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Volumn 7, Issue 6, 2013, Pages

Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization

Author keywords

[No Author keywords available]

Indexed keywords

BACTENECIN; BOVINE MYELOID ANTIMICROBIAL PEPTIDE 18; CECROPIN A; CEFTAZIDIME; LIPOPOLYSACCHARIDE; MAGAININ DERIVATIVE; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; RTA 3; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; CYCLOPEPTIDE;

EID: 84879515335     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0002267     Document Type: Article
Times cited : (41)

References (56)
  • 1
    • 0033959534 scopus 로고    scopus 로고
    • Pathogenesis of and immunity to melioidosis
    • Brett PJ, Woods DE, (2000) Pathogenesis of and immunity to melioidosis. Acta Tropica 74: 201-210.
    • (2000) Acta Tropica , vol.74 , pp. 201-210
    • Brett, P.J.1    Woods, D.E.2
  • 2
    • 0038324480 scopus 로고    scopus 로고
    • Melioidosis
    • White NJ, (2003) Melioidosis. The Lancet 361: 1715-1722.
    • (2003) The Lancet , vol.361 , pp. 1715-1722
    • White, N.J.1
  • 4
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M, (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 5
    • 0032412381 scopus 로고    scopus 로고
    • Animal Antimicrobial Peptides: An Overview
    • Andreu D, Rivas L, (1998) Animal Antimicrobial Peptides: An Overview. Biopolymers 47: 415-433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 8
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • Wu M, Hancock REW, (1999) Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. Journal of Biological Chemistry 274: 29-35.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 29-35
    • Wu, M.1    Hancock, R.E.W.2
  • 9
    • 79957976381 scopus 로고    scopus 로고
    • Cell selectivity, mechanism of action and LPS-neutralizing activity of bovine myeloid antimicrobial peptide-18 (BMAP-18) and its analogs
    • Lee EK, Kim Y-C, Nan YH, Shin SY, (2011) Cell selectivity, mechanism of action and LPS-neutralizing activity of bovine myeloid antimicrobial peptide-18 (BMAP-18) and its analogs. Peptides 32: 1123-1130.
    • (2011) Peptides , vol.32 , pp. 1123-1130
    • Lee, E.K.1    Kim, Y.-C.2    Nan, Y.H.3    Shin, S.Y.4
  • 10
    • 33644836799 scopus 로고    scopus 로고
    • Synergism of Leu-Lys rich antimicrobial peptides and chloramphenicol against bacterial cells
    • Park Y, Park SN, Park SC, Shin SO, Kim JY, et al. (2006) Synergism of Leu-Lys rich antimicrobial peptides and chloramphenicol against bacterial cells. Biochimica Et Biophysica Acta (BBA) 1764: 24-32.
    • (2006) Biochimica Et Biophysica Acta (BBA) , vol.1764 , pp. 24-32
    • Park, Y.1    Park, S.N.2    Park, S.C.3    Shin, S.O.4    Kim, J.Y.5
  • 14
    • 0023746603 scopus 로고
    • Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo D, Skerlavaj B, Bolognesi M, Gennaro R, (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
  • 15
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • Wu M, Hancock RE, (1999) Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. J Biol Chem 274: 29-35.
    • (1999) J Biol Chem , vol.274 , pp. 29-35
    • Wu, M.1    Hancock, R.E.2
  • 16
    • 0032907969 scopus 로고    scopus 로고
    • Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide
    • Wu M, Hancock RE, (1999) Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. Antimicrob Agents Chemother 43: 1274-1276.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1274-1276
    • Wu, M.1    Hancock, R.E.2
  • 17
    • 84869195634 scopus 로고    scopus 로고
    • Linear bactenecin analogs with cell selectivity and anti-endotoxic activity
    • Hai Nan Y, Jacob B, Kim Y, Yub Shin S, (2012) Linear bactenecin analogs with cell selectivity and anti-endotoxic activity. Journal of Peptide Science 18: 740-747.
    • (2012) Journal of Peptide Science , vol.18 , pp. 740-747
    • Hai Nan, Y.1    Jacob, B.2    Kim, Y.3    Yub Shin, S.4
  • 18
    • 47249135720 scopus 로고    scopus 로고
    • Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide
    • Lee JY, Yang S-T, Lee SK, Jung HH, Shin SY, et al. (2008) Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide. FEBS Journal 275: 3911-3920.
    • (2008) FEBS Journal , vol.275 , pp. 3911-3920
    • Lee, J.Y.1    Yang, S.-T.2    Lee, S.K.3    Jung, H.H.4    Shin, S.Y.5
  • 19
    • 70449719332 scopus 로고    scopus 로고
    • Different modes of antibiotic action of homodimeric and monomeric bactenecin, a cathelicidin-derived antibacterial peptide
    • Lee JY, Yang ST, Kim HJ, Lee SK, Jung HH, et al. (2009) Different modes of antibiotic action of homodimeric and monomeric bactenecin, a cathelicidin-derived antibacterial peptide. BMB Rep 42: 586-592.
    • (2009) BMB Rep , vol.42 , pp. 586-592
    • Lee, J.Y.1    Yang, S.T.2    Kim, H.J.3    Lee, S.K.4    Jung, H.H.5
  • 21
    • 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, Merluzzi L, Risso A, et al. (1996) Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J Biol Chem 271: 28375-28381.
    • (1996) J Biol Chem , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5
  • 23
    • 0000378555 scopus 로고    scopus 로고
    • Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides
    • Shin SY, Lee MK, Kim KL, Hahm K-S, (1997) Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides. The Journal of Peptide Research 50: 279-285.
    • (1997) The Journal of Peptide Research , vol.50 , pp. 279-285
    • Shin, S.Y.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.-S.4
  • 24
    • 0034618590 scopus 로고    scopus 로고
    • CRAMP Analogues Having Potent Antibiotic Activity against Bacterial, Fungal, and Tumor Cells without Hemolytic Activity
    • Shin SY, Kang S-W, Lee DG, Eom SH, Song WK, et al. (2000) CRAMP Analogues Having Potent Antibiotic Activity against Bacterial, Fungal, and Tumor Cells without Hemolytic Activity. Biochemical and Biophysical Research Communications 275: 904-909.
    • (2000) Biochemical and Biophysical Research Communications , vol.275 , pp. 904-909
    • Shin, S.Y.1    Kang, S.-W.2    Lee, D.G.3    Eom, S.H.4    Song, W.K.5
  • 26
    • 48249123462 scopus 로고    scopus 로고
    • Bacterial selectivity and plausible mode of antibacterial action of designed Pro-rich short model antimicrobial peptides
    • Park KH, Park Y, Park S II, Hahm K-S, Shin SY, (2008) Bacterial selectivity and plausible mode of antibacterial action of designed Pro-rich short model antimicrobial peptides. Journal of Peptide Science 14: 876-882.
    • (2008) Journal of Peptide Science , vol.14 , pp. 876-882
    • Park, K.H.1    Park, Y.2    Park II, S.3    Hahm, K.-S.4    Shin, S.Y.5
  • 27
    • 49649113211 scopus 로고    scopus 로고
    • Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides
    • Hawrani A, Howe RA, Walsh TR, Dempsey CE, (2008) Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides. J Biol Chem 283: 18636-18645.
    • (2008) J Biol Chem , vol.283 , pp. 18636-18645
    • Hawrani, A.1    Howe, R.A.2    Walsh, T.R.3    Dempsey, C.E.4
  • 29
    • 79952802131 scopus 로고    scopus 로고
    • The third-generation P-glycoprotein inhibitor tariquidar may overcome bacterial multidrug resistance by increasing intracellular drug concentration
    • Leitner I, Nemeth J, Feurstein T, Abrahim A, Matzneller P, et al. (2011) The third-generation P-glycoprotein inhibitor tariquidar may overcome bacterial multidrug resistance by increasing intracellular drug concentration. Journal of Antimicrobial Chemotherapy 66: 834-839.
    • (2011) Journal of Antimicrobial Chemotherapy , vol.66 , pp. 834-839
    • Leitner, I.1    Nemeth, J.2    Feurstein, T.3    Abrahim, A.4    Matzneller, P.5
  • 30
    • 22544441350 scopus 로고    scopus 로고
    • Iron Salts Perturb Biofilm Formation and Disrupt Existing Biofilms of Pseudomonas aeruginosa
    • Musk DJ, Banko DA, Hergenrother PJ, (2005) Iron Salts Perturb Biofilm Formation and Disrupt Existing Biofilms of Pseudomonas aeruginosa. Chemistry & Biology 12: 789-796.
    • (2005) Chemistry & Biology , vol.12 , pp. 789-796
    • Musk, D.J.1    Banko, D.A.2    Hergenrother, P.J.3
  • 31
    • 67749114474 scopus 로고    scopus 로고
    • Rapid and Reliable Detection of Antimicrobial Peptide Penetration into Gram-Negative Bacteria Based on Fluorescence Quenching
    • Benincasa M, Pacor S, Gennaro R, Scocchi M, (2009) Rapid and Reliable Detection of Antimicrobial Peptide Penetration into Gram-Negative Bacteria Based on Fluorescence Quenching. Antimicrobial Agents and Chemotherapy 53: 3501-3504.
    • (2009) Antimicrobial Agents and Chemotherapy , vol.53 , pp. 3501-3504
    • Benincasa, M.1    Pacor, S.2    Gennaro, R.3    Scocchi, M.4
  • 32
    • 0036510769 scopus 로고    scopus 로고
    • Cell Permeabilization and Uptake of Antisense Peptide-Peptide Nucleic Acid (PNA) into
    • Eriksson M, Nielsen PE, Good L, (2002) Cell Permeabilization and Uptake of Antisense Peptide-Peptide Nucleic Acid (PNA) into. Escherichia coli. 277: 7144-7147.
    • (2002) Escherichia Coli , vol.277 , pp. 7144-7147
    • Eriksson, M.1    Nielsen, P.E.2    Good, L.3
  • 33
    • 0023920225 scopus 로고
    • Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry
    • Lehrer RI, Barton A, Ganz T, (1988) Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry. Journal of Immunological Methods 108: 153-158.
    • (1988) Journal of Immunological Methods , vol.108 , pp. 153-158
    • Lehrer, R.I.1    Barton, A.2    Ganz, T.3
  • 34
  • 35
    • 69249227505 scopus 로고    scopus 로고
    • Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment
    • Torrent M, de la Torre Beatriz G, Nogués Victòria M, Andreu D, Boix E, (2009) Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment. Biochemical Journal 421: 425-434.
    • (2009) Biochemical Journal , vol.421 , pp. 425-434
    • Torrent, M.1    de la Torre Beatriz, G.2    Nogués Victòria, M.3    Andreu, D.4    Boix, E.5
  • 36
    • 0020769095 scopus 로고
    • TMA-DPH: A suitable fluorescence polarization probe for specific plasma membrane fluidity studies in intact living cells
    • Kuhry J-G, Fonteneau P, Duportail G, Maechling C, Laustriat G, (1983) TMA-DPH: A suitable fluorescence polarization probe for specific plasma membrane fluidity studies in intact living cells. Cell Biophysics 5: 129-140.
    • (1983) Cell Biophysics , vol.5 , pp. 129-140
    • Kuhry, J.-G.1    Fonteneau, P.2    Duportail, G.3    Maechling, C.4    Laustriat, G.5
  • 37
    • 84879539012 scopus 로고    scopus 로고
    • Thermodynamic approach to large-scale modeling of alpha-helices in membranes
    • Lomize AL, Mosberg HI, Pogozheva ID, (2012) Thermodynamic approach to large-scale modeling of alpha-helices in membranes. Biophysical Journal 102: 490a-491a.
    • (2012) Biophysical Journal , vol.102
    • Lomize, A.L.1    Mosberg, H.I.2    Pogozheva, I.D.3
  • 39
    • 79955406829 scopus 로고    scopus 로고
    • Anisotropic solvent model of the lipid bilayer. 1. Parameterization of long-range electrostatics and first solvation shell effects
    • Lomize AL, Pogozheva ID, Mosberg HI, (2011) Anisotropic solvent model of the lipid bilayer. 1. Parameterization of long-range electrostatics and first solvation shell effects. J Chem Inf Model 51: 918-929.
    • (2011) J Chem Inf Model , vol.51 , pp. 918-929
    • Lomize, A.L.1    Pogozheva, I.D.2    Mosberg, H.I.3
  • 40
    • 33744490360 scopus 로고    scopus 로고
    • Positioning of proteins in membranes: a computational approach
    • Lomize AL, Pogozheva ID, Lomize MA, Mosberg HI, (2006) Positioning of proteins in membranes: a computational approach. Protein Sci 15: 1318-1333.
    • (2006) Protein Sci , vol.15 , pp. 1318-1333
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 41
    • 79955409906 scopus 로고    scopus 로고
    • Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes
    • Lomize AL, Pogozheva ID, Mosberg HI, (2011) Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes. J Chem Inf Model 51: 930-946.
    • (2011) J Chem Inf Model , vol.51 , pp. 930-946
    • Lomize, A.L.1    Pogozheva, I.D.2    Mosberg, H.I.3
  • 42
    • 34547618240 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in positioning of peripheral proteins in membranes
    • Lomize AL, Pogozheva ID, Lomize MA, Mosberg HI, (2007) The role of hydrophobic interactions in positioning of peripheral proteins in membranes. BMC Struct Biol 7: 44.
    • (2007) BMC Struct Biol , vol.7 , pp. 44
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 43
    • 79251598103 scopus 로고    scopus 로고
    • The contribution of surface residues to membrane binding and ligand transfer by the α-tocopherol transfer protein (α-TTP)
    • Zhang WX, Thakur V, Lomize AL, Pogozheva I, Panagabko C, et al. (2011) The contribution of surface residues to membrane binding and ligand transfer by the α-tocopherol transfer protein (α-TTP). J Mol Biol 405: 972-988.
    • (2011) J Mol Biol , vol.405 , pp. 972-988
    • Zhang, W.X.1    Thakur, V.2    Lomize, A.L.3    Pogozheva, I.4    Panagabko, C.5
  • 44
    • 79958024940 scopus 로고    scopus 로고
    • Membrane topology of the colicin E1 channel using genetically encoded fluorescence
    • Ho D, Lugo MR, Lomize AL, Pogozheva ID, Singh SP, et al. (2011) Membrane topology of the colicin E1 channel using genetically encoded fluorescence. Biochemistry 50: 4830-4842.
    • (2011) Biochemistry , vol.50 , pp. 4830-4842
    • Ho, D.1    Lugo, M.R.2    Lomize, A.L.3    Pogozheva, I.D.4    Singh, S.P.5
  • 45
    • 79955437263 scopus 로고    scopus 로고
    • Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air-water interface
    • López-Oyama AB, Taboada P, Burboa MG, Rodríguez E, Mosquera V, et al. (2011) Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air-water interface. J Colloid Interface Sci 359: 279-288.
    • (2011) J Colloid Interface Sci , vol.359 , pp. 279-288
    • López-Oyama, A.B.1    Taboada, P.2    Burboa, M.G.3    Rodríguez, E.4    Mosquera, V.5
  • 46
    • 67650351047 scopus 로고    scopus 로고
    • The membrane action mechanism of analogs of the antimicrobial peptide Buforin 2
    • Hao G, Shi Y-H, Tang Y-L, Le G-W, (2009) The membrane action mechanism of analogs of the antimicrobial peptide Buforin 2. Peptides 30: 1421-1427.
    • (2009) Peptides , vol.30 , pp. 1421-1427
    • Hao, G.1    Shi, Y.-H.2    Tang, Y.-L.3    Le, G.-W.4
  • 47
    • 0031214521 scopus 로고    scopus 로고
    • Thermodynamic model of secondary structure for alpha-helical peptides and proteins
    • Lomize AL, Mosberg HI, (1997) Thermodynamic model of secondary structure for alpha-helical peptides and proteins. Biopolymers 42: 239-269.
    • (1997) Biopolymers , vol.42 , pp. 239-269
    • Lomize, A.L.1    Mosberg, H.I.2
  • 49
    • 0026351935 scopus 로고
    • Conformation of beta hairpins in protein structures: classification and diversity in homologous structures
    • Sibanda BL, Thornton JM, (1991) Conformation of beta hairpins in protein structures: classification and diversity in homologous structures. Meth Enzymol 202: 59-82.
    • (1991) Meth Enzymol , vol.202 , pp. 59-82
    • Sibanda, B.L.1    Thornton, J.M.2
  • 50
    • 80053175097 scopus 로고    scopus 로고
    • Transcriptional responses of Burkholderia cenocepacia to polymyxin B in isogenic strains with diverse polymyxin B resistance phenotypes
    • Loutet S, Di Lorenzo F, Clarke C, Molinaro A, Valvano MA, (2011) Transcriptional responses of Burkholderia cenocepacia to polymyxin B in isogenic strains with diverse polymyxin B resistance phenotypes. BMC Genomics 12: 472.
    • (2011) BMC Genomics , vol.12 , pp. 472
    • Loutet, S.1    Di Lorenzo, F.2    Clarke, C.3    Molinaro, A.4    Valvano, M.A.5
  • 53
    • 77949430037 scopus 로고    scopus 로고
    • Growing Burkholderia pseudomallei in biofilm stimulating conditions significantly induces antimicrobial resistance
    • Sawasdidoln C, Taweechaisupapong S, Sermswan RW, Tattawasart U, Tungpradabkul S, et al. (2010) Growing Burkholderia pseudomallei in biofilm stimulating conditions significantly induces antimicrobial resistance. PloS One 5: e9196.
    • (2010) PloS One , vol.5
    • Sawasdidoln, C.1    Taweechaisupapong, S.2    Sermswan, R.W.3    Tattawasart, U.4    Tungpradabkul, S.5
  • 55
    • 79953186604 scopus 로고    scopus 로고
    • Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR
    • Hong M, Su Y, (2011) Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR. Protein Sci 20: 641-655.
    • (2011) Protein Sci , vol.20 , pp. 641-655
    • Hong, M.1    Su, Y.2
  • 56
    • 0026351935 scopus 로고
    • [5] Conformation of β hairpins in protein structures: Classification and diversity in homologous structures
    • In: John JL, editor,. Academic Press
    • Sibanda BL, Thornton JM (1991) [5] Conformation of β hairpins in protein structures: Classification and diversity in homologous structures. In: John JL, editor. Methods in Enzymology. Academic Press. pp. 59-82.
    • (1991) Methods in Enzymology , pp. 59-82
    • Sibanda, B.L.1    Thornton, J.M.2


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