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Volumn 58, Issue 5, 2006, Pages 950-959

Fungicidal activity of five cathelicidin peptides against clinically isolated yeasts

Author keywords

Antifungals; Cathelicidin; Clinical isolates; Host defence; Immunocompromised patients; Innate immunity; Pathogenic fungi

Indexed keywords

ANTIFUNGAL AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; CAP18 LIPOPOLYSACCHARIDE BINDING PROTEIN; CAP18 LIPOPOLYSACCHARIDE-BINDING PROTEIN;

EID: 39049135214     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkl382     Document Type: Article
Times cited : (124)

References (44)
  • 1
    • 18844392815 scopus 로고    scopus 로고
    • Evaluation and management of fungal infections in immunocompromised patients
    • Venkatesan P, Perfect JR, Myers SA. Evaluation and management of fungal infections in immunocompromised patients. Dermatol Ther 2005; 18: 44-57.
    • (2005) Dermatol Ther , vol.18 , pp. 44-57
    • Venkatesan, P.1    Perfect, J.R.2    Myers, S.A.3
  • 3
    • 10444285332 scopus 로고    scopus 로고
    • Multidrug resistance in yeast Candida
    • Prasad R, Kapoor K. Multidrug resistance in yeast Candida. Int Rev Cytol 2005; 242: 215-48.
    • (2005) Int Rev Cytol , vol.242 , pp. 215-248
    • Prasad, R.1    Kapoor, K.2
  • 4
    • 0036828026 scopus 로고    scopus 로고
    • Antifungal resistance in pathogenic fungi
    • Perea S, Patterson TF. Antifungal resistance in pathogenic fungi. Clin Infect Dis 2002; 35: 1073-80.
    • (2002) Clin Infect Dis , vol.35 , pp. 1073-1080
    • Perea, S.1    Patterson, T.F.2
  • 5
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • Lehrer RI, Ganz T. Defensins of vertebrate animals. Curr Opin Immunol 2002; 14: 96-102.
    • (2002) Curr Opin Immunol , vol.14 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 6
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J Leukoc Biol 2004; 75: 39-48.
    • (2004) J Leukoc Biol , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 7
    • 0033863168 scopus 로고    scopus 로고
    • Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
    • Gennaro R, Zanetti M. Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 2000; 55: 31-49.
    • (2000) Biopolymers , vol.55 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 8
    • 1042278913 scopus 로고    scopus 로고
    • In vitro and in vivo antimicrobial activity of two α-helical cathelicidin peptides and of their synthetic analogs
    • Benincasa M, Skerlavaj B, Gennaro R et al. In vitro and in vivo antimicrobial activity of two α-helical cathelicidin peptides and of their synthetic analogs. Peptides 2003; 24: 1723-31.
    • (2003) Peptides , vol.24 , pp. 1723-1731
    • Benincasa, M.1    Skerlavaj, B.2    Gennaro, R.3
  • 9
    • 0035160960 scopus 로고    scopus 로고
    • The ovine cathelicidin SMAP29 kills ovine respiratory pathogens in vitro and in an ovine model of pulmonary infection
    • Brogden KA, Kalfa VC, Ackermann MR et al. The ovine cathelicidin SMAP29 kills ovine respiratory pathogens in vitro and in an ovine model of pulmonary infection. Antimicrob Agents Chemother 2001; 45: 331-4.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 331-334
    • Brogden, K.A.1    Kalfa, V.C.2    Ackermann, M.R.3
  • 10
    • 10644276256 scopus 로고    scopus 로고
    • The antimicrobial peptide BMAP-28 reduces lethality in mouse models of staphylococcal sepsis
    • Giacometti A, Cirioni O, Ghiselli R et al. The antimicrobial peptide BMAP-28 reduces lethality in mouse models of staphylococcal sepsis. Crit Care Med 2004; 32: 2485-90.
    • (2004) Crit Care Med , vol.32 , pp. 2485-2490
    • Giacometti, A.1    Cirioni, O.2    Ghiselli, R.3
  • 11
    • 9144223625 scopus 로고    scopus 로고
    • Cathelicidin peptide sheep myeloid antimicrobial peptide-29 prevents endotoxin-induced mortality in rat models of septic shock
    • Giacometti A, Cirioni O, Ghiselli R et al. Cathelicidin peptide sheep myeloid antimicrobial peptide-29 prevents endotoxin-induced mortality in rat models of septic shock. Am J Respir Crit Care Med 2004; 169: 187-94.
    • (2004) Am J Respir Crit Care Med , vol.169 , pp. 187-194
    • Giacometti, A.1    Cirioni, O.2    Ghiselli, R.3
  • 12
    • 0033433992 scopus 로고    scopus 로고
    • SMAP-29: A potent antibacterial and antifungal peptide from sheep leukocytes
    • Skerlavaj B, Benincasa M, Risso A et al. SMAP-29: A potent antibacterial and antifungal peptide from sheep leukocytes. FEBS Lett 1999; 463: 58-62.
    • (1999) FEBS Lett , vol.463 , pp. 58-62
    • Skerlavaj, B.1    Benincasa, M.2    Risso, A.3
  • 13
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • Skerlavaj B, Gennaro R, Bagella L et al. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J Biol Chem 1996; 271: 28375-81.
    • (1996) J Biol Chem , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3
  • 14
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 2005; 3: 238-50.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 15
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • in press
    • Chan DI, Prenner EJ, Vogel HJ. Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action. Biochim Biophys Acta 2006, in press.
    • (2006) Biochim Biophys Acta
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 16
    • 0038706024 scopus 로고    scopus 로고
    • Fungicidal effect of indolicidin and its interaction with phospholipid membranes
    • Lee DG, Kim HK, Kim SA et al. Fungicidal effect of indolicidin and its interaction with phospholipid membranes. Biochem Biophys Res Commun 2003; 305: 305-10.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 305-310
    • Lee, D.G.1    Kim, H.K.2    Kim, S.A.3
  • 17
    • 0029886161 scopus 로고    scopus 로고
    • Synthesis and solution structure of the antimicrobial peptide protegrin-1
    • Aumelas A, Mangoni M, Roumestand C et al. Synthesis and solution structure of the antimicrobial peptide protegrin-1. Eur J Biochem 1996; 237: 575-83.
    • (1996) Eur J Biochem , vol.237 , pp. 575-583
    • Aumelas, A.1    Mangoni, M.2    Roumestand, C.3
  • 18
    • 0345276804 scopus 로고    scopus 로고
    • Immobilization and aggregation of the antimicrobial peptide protegrin-1 in lipid bilayers investigated by solid-state NMR
    • Buffy JJ, Waring AJ, Lehrer RI et al. Immobilization and aggregation of the antimicrobial peptide protegrin-1 in lipid bilayers investigated by solid-state NMR. Biochemistry 2003; 42: 13725-34.
    • (2003) Biochemistry , vol.42 , pp. 13725-13734
    • Buffy, J.J.1    Waring, A.J.2    Lehrer, R.I.3
  • 19
    • 0031842041 scopus 로고    scopus 로고
    • Activity of protegrins against yeast-phase Candida albicans
    • Cho Y, Turner JS, Dinh NN et al. Activity of protegrins against yeast-phase Candida albicans. Infect Immun 1998; 66: 2486-93.
    • (1998) Infect Immun , vol.66 , pp. 2486-2493
    • Cho, Y.1    Turner, J.S.2    Dinh, N.N.3
  • 20
    • 0033858613 scopus 로고    scopus 로고
    • Development of protegrins for the treatment and prevention of oral mucositis: Structure-activity relationships of synthetic protegrin analogues
    • Chen J, Falla TJ, Liu H et al. Development of protegrins for the treatment and prevention of oral mucositis: Structure-activity relationships of synthetic protegrin analogues. Biopolymers 2000; 55: 88-98.
    • (2000) Biopolymers , vol.55 , pp. 88-98
    • Chen, J.1    Falla, T.J.2    Liu, H.3
  • 21
    • 11144357269 scopus 로고    scopus 로고
    • A phase III, randomized, double-blind, placebo-controlled, study of iseganan for the reduction of stomatitis in patients receiving stomatotoxic chemotherapy
    • Giles FJ, Rodriguez R, Weisdorf D et al. A phase III, randomized, double-blind, placebo-controlled, study of iseganan for the reduction of stomatitis in patients receiving stomatotoxic chemotherapy. Leuk Res 2004; 28: 559-65.
    • (2004) Leuk Res , vol.28 , pp. 559-565
    • Giles, F.J.1    Rodriguez, R.2    Weisdorf, D.3
  • 22
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: An observation study
    • Putsep K, Carlsson G, Boman HG et al. Deficiency of antibacterial peptides in patients with morbus Kostmann: An observation study. Lancet 2002; 360: 1144-9.
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3
  • 23
    • 13444259757 scopus 로고    scopus 로고
    • Mig-14 is an inner membrane-associated protein that promotes Salmonella typhimurium resistance to CRAMP, survival within activated macrophages and persistent infection
    • Brodsky IE, Ghori N, Falkow S et al. Mig-14 is an inner membrane-associated protein that promotes Salmonella typhimurium resistance to CRAMP, survival within activated macrophages and persistent infection. Mol Microbiol 2005; 55: 954-72.
    • (2005) Mol Microbiol , vol.55 , pp. 954-972
    • Brodsky, I.E.1    Ghori, N.2    Falkow, S.3
  • 24
    • 0029795520 scopus 로고    scopus 로고
    • Comparison of a spectrophotometric microdilution method with RPMI-2% glucose with the National Committee for Clinical Laboratory Standards reference macrodilution method M27-P for in vitro susceptibility testing of amphotericin B, flucytosine, and fluconazole against Candida albicans
    • Rodriguez-Tudela JL, Berenguer J, Martinez-Suarez JV et al. Comparison of a spectrophotometric microdilution method with RPMI-2% glucose with the National Committee for Clinical Laboratory Standards reference macrodilution method M27-P for in vitro susceptibility testing of amphotericin B, flucytosine, and fluconazole against Candida albicans. Antimicrob Agents Chemother 1996; 40: 1998-2003.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1998-2003
    • Rodriguez-Tudela, J.L.1    Berenguer, J.2    Martinez-Suarez, J.V.3
  • 25
    • 0033516461 scopus 로고    scopus 로고
    • Salivary histatin 5 induces non-lytic release of ATP from Candida albicans leading to cell death
    • Koshlukova SE, Lloyd TL, Araujo MW et al. Salivary histatin 5 induces non-lytic release of ATP from Candida albicans leading to cell death. J Biol Chem 1999; 274: 18872-9.
    • (1999) J Biol Chem , vol.274 , pp. 18872-18879
    • Koshlukova, S.E.1    Lloyd, T.L.2    Araujo, M.W.3
  • 26
    • 0032129784 scopus 로고    scopus 로고
    • Gene disruption to evaluate the role of fungal candidate virulence genes
    • Kwon-Chung K. Gene disruption to evaluate the role of fungal candidate virulence genes. Curr Opin Microbiol 1998; 1: 381-9.
    • (1998) Curr Opin Microbiol , vol.1 , pp. 381-389
    • Kwon-Chung, K.1
  • 27
    • 0024044623 scopus 로고
    • Role of the capsule in phagocytosis of Cryptococcus neoformans
    • Kozel TR, Pfrommer GS, Guerlain AS et al. Role of the capsule in phagocytosis of Cryptococcus neoformans. Rev Infect Dis 1988; 10 Suppl 2: S436-9.
    • (1988) Rev Infect Dis , vol.10 , Issue.SUPPL. 2
    • Kozel, T.R.1    Pfrommer, G.S.2    Guerlain, A.S.3
  • 28
    • 0032504531 scopus 로고    scopus 로고
    • Wide-spectrum antibiotic activity of synthetic, amphipathic peptides
    • Tiozzo E, Rocco G, Tossi A et al. Wide-spectrum antibiotic activity of synthetic, amphipathic peptides. Biochem Biophys Res Commun 1998; 249: 202-6.
    • (1998) Biochem Biophys Res Commun , vol.249 , pp. 202-206
    • Tiozzo, E.1    Rocco, G.2    Tossi, A.3
  • 29
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic α-helical antimicrobial peptides
    • Giangaspero A, Sandri L, Tossi A. Amphipathic α-helical antimicrobial peptides. Eur J Biochem 2001; 268: 5589-600.
    • (2001) Eur J Biochem , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 30
    • 3042577890 scopus 로고    scopus 로고
    • Patterns of amphotericin B killing kinetics against seven Candida species
    • Canton E, Peman J, Gobernado M et al. Patterns of amphotericin B killing kinetics against seven Candida species. Antimicrob Agents Chemother 2004; 48: 2477-82.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 2477-2482
    • Canton, E.1    Peman, J.2    Gobernado, M.3
  • 31
    • 0033777060 scopus 로고    scopus 로고
    • A comparison of dynamic characteristics of fluconazole, itraconazole, and amphotericin B against Cryptococcus neoformans using time-kill methodology
    • Burgess DS, Hastings RW. A comparison of dynamic characteristics of fluconazole, itraconazole, and amphotericin B against Cryptococcus neoformans using time-kill methodology. Diagn Microbiol Infect Dis 2000; 38: 87-93.
    • (2000) Diagn Microbiol Infect Dis , vol.38 , pp. 87-93
    • Burgess, D.S.1    Hastings, R.W.2
  • 32
    • 0036272920 scopus 로고    scopus 로고
    • Antifungal activities of fluconazole, caspofungin (MK0991), and anidulafungin (LY 303366) alone and in combination against Candida spp. and Crytococcus neoformans via time-kill methods
    • Roling EE, Klepser ME, Wasson A et al. Antifungal activities of fluconazole, caspofungin (MK0991), and anidulafungin (LY 303366) alone and in combination against Candida spp. and Crytococcus neoformans via time-kill methods. Diagn Microbiol Infect Dis 2002; 43: 13-17.
    • (2002) Diagn Microbiol Infect Dis , vol.43 , pp. 13-17
    • Roling, E.E.1    Klepser, M.E.2    Wasson, A.3
  • 33
    • 0035522314 scopus 로고    scopus 로고
    • Cytometric approach for a rapid evaluation of susceptibility of Candida strains to antifungals
    • Pina-Vaz C, Sansonetty F, Rodrigues AG et al. Cytometric approach for a rapid evaluation of susceptibility of Candida strains to antifungals. Clin Microbiol Infect 2001; 7: 609-18.
    • (2001) Clin Microbiol Infect , vol.7 , pp. 609-618
    • Pina-Vaz, C.1    Sansonetty, F.2    Rodrigues, A.G.3
  • 34
    • 0033029684 scopus 로고    scopus 로고
    • Amphotericin B and fluconazole affect cellular charge, macrophage phagocytosis, and cellular morphology of Cryptococcus neoformans at subinhibitory concentrations
    • Nosanchuk JD, Cleare W, Franzot SP et al. Amphotericin B and fluconazole affect cellular charge, macrophage phagocytosis, and cellular morphology of Cryptococcus neoformans at subinhibitory concentrations. Antimicrob Agents Chemother 1999; 43: 233-9.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 233-239
    • Nosanchuk, J.D.1    Cleare, W.2    Franzot, S.P.3
  • 35
    • 0031969879 scopus 로고    scopus 로고
    • Clinical, cellular, and molecular factors that contribute to antifungal drug resistance
    • White TC, Marr KA, Bowden RA. Clinical, cellular, and molecular factors that contribute to antifungal drug resistance. Clin Microbiol Rev 1998; 11: 382-402.
    • (1998) Clin Microbiol Rev , vol.11 , pp. 382-402
    • White, T.C.1    Marr, K.A.2    Bowden, R.A.3
  • 36
    • 0026093688 scopus 로고
    • Increase in Candida krusei infection among patients with bone marrow transplantation and neutropenia treated prophylactically with fluconazole
    • Wingard JR, Merz WG, Rinaldi MG et al. Increase in Candida krusei infection among patients with bone marrow transplantation and neutropenia treated prophylactically with fluconazole. N Engl J Med 1991; 325: 1274-7.
    • (1991) N Engl J Med , vol.325 , pp. 1274-1277
    • Wingard, J.R.1    Merz, W.G.2    Rinaldi, M.G.3
  • 37
    • 22144453571 scopus 로고    scopus 로고
    • Anti-fungal activity of cathelicidins and their potential role in Candida albicans skin infection
    • Lopez-Garcia B, Lee PH, Yamasaki K et al. Anti-fungal activity of cathelicidins and their potential role in Candida albicans skin infection. J Invest Dermatol 2005; 125: 108-115.
    • (2005) J Invest Dermatol , vol.125 , pp. 108-115
    • Lopez-Garcia, B.1    Lee, P.H.2    Yamasaki, K.3
  • 38
    • 11844252589 scopus 로고    scopus 로고
    • Expression of SMAP-29 cathelicidin-like peptide in bacterial cells by intein-mediated system
    • Morassutti C, De Amicis F, Bandiera A et al. Expression of SMAP-29 cathelicidin-like peptide in bacterial cells by intein-mediated system. Protein Expr Purif 2005; 39: 160-8.
    • (2005) Protein Expr Purif , vol.39 , pp. 160-168
    • Morassutti, C.1    De Amicis, F.2    Bandiera, A.3
  • 39
    • 33646787464 scopus 로고    scopus 로고
    • Recombinant expression of indolicidin concatamers in Escherichia coli
    • Morin KM, Arcidiacono S, Beckwitt R et al. Recombinant expression of indolicidin concatamers in Escherichia coli. Appl Microbiol Biotechnol 2006; 70: 698-704.
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 698-704
    • Morin, K.M.1    Arcidiacono, S.2    Beckwitt, R.3
  • 40
    • 0029163069 scopus 로고
    • Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity
    • Ahmad I, Perkins WR, Lupan DM et al. Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity. Biochim Biophys Acta 1995; 1237: 109-14.
    • (1995) Biochim Biophys Acta , vol.1237 , pp. 109-114
    • Ahmad, I.1    Perkins, W.R.2    Lupan, D.M.3
  • 41
    • 0032211616 scopus 로고    scopus 로고
    • Cytotoxicity and apoptosis mediated by two peptides of innate immunity
    • Risso A, Zanetti M, Gennaro R. Cytotoxicity and apoptosis mediated by two peptides of innate immunity. Cell Immunol 1998; 189: 107-15.
    • (1998) Cell Immunol , vol.189 , pp. 107-115
    • Risso, A.1    Zanetti, M.2    Gennaro, R.3
  • 42
    • 33646367203 scopus 로고    scopus 로고
    • Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity
    • Xiao Y, Cai Y, Bommineni YR et al. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J Biol Chem 2006; 281: 2858-67.
    • (2006) J Biol Chem , vol.281 , pp. 2858-2867
    • Xiao, Y.1    Cai, Y.2    Bommineni, Y.R.3
  • 44
    • 0036095738 scopus 로고    scopus 로고
    • Activity of novispirin G10 against Pseudomonas aeruginosa in vitro and in infected burns
    • Steinstraesser L, Tack BF, Waring AJ et al. Activity of novispirin G10 against Pseudomonas aeruginosa in vitro and in infected burns. Antimicrob Agents Chemother 2002; 46: 1837-44.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1837-1844
    • Steinstraesser, L.1    Tack, B.F.2    Waring, A.J.3


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