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Volumn 76, Issue 21, 2010, Pages 7102-7108

Screening for antifungal peptides and their modes of action in Aspergillus nidulans

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-BACTERIAL ACTIVITY; ANTI-FUNGAL; ANTI-FUNGAL ACTIVITY; ANTI-MICROBIAL AGENT; ANTIBACTERIAL AGENT; ANTIBACTERIAL PEPTIDES; ASPERGILLUS NIDULANS; BRANCH FORMATION; CATIONIC PEPTIDES; CELLULOSE MEMBRANES; CYTOPLASMIC MEMBRANE; FLUORESCEIN ISOTHIOCYANATE; HIGH-THROUGHPUT ASSAYS; HYPHAL TIP; MEMBRANE DOMAIN; MICROTITER PLATES; MODE OF ACTION; PEPTIDE LIBRARY; PEPTIDE SYNTHESIS; POLARIZED GROWTH; SCREENING METHODS; TIP GROWTH;

EID: 78149439531     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01560-10     Document Type: Article
Times cited : (49)

References (44)
  • 2
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. 2005. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3:238-250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 3
    • 60749130267 scopus 로고    scopus 로고
    • Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs
    • Cherkasov, A., K. Hilpert, H. Jenssen, C. D. Fjell, M. Waldbrook, S. C. Mullaly, R. Volkmer, and R. E. Hancock. 2009. Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs. ACS Chem. Biol. 4:65-74.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 65-74
    • Cherkasov, A.1    Hilpert, K.2    Jenssen, H.3    Fjell, C.D.4    Waldbrook, M.5    Mullaly, S.C.6    Volkmer, R.7    Hancock, R.E.8
  • 4
    • 77952362863 scopus 로고    scopus 로고
    • Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: Lipid clustering in anionic membranes
    • Epand, R. F., L. Maloy, A. Ramamoorthy, and R. M. Epand. 2010. Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: Lipid clustering in anionic membranes. Biophys. J. 98:2564-2573.
    • (2010) Biophys. J. , vol.98 , pp. 2564-2573
    • Epand, R.F.1    Maloy, L.2    Ramamoorthy, A.3    Epand, R.M.4
  • 5
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • Epand, R. M., and R. F. Epand. 2009. Lipid domains in bacterial membranes and the action of antimicrobial agents. Biochim. Biophys. Acta 1788:289-294.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 6
    • 61349203825 scopus 로고    scopus 로고
    • A rapid resazurin bioassay for assessing the toxicity of fungicides
    • Fai, P. B., and A. Grant. 2009. A rapid resazurin bioassay for assessing the toxicity of fungicides. Chemosphere 74:1165-1170.
    • (2009) Chemosphere , vol.74 , pp. 1165-1170
    • Fai, P.B.1    Grant, A.2
  • 7
    • 42549091729 scopus 로고    scopus 로고
    • Polarized growth in fungi-interplay between the cytoskeleton, positional markers and membrane domains
    • Fischer, R., N. Zekert, and N. Takeshita. 2008. Polarized growth in fungi- interplay between the cytoskeleton, positional markers and membrane domains. Mol. Microbiol. 68:813-826.
    • (2008) Mol. Microbiol. , vol.68 , pp. 813-826
    • Fischer, R.1    Zekert, N.2    Takeshita, N.3
  • 11
    • 0036893607 scopus 로고    scopus 로고
    • Design and use of a peptide nucleic acid for detection of the heteroplasmic low-frequency mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS) mutation in human mitochondrial DNA
    • Hancock, D. K., F. P. Schwarz, F. Song, L. J. Wong, and B. C. Levin. 2002. Design and use of a peptide nucleic acid for detection of the heteroplasmic low-frequency mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS) mutation in human mitochondrial DNA. Clin. Chem. 48:2155-2163.
    • (2002) Clin. Chem. , vol.48 , pp. 2155-2163
    • Hancock, D.K.1    Schwarz, F.P.2    Song, F.3    Wong, L.J.4    Levin, B.C.5
  • 12
    • 21344467254 scopus 로고    scopus 로고
    • Comparison of susceptibility of fungal isolates to lufenuron and nikkomycin Z alone or in combination with itraconazole
    • Hector, R. F., A. P. Davidson, and S. M. Johnson. 2005. Comparison of susceptibility of fungal isolates to lufenuron and nikkomycin Z alone or in combination with itraconazole. Am. J. Vet. Res. 66:1090-1093.
    • (2005) Am. J. Vet. Res. , vol.66 , pp. 1090-1093
    • Hector, R.F.1    Davidson, A.P.2    Johnson, S.M.3
  • 13
    • 0345071480 scopus 로고    scopus 로고
    • Improved protocols for Aspergillus minimal medium: Trace element and minimal medium salt stock solutions
    • Hill, T. W., and E. Käfer. 2001. Improved protocols for Aspergillus minimal medium: Trace element and minimal medium salt stock solutions. Fungal Genet. News 48:20-21.
    • (2001) Fungal Genet. News , vol.48 , pp. 20-21
    • Hill, T.W.1    Käfer, E.2
  • 16
    • 34548595245 scopus 로고    scopus 로고
    • Use of luminescent bacteria for rapid screening and characterization of short cationic antimicrobial peptides synthesized on cellulose using peptide array technology
    • Hilpert, K., and R. E. Hancock. 2007. Use of luminescent bacteria for rapid screening and characterization of short cationic antimicrobial peptides synthesized on cellulose using peptide array technology. Nat. Protoc. 2:1652-1660.
    • (2007) Nat. Protoc. , vol.2 , pp. 1652-1660
    • Hilpert, K.1    Hancock, R.E.2
  • 18
    • 23444451770 scopus 로고    scopus 로고
    • Highthroughput generation of small antibacterial peptides with improved activity
    • Hilpert, K., R. Volkmer-Engert, T. Walter, and R. E. Hancock. 2005. Highthroughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 23:1008-1012.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.4
  • 19
    • 34250721648 scopus 로고    scopus 로고
    • Peptide arrays on cellulose support: SPOT synthesis, a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion
    • Hilpert, K., D. F. Winkler, and R. E. Hancock. 2007. Peptide arrays on cellulose support: SPOT synthesis, a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion. Nat. Protoc. 2:1333-1349.
    • (2007) Nat. Protoc. , vol.2 , pp. 1333-1349
    • Hilpert, K.1    Winkler, D.F.2    Hancock, R.E.3
  • 20
    • 20344392686 scopus 로고    scopus 로고
    • Natural products and antifungal drug discovery
    • Jacob, M. R., and L. A. Walker. 2005. Natural products and antifungal drug discovery. Methods Mol. Med. 118:83-109.
    • (2005) Methods Mol. Med. , vol.118 , pp. 83-109
    • Jacob, M.R.1    Walker, L.A.2
  • 22
    • 77956125592 scopus 로고    scopus 로고
    • Easy strategy to protect antimicrobial peptides from fast degradation in serum
    • Knappe, D., P. Henklein, R. Hoffmann, and K. Hilpert. 2010. Easy strategy to protect antimicrobial peptides from fast degradation in serum. Antimicrob. Agents Chemother. 54:4003-4005.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 4003-4005
    • Knappe, D.1    Henklein, P.2    Hoffmann, R.3    Hilpert, K.4
  • 24
    • 2942662225 scopus 로고    scopus 로고
    • Lipid raft polarization contributes to hyphal growth in Candida albicans
    • Martin, S. W., and J. B. Konopka. 2004. Lipid raft polarization contributes to hyphal growth in Candida albicans. Eukaryot. Cell 3:675-684.
    • (2004) Eukaryot. Cell , vol.3 , pp. 675-684
    • Martin, S.W.1    Konopka, J.B.2
  • 26
    • 67349172950 scopus 로고    scopus 로고
    • Interpretable features for the activity prediction of short antimicrobial peptides using fuzzy logic
    • Mikut, R., and K. Hilpert. 2009. Interpretable features for the activity prediction of short antimicrobial peptides using fuzzy logic. Int. J. Pept. Res. Ther. 15:129-137.
    • (2009) Int. J. Pept. Res. Ther. , vol.15 , pp. 129-137
    • Mikut, R.1    Hilpert, K.2
  • 27
    • 15744398051 scopus 로고    scopus 로고
    • Role of membrane lipids in bacterial division-site selection
    • Mileykovskaya, E., and W. Dowhan. 2005. Role of membrane lipids in bacterial division-site selection. Curr. Opin. Microbiol. 8:135-142.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 135-142
    • Mileykovskaya, E.1    Dowhan, W.2
  • 28
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • Mileykovskaya, E., and W. Dowhan. 2000. Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange. J. Bacteriol. 182:1172-1175.
    • (2000) J. Bacteriol. , vol.182 , pp. 1172-1175
    • Mileykovskaya, E.1    Dowhan, W.2
  • 29
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections
    • Mookherjee, N., and R. E. Hancock. 2007. Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections. Cell Mol. Life Sci. 64:922-933.
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.2
  • 30
    • 4644232332 scopus 로고    scopus 로고
    • PAK kinases Ste20 and Pak1 govern cell polarity at different stages of mating in Cryptococcus neoformans
    • Nichols, C. B., J. A. Fraser, and J. Heitman. 2004. PAK kinases Ste20 and Pak1 govern cell polarity at different stages of mating in Cryptococcus neoformans. Mol. Biol. Cell 15:4476-4489.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4476-4489
    • Nichols, C.B.1    Fraser, J.A.2    Heitman, J.3
  • 31
    • 0033856957 scopus 로고    scopus 로고
    • Investigation of the Alamar Blue (resazurin) fluorescent dye for the assessment of mammalian cell cytotoxicity
    • O'Brien, J., I. Wilson, T. Orton, and F. Pognan. 2000. Investigation of the Alamar Blue (resazurin) fluorescent dye for the assessment of mammalian cell cytotoxicity. Eur. J. Biochem. 267:5421-5426.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5421-5426
    • O'Brien, J.1    Wilson, I.2    Orton, T.3    Pognan, F.4
  • 32
    • 27844610224 scopus 로고    scopus 로고
    • Tracing the endocytic pathway of Aspergillus nidulans with FM4-64
    • Penalva, M. A. 2005. Tracing the endocytic pathway of Aspergillus nidulans with FM4-64. Fungal Genet. Biol. 42:963-975.
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 963-975
    • Penalva, M.A.1
  • 33
    • 17244380947 scopus 로고    scopus 로고
    • Lipid rafts and membrane dynamics
    • Rajendran, L., and K. Simons. 2005. Lipid rafts and membrane dynamics. J. Cell Sci. 118:1099-1102.
    • (2005) J. Cell Sci. , vol.118 , pp. 1099-1102
    • Rajendran, L.1    Simons, K.2
  • 34
    • 0023746603 scopus 로고
    • Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo, D., B. Skerlavaj, M. Bolognesi, and R. Gennaro. 1988. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J. Biol. Chem. 263:9573-9575.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9573-9575
    • Romeo, D.1    Skerlavaj, B.2    Bolognesi, M.3    Gennaro, R.4
  • 35
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • Rozek, A., C. L. Friedrich, and R. E. Hancock. 2000. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 39:15765-15774.
    • (2000) Biochemistry , vol.39 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.3
  • 37
    • 67649408946 scopus 로고    scopus 로고
    • Bombinins, antimicrobial peptides from Bombina species
    • Simmaco, M., G. Kreil, and D. Barra. 2009. Bombinins, antimicrobial peptides from Bombina species. Biochim. Biophys. Acta 1788:1551-1555.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1551-1555
    • Simmaco, M.1    Kreil, G.2    Barra, D.3
  • 38
    • 38749129692 scopus 로고    scopus 로고
    • Apical sterol-rich membranes are essential for localizing cell end markers that determine growth directionality in the filamentous fungus Aspergillus nidulans
    • Takeshita, N., Y. Higashitsuji, S. Konzack, and R. Fischer. 2008. Apical sterol-rich membranes are essential for localizing cell end markers that determine growth directionality in the filamentous fungus Aspergillus nidulans. Mol. Biol. Cell 19:339-351.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 339-351
    • Takeshita, N.1    Higashitsuji, Y.2    Konzack, S.3    Fischer, R.4
  • 40
    • 3042732666 scopus 로고    scopus 로고
    • Establishment of mRFP1 as a fluorescent marker in Aspergillus nidulans and construction of expression vectors for high-throughput protein tagging using recombination in vitro (GATEWAY)
    • Toews, M. W., J. Warmbold, S. Konzack, P. Rischitor, D. Veith, K. Vienken, C. Vinuesa, H. Wei, and R. Fischer. 2004. Establishment of mRFP1 as a fluorescent marker in Aspergillus nidulans and construction of expression vectors for high-throughput protein tagging using recombination in vitro (GATEWAY). Curr. Genet. 45:383-389.
    • (2004) Curr. Genet. , vol.45 , pp. 383-389
    • Toews, M.W.1    Warmbold, J.2    Konzack, S.3    Rischitor, P.4    Veith, D.5    Vienken, K.6    Vinuesa, C.7    Wei, H.8    Fischer, R.9
  • 41
    • 0042565977 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labelled phospholipids
    • Vanounou, S., A. H. Parola, and I. Fishov. 2003. Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labelled phospholipids. Mol. Microbiol. 49:1067-1079.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1067-1079
    • Vanounou, S.1    Parola, A.H.2    Fishov, I.3
  • 42
    • 58149187882 scopus 로고    scopus 로고
    • APD2: The updated antimicrobial peptide database and its application in peptide design
    • Wang, G., X. Li, and Z. Wang. 2009. APD2: The updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 37:D933-D937.
    • (2009) Nucleic Acids Res. , vol.37
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 43
    • 34250648471 scopus 로고    scopus 로고
    • The echinocandin micafungin: A review of the pharmacology, spectrum of activity, clinical efficacy and safety
    • Wiederhold, N. P., and J. S. Lewis II. 2007. The echinocandin micafungin: A review of the pharmacology, spectrum of activity, clinical efficacy and safety. Expert Opin. Pharmacother 8:1155-1166.
    • (2007) Expert Opin. Pharmacother , vol.8 , pp. 1155-1166
    • Wiederhold, N.P.1    Lewis II, J.S.2
  • 44
    • 0032907969 scopus 로고    scopus 로고
    • Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide
    • Wu, M., and R. E. Hancock. 1999. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. Antimicrob. Agents Chemother. 43:1274-1276. (Pubitemid 29214762)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.5 , pp. 1274-1276
    • Wu, M.1    Hancock, R.E.W.2


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