메뉴 건너뛰기




Volumn 51, Issue 11, 2007, Pages 3908-3914

Polymyxin B induces lysis of marine pseudoalteromonads

Author keywords

[No Author keywords available]

Indexed keywords

NIGERICIN; POLYMYXIN B;

EID: 35848945053     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.00449-07     Document Type: Article
Times cited : (12)

References (53)
  • 1
    • 34250007704 scopus 로고    scopus 로고
    • Lipid-containing bacteriophage PM2, the type-organism of Corticoviridae
    • R. Calendar ed, 2nd ed. Oxford University Press, Oxford, United Kingdom
    • Bamford, D. H., and J. K. H. Bamford. 2006. Lipid-containing bacteriophage PM2, the type-organism of Corticoviridae, p. 171-175. In R. Calendar (ed.), The bacteriophages, 2nd ed. Oxford University Press, Oxford, United Kingdom.
    • (2006) The bacteriophages , pp. 171-175
    • Bamford, D.H.1    Bamford, J.K.H.2
  • 3
    • 0030002510 scopus 로고    scopus 로고
    • Specificity for the exchange of phospholipids through polymyxin B mediated intermembrane molecular contacts
    • Cajal, Y., J. Ghanta, K. Easwaran, A. Surolia, and M. K. Jain. 1996. Specificity for the exchange of phospholipids through polymyxin B mediated intermembrane molecular contacts. Biochemistry 35:5684-5695.
    • (1996) Biochemistry , vol.35 , pp. 5684-5695
    • Cajal, Y.1    Ghanta, J.2    Easwaran, K.3    Surolia, A.4    Jain, M.K.5
  • 4
    • 0030022871 scopus 로고    scopus 로고
    • Intermembrane molecular contacts by polymyxin B mediate exchange of phospholipids
    • Cajal, Y., J. Rogers, O. G. Berg, and M. K. Jain. 1996. Intermembrane molecular contacts by polymyxin B mediate exchange of phospholipids. Biochemistry 35:299-308.
    • (1996) Biochemistry , vol.35 , pp. 299-308
    • Cajal, Y.1    Rogers, J.2    Berg, O.G.3    Jain, M.K.4
  • 5
    • 0036091211 scopus 로고    scopus 로고
    • Regulation of autolysins in teichuronic acid-containing Bacillus subtilis cells
    • Calamita, H. G., and R. J. Doyle. 2002. Regulation of autolysins in teichuronic acid-containing Bacillus subtilis cells. Mol. Microbiol. 44:601-606.
    • (2002) Mol. Microbiol , vol.44 , pp. 601-606
    • Calamita, H.G.1    Doyle, R.J.2
  • 6
    • 0015000401 scopus 로고
    • Differential release of periplasmic versus cytoplasmic enzymes from Escherichia coli B by polymixin B
    • Cerny, G., and M. Teuber. 1971. Differential release of periplasmic versus cytoplasmic enzymes from Escherichia coli B by polymixin B. Arch. Mikrobiol. 78:166-179.
    • (1971) Arch. Mikrobiol , vol.78 , pp. 166-179
    • Cerny, G.1    Teuber, M.2
  • 7
    • 0015434379 scopus 로고
    • Locus of divalent cation inhibition of the bactericidal action of polymyxin B
    • Chen, C. C., and D. S. Feingold. 1972. Locus of divalent cation inhibition of the bactericidal action of polymyxin B. Antimicrob. Agents Chemother. 2:331-335.
    • (1972) Antimicrob. Agents Chemother , vol.2 , pp. 331-335
    • Chen, C.C.1    Feingold, D.S.2
  • 9
    • 0036834373 scopus 로고    scopus 로고
    • The future challenges facing the development of new antimicrobial drugs
    • Coates, A., Y. Hu, R. Bax, and C. Page. 2002. The future challenges facing the development of new antimicrobial drugs. Nat. Rev. Drug Discov. 1:895-910.
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 895-910
    • Coates, A.1    Hu, Y.2    Bax, R.3    Page, C.4
  • 10
    • 0018194284 scopus 로고
    • Cellular lysis of Streptococcus faecalis induced with Triton X-100
    • Cornett, J. B., and G. D. Shockman. 1978. Cellular lysis of Streptococcus faecalis induced with Triton X-100. J. Bacteriol. 135:153-160.
    • (1978) J. Bacteriol , vol.135 , pp. 153-160
    • Cornett, J.B.1    Shockman, G.D.2
  • 11
    • 33750969982 scopus 로고    scopus 로고
    • New uses for older antibiotics: Nitrofurantoin, amikacin, colistin, polymyxin B, doxycycline, and minocycline revisited
    • Cunha, B. A. 2006. New uses for older antibiotics: nitrofurantoin, amikacin, colistin, polymyxin B, doxycycline, and minocycline revisited. Med. Clin. N. Am. 90:1089-1107.
    • (2006) Med. Clin. N. Am , vol.90 , pp. 1089-1107
    • Cunha, B.A.1
  • 12
    • 0033743315 scopus 로고    scopus 로고
    • Stages of polymyxin B interaction with the Escherichia coli cell envelope
    • Daugelavičius, R., E. Bakienė, and D. H. Bamford. 2000. Stages of polymyxin B interaction with the Escherichia coli cell envelope. Antimicrob. Agents Chemother. 44:2969-2978.
    • (2000) Antimicrob. Agents Chemother , vol.44 , pp. 2969-2978
    • Daugelavičius, R.1    Bakienė, E.2    Bamford, D.H.3
  • 15
    • 0030755555 scopus 로고    scopus 로고
    • Changes in host cell energetics in response to bacteriophage PRD1 DNA entry
    • Daugelavičius, R., J. K. Bamtord, and D. H. Bamford. 1997. Changes in host cell energetics in response to bacteriophage PRD1 DNA entry. J. Bacteriol. 179:5203-5210.
    • (1997) J. Bacteriol , vol.179 , pp. 5203-5210
    • Daugelavičius, R.1    Bamtord, J.K.2    Bamford, D.H.3
  • 16
    • 33947267137 scopus 로고    scopus 로고
    • On-line monitoring of changes in host cell physiology during the one-step growth cycle of Bacillus phage Bam35
    • Daugelavičius, R., A. Gaidelytė, V. Cvirkaitė- Krupovič, and D. H. Bamford. 2007. On-line monitoring of changes in host cell physiology during the one-step growth cycle of Bacillus phage Bam35. J. Microbiol. Methods 69:174-179.
    • (2007) J. Microbiol. Methods , vol.69 , pp. 174-179
    • Daugelavičius, R.1    Gaidelytė, A.2    Cvirkaitė- Krupovič, V.3    Bamford, D.H.4
  • 17
    • 0022644695 scopus 로고
    • Leakage of periplasmic proteins from Escherichia coli mediated by polymyxin B nonapeptide
    • Dixon, R. A., and I. Chopra. 1986. Leakage of periplasmic proteins from Escherichia coli mediated by polymyxin B nonapeptide. Antimicrob. Agents Chemother. 29:781-788.
    • (1986) Antimicrob. Agents Chemother , vol.29 , pp. 781-788
    • Dixon, R.A.1    Chopra, I.2
  • 18
    • 0023033246 scopus 로고
    • Polymyxin B and polymyxin B nonapeptide alter cytoplasmic membrane permeability in Escherichia coli
    • Dixon, R. A., and I. Chopra. 1986. Polymyxin B and polymyxin B nonapeptide alter cytoplasmic membrane permeability in Escherichia coli. J. Antimicrob. Chemother. 18:557-563.
    • (1986) J. Antimicrob. Chemother , vol.18 , pp. 557-563
    • Dixon, R.A.1    Chopra, I.2
  • 19
    • 0014284555 scopus 로고
    • Properties and characterization of the host bacterium of bacteriophage PM2
    • Espejo, R. T., and E. S. Canelo. 1968. Properties and characterization of the host bacterium of bacteriophage PM2. J. Bacteriol. 95:1887-1891.
    • (1968) J. Bacteriol , vol.95 , pp. 1887-1891
    • Espejo, R.T.1    Canelo, E.S.2
  • 20
    • 0014275022 scopus 로고
    • Properties of bacteriophage PM2: A lipid-containing bacterial virus
    • Espejo, R. T., and E. S. Canelo. 1968. Properties of bacteriophage PM2: a lipid-containing bacterial virus. Virology 34:738-747.
    • (1968) Virology , vol.34 , pp. 738-747
    • Espejo, R.T.1    Canelo, E.S.2
  • 21
    • 0032826448 scopus 로고    scopus 로고
    • Polymyxin B sulfate and Colistin: Old antibiotics for emerging multiresistant gram-negative bacteria
    • Evans, M. E., D. J. Feola, and R. P. Rapp. 1999. Polymyxin B sulfate and Colistin: old antibiotics for emerging multiresistant gram-negative bacteria. Ann. Pharmacother. 33:960-967.
    • (1999) Ann. Pharmacother , vol.33 , pp. 960-967
    • Evans, M.E.1    Feola, D.J.2    Rapp, R.P.3
  • 22
    • 33847122008 scopus 로고    scopus 로고
    • Local administration of polymyxins into the respiratory tract for the prevention and treatment of pulmonary infections in patients without cystic fibrosis
    • Falagas, M. E., and S. K. Kasiakou. 2007. Local administration of polymyxins into the respiratory tract for the prevention and treatment of pulmonary infections in patients without cystic fibrosis. Infection 35:3-10.
    • (2007) Infection , vol.35 , pp. 3-10
    • Falagas, M.E.1    Kasiakou, S.K.2
  • 23
    • 34447560960 scopus 로고    scopus 로고
    • Toxicity of polymyxins: A systematic review of the evidence from old and recent studies
    • Falagas, M. E., and S. K. Kasiakou. 2006. Toxicity of polymyxins: a systematic review of the evidence from old and recent studies. Crit. Care 10:R27.
    • (2006) Crit. Care , vol.10
    • Falagas, M.E.1    Kasiakou, S.K.2
  • 24
    • 33344469704 scopus 로고    scopus 로고
    • Polymyxins: Old antibiotics are back
    • Falagas, M. E., and A. Michalopoulos. 2006. Polymyxins: old antibiotics are back. Lancet 367:633-634.
    • (2006) Lancet , vol.367 , pp. 633-634
    • Falagas, M.E.1    Michalopoulos, A.2
  • 25
    • 0028799334 scopus 로고
    • Phylogenese analysis of the genera Alteromonas, Shewanella, and Moritella using genes coding for small-subunit rRNA sequences and division of the genus Alteromonas into two genera, Alteromonas (emended) and Pseudoalteromonas gen. nov., and proposal of twelve new species combinations
    • Gauthier, G., M. Gauthier, and R. Christen. 1995. Phylogenese analysis of the genera Alteromonas, Shewanella, and Moritella using genes coding for small-subunit rRNA sequences and division of the genus Alteromonas into two genera, Alteromonas (emended) and Pseudoalteromonas gen. nov., and proposal of twelve new species combinations. Int. J. Syst. Bacteriol. 45:755-761.
    • (1995) Int. J. Syst. Bacteriol , vol.45 , pp. 755-761
    • Gauthier, G.1    Gauthier, M.2    Christen, R.3
  • 27
    • 0025862413 scopus 로고
    • Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli
    • Hancock, R. E., S. W. Farmer, Z. S. Li, and K. Poole. 1991. Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli. Antimicrob. Agents Chemother. 35:1309-1314.
    • (1991) Antimicrob. Agents Chemother , vol.35 , pp. 1309-1314
    • Hancock, R.E.1    Farmer, S.W.2    Li, Z.S.3    Poole, K.4
  • 28
    • 0021282341 scopus 로고
    • Compounds which increase the permeability of the Pseudomonas aeruginosa outer membrane
    • Hancock, R. E., and P. G. Wong. 1984. Compounds which increase the permeability of the Pseudomonas aeruginosa outer membrane. Antimicrob. Agents Chemother. 26:48-52.
    • (1984) Antimicrob. Agents Chemother , vol.26 , pp. 48-52
    • Hancock, R.E.1    Wong, P.G.2
  • 29
    • 34147162786 scopus 로고    scopus 로고
    • Thermodynamic analysis of the lipopolysaccharide-dependent resistance of Gram-negative bacteria against polymyxin B
    • Howe, J., J. Andra, R. Conde, M. Iriarte, P. Garidel, M. H. Koch, T. Gutsmann, I. Moriyon, and K. Brandenburg. 2007. Thermodynamic analysis of the lipopolysaccharide-dependent resistance of Gram-negative bacteria against polymyxin B. Biophys. J. 92:2796-2805.
    • (2007) Biophys. J , vol.92 , pp. 2796-2805
    • Howe, J.1    Andra, J.2    Conde, R.3    Iriarte, M.4    Garidel, P.5    Koch, M.H.6    Gutsmann, T.7    Moriyon, I.8    Brandenburg, K.9
  • 30
    • 0019452877 scopus 로고
    • The energized membrane and cellular autolysis in Bacillus subtilis
    • Jolliffe, L. K., R. J. Doyle, and U. N. Streips. 1981. The energized membrane and cellular autolysis in Bacillus subtilis. Cell 25:753-763.
    • (1981) Cell , vol.25 , pp. 753-763
    • Jolliffe, L.K.1    Doyle, R.J.2    Streips, U.N.3
  • 32
    • 0344761956 scopus 로고    scopus 로고
    • Purification and protein composition of PM2, the first lipid-containing bacterial virus to be isolated
    • Kivelä, H. M., R. H. Männistö, N. Kalkkinen, and D. H. Bamford. 1999. Purification and protein composition of PM2, the first lipid-containing bacterial virus to be isolated. Virology 262:364-374.
    • (1999) Virology , vol.262 , pp. 364-374
    • Kivelä, H.M.1    Männistö, R.H.2    Kalkkinen, N.3    Bamford, D.H.4
  • 33
    • 34249993104 scopus 로고    scopus 로고
    • A novel lysis system in PM2, a lipid-containing marine dsDNA bacteriophage
    • Krupovič, M., R. Daugelavičius, and D. H. Bamford. 2007. A novel lysis system in PM2, a lipid-containing marine dsDNA bacteriophage. Mol. Microbiol. 64:1635-1648.
    • (2007) Mol. Microbiol , vol.64 , pp. 1635-1648
    • Krupovič, M.1    Daugelavičius, R.2    Bamford, D.H.3
  • 34
    • 0014734242 scopus 로고
    • Mutants of Diplococcus pneumoniae that lack deoxyribonucleases and other activities possibly pertinent to genetic transformation
    • Lacks, S. 1970. Mutants of Diplococcus pneumoniae that lack deoxyribonucleases and other activities possibly pertinent to genetic transformation. J. Bacteriol. 101:373-383.
    • (1970) J. Bacteriol , vol.101 , pp. 373-383
    • Lacks, S.1
  • 35
    • 33747360999 scopus 로고    scopus 로고
    • Ecological advantages of autolysis during the development and dispersal of Pseudoalteromonas tunicata biofilms
    • Mai-Prochnow, A., J. S. Webb, B. C. Ferrari, and S. Kjelleberg. 2006. Ecological advantages of autolysis during the development and dispersal of Pseudoalteromonas tunicata biofilms. Appl. Environ. Microbiol. 72:5414-5420.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 5414-5420
    • Mai-Prochnow, A.1    Webb, J.S.2    Ferrari, B.C.3    Kjelleberg, S.4
  • 36
    • 0017834365 scopus 로고
    • Effect of polymyxin B on the structure and the stability of lipid layers
    • Miller, I. R., D. Bach, and M. Teuber. 1978. Effect of polymyxin B on the structure and the stability of lipid layers. J. Membr. Biol. 39:49-56.
    • (1978) J. Membr. Biol , vol.39 , pp. 49-56
    • Miller, I.R.1    Bach, D.2    Teuber, M.3
  • 37
    • 0022580949 scopus 로고
    • Interaction of polycationic antibiotics with Pseudomonas aeruginosa lipopolysaccharide and lipid A studied by using dansyl-polymyxin
    • Moore, R. A., N. C. Bates, and R. E. Hancock. 1986. Interaction of polycationic antibiotics with Pseudomonas aeruginosa lipopolysaccharide and lipid A studied by using dansyl-polymyxin. Antimicrob. Agents Chemother. 29:496-500.
    • (1986) Antimicrob. Agents Chemother , vol.29 , pp. 496-500
    • Moore, R.A.1    Bates, N.C.2    Hancock, R.E.3
  • 38
    • 0004064798 scopus 로고    scopus 로고
    • 3rd ed. Academic Press, London, United Kingdom
    • Nicholls, D., and S. Ferguson. 2002. Bioenergetics 3,3rd ed. Academic Press, London, United Kingdom.
    • (2002) Bioenergetics , vol.3
    • Nicholls, D.1    Ferguson, S.2
  • 39
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-656.
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 40
    • 0028139998 scopus 로고
    • Antibacterial synergism of polymyxin B nonapeptide and hydrophobic antibiotics in experimental gram-negative infections in mice
    • Ofek, I., S. Cohen, R. Rahmani, K. Kabha, D. Tamarkin, Y. Herzig, and E. Rubinstein. 1994. Antibacterial synergism of polymyxin B nonapeptide and hydrophobic antibiotics in experimental gram-negative infections in mice. Antimicrob. Agents Chemother. 38:374-377.
    • (1994) Antimicrob. Agents Chemother , vol.38 , pp. 374-377
    • Ofek, I.1    Cohen, S.2    Rahmani, R.3    Kabha, K.4    Tamarkin, D.5    Herzig, Y.6    Rubinstein, E.7
  • 41
    • 0032577249 scopus 로고    scopus 로고
    • Osmotic stress in viable Escherichia coli as the basis for the antibiotic response by polymyxin B
    • Oh, J. T., T. K. Van Dyk, Y. Cajal, P. S. Dhurjati, M. Sasser, and M. K. Jain. 1998. Osmotic stress in viable Escherichia coli as the basis for the antibiotic response by polymyxin B. Biochem. Biophys. Res. Commun. 246:619-623.
    • (1998) Biochem. Biophys. Res. Commun , vol.246 , pp. 619-623
    • Oh, J.T.1    Van Dyk, T.K.2    Cajal, Y.3    Dhurjati, P.S.4    Sasser, M.5    Jain, M.K.6
  • 42
    • 0036289543 scopus 로고    scopus 로고
    • Depolarization of the membrane potential by beta-lactams as a signal to induce autolysis
    • Penyige, A., J. Matko, E. Deak, A. Bodnar, and G. Barabas. 2002. Depolarization of the membrane potential by beta-lactams as a signal to induce autolysis. Biochem. Biophys. Res. Commun. 290:1169-1175.
    • (2002) Biochem. Biophys. Res. Commun , vol.290 , pp. 1169-1175
    • Penyige, A.1    Matko, J.2    Deak, E.3    Bodnar, A.4    Barabas, G.5
  • 43
    • 0014077554 scopus 로고
    • Prevention by polymyxin B of endotoxin lethality in mice
    • Rifkind, D. 1967. Prevention by polymyxin B of endotoxin lethality in mice. J. Bacteriol. 93:1463-1464.
    • (1967) J. Bacteriol , vol.93 , pp. 1463-1464
    • Rifkind, D.1
  • 45
    • 0023848271 scopus 로고
    • Interaction of macrophage cationic proteins with the outer membrane of Pseudomonas aeruginosa
    • Sawyer, J. G., N. L. Martin, and R. E. Hancock. 1988. Interaction of macrophage cationic proteins with the outer membrane of Pseudomonas aeruginosa. Infect. Immun. 56:693-698.
    • (1988) Infect. Immun , vol.56 , pp. 693-698
    • Sawyer, J.G.1    Martin, N.L.2    Hancock, R.E.3
  • 46
    • 0020037912 scopus 로고
    • Mechanisms of antibiotic-induced nephrotoxicity
    • Seale, T. W., and O. M. Rennert. 1982. Mechanisms of antibiotic-induced nephrotoxicity. Ann. Clin. Lab. Sci. 12:1-10.
    • (1982) Ann. Clin. Lab. Sci , vol.12 , pp. 1-10
    • Seale, T.W.1    Rennert, O.M.2
  • 48
    • 0016658917 scopus 로고
    • Capacity of the outer membrane of a gram-negative marine bacterium in the presence of cations to prevent lysis by Triton X-100
    • Unemoto, T., and R. A. MacLeod. 1975. Capacity of the outer membrane of a gram-negative marine bacterium in the presence of cations to prevent lysis by Triton X-100. J. Bacteriol. 121:800-806.
    • (1975) J. Bacteriol , vol.121 , pp. 800-806
    • Unemoto, T.1    MacLeod, R.A.2
  • 49
    • 0020583794 scopus 로고
    • Polycations as outer membrane-disorganizing agents
    • Vaara, M., and T. Vaara. 1983. Polycations as outer membrane-disorganizing agents. Antimicrob. Agents Chemother. 24:114-122.
    • (1983) Antimicrob. Agents Chemother , vol.24 , pp. 114-122
    • Vaara, M.1    Vaara, T.2
  • 50
    • 0020641094 scopus 로고
    • Polycations sensitize enteric bacteria to antibiotics
    • Vaara, M., and T. Vaara. 1983. Polycations sensitize enteric bacteria to antibiotics. Antimicrob. Agents Chemother. 24:107-113.
    • (1983) Antimicrob. Agents Chemother , vol.24 , pp. 107-113
    • Vaara, M.1    Vaara, T.2
  • 51
    • 0020638314 scopus 로고
    • Sensitization of Gram-negative bacteria to antibiotics and complement by a nontoxic oligopeptide
    • Vaara, M., and T. Vaara. 1983. Sensitization of Gram-negative bacteria to antibiotics and complement by a nontoxic oligopeptide. Nature 303:526-528.
    • (1983) Nature , vol.303 , pp. 526-528
    • Vaara, M.1    Vaara, T.2
  • 52
    • 0033546193 scopus 로고    scopus 로고
    • A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase
    • Wada, T., J. C. Long, D. Zhang, and S. B. Vik. 1999. A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase. J. Biol. Chem. 274:17353-17357.
    • (1999) J. Biol. Chem , vol.274 , pp. 17353-17357
    • Wada, T.1    Long, J.C.2    Zhang, D.3    Vik, S.B.4
  • 53
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • Wu, M., E. Maier, R. Benz, and R. E. Hancock. 1999. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38:7235-7242.
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.