studies of the mechanism of human salivary histatin-5 candidacidal activity with histatin-5 variants and azole-sensitive and -resistant Candida species
    • Tsai, H. & Bobek, L. A. (1997). Studies of the mechanism of human salivary histatin-5 candidacidal activity with histatin-5 variants and azole-sensitive and -resistant Candida species. Antimicrobial Agents and Chemotherapy 41, 2224-8.
    • (1997) Antimicrobial Agents and Chemotherapy , vol.41 , pp. 2224-2228
    • Tsai, H.1    Bobek, L.A.2
  • 45
    • 0037194346 scopus 로고    scopus 로고
    • Design of novel analogue peptides with potent antibiotic activity based on the antimicrobial peptide, HP (2-20), derived from N-terminus of Helicobacter pylori ribosomal protein L1
    • Lee, D. G., Kim, H. N., Park, Y. et al. (2002). Design of novel analogue peptides with potent antibiotic activity based on the antimicrobial peptide, HP (2-20), derived from N-terminus of Helicobacter pylori ribosomal protein L1. Biochimica et Biophysica Acta 1598, 185-94.
    • (2002) Biochimica et Biophysica Acta , vol.1598 , pp. 185-194
    • Lee, D.G.1    Kim, H.N.2    Park, Y.3
  • 46
    • 0037179619 scopus 로고    scopus 로고
    • Antimicrobial peptides: Synthesis and antibacterial activity of linear and cyclic drosocin and apidaecin 1b analogues
    • Gobbo, M., Biondi, L., Filira, F. et al. (2002). Antimicrobial peptides: synthesis and antibacterial activity of linear and cyclic drosocin and apidaecin 1b analogues. Journal of Medicinal Chemistry 45, 4494-504.
    • (2002) Journal of Medicinal Chemistry , vol.45 , pp. 4494-4504
    • Gobbo, M.1    Biondi, L.2    Filira, F.3


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