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Volumn 10, Issue 4, 2014, Pages

Cationic Antimicrobial Peptides Promote Microbial Mutagenesis and Pathoadaptation in Chronic Infections

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; DNA POLYMERASE; GENOMIC DNA; REACTIVE OXYGEN METABOLITE; RIFAMPICIN; BACTERIAL DNA; BACTERIAL PROTEIN; CAP18 LIPOPOLYSACCHARIDE-BINDING PROTEIN; MUCA PROTEIN, PSEUDOMONAS;

EID: 84901342125     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004083     Document Type: Article
Times cited : (69)

References (69)
  • 1
    • 0346505482 scopus 로고    scopus 로고
    • New concepts of the pathogenesis of cystic fibrosis lung disease
    • Boucher R, (2004) New concepts of the pathogenesis of cystic fibrosis lung disease. European Respiratory Journal 23: 146.
    • (2004) European Respiratory Journal , vol.23 , pp. 146
    • Boucher, R.1
  • 4
    • 0027074880 scopus 로고
    • Emergence and persistence of Pseudomonas aeruginosa in the cystic fibrosis airway
    • Fick R, Sonoda F, Hornick D, (1992) Emergence and persistence of Pseudomonas aeruginosa in the cystic fibrosis airway. Sem Resp Infec 7: 168-178.
    • (1992) Sem Resp Infec , vol.7 , pp. 168-178
    • Fick, R.1    Sonoda, F.2    Hornick, D.3
  • 5
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan JR, Deretic V, (1996) Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia. Microbiol Rev 60: 539-574.
    • (1996) Microbiol Rev , vol.60 , pp. 539-574
    • Govan, J.R.1    Deretic, V.2
  • 6
    • 17144382063 scopus 로고    scopus 로고
    • Understanding the control of Pseudomonas aeruginosa alginate synthesis and the prospects for management of chronic infections in cystic fibrosis
    • Ramsey D, Wozniak D, (2005) Understanding the control of Pseudomonas aeruginosa alginate synthesis and the prospects for management of chronic infections in cystic fibrosis. Mol Microbiol 56: 309-332.
    • (2005) Mol Microbiol , vol.56 , pp. 309-332
    • Ramsey, D.1    Wozniak, D.2
  • 7
    • 0027267656 scopus 로고
    • Mechanism of conversion to mucoidy in Pseudomonas aeruginosa infecting cystic fibrosis patients
    • Martin DW, Schurr MJ, Mudd MH, Govan JR, Holloway BW, et al. (1993) Mechanism of conversion to mucoidy in Pseudomonas aeruginosa infecting cystic fibrosis patients. Proc Natl Acad Sci USA 90: 8377-8381.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8377-8381
    • Martin, D.W.1    Schurr, M.J.2    Mudd, M.H.3    Govan, J.R.4    Holloway, B.W.5
  • 8
    • 84860557951 scopus 로고    scopus 로고
    • Proteolytic regulation of alginate overproduction in Pseudomonas aeruginosa
    • doi:10.1111/j.1365-2958.2012.08049.x
    • Damron FH, Goldberg JB, (2012) Proteolytic regulation of alginate overproduction in Pseudomonas aeruginosa. Mol Microbiol 84: 595-607 doi:10.1111/j.1365-2958.2012.08049.x.
    • (2012) Mol Microbiol , vol.84 , pp. 595-607
    • Damron, F.H.1    Goldberg, J.B.2
  • 9
    • 84901296880 scopus 로고
    • A revised chromosomal location for muc: a locus involved in the control of alginate production by mucoid Pseudomonas aeruginosa
    • Fyfe J, Govan J, (1981) A revised chromosomal location for muc: a locus involved in the control of alginate production by mucoid Pseudomonas aeruginosa. Soc Gen Microbiol Q 8: 250-251.
    • (1981) Soc Gen Microbiol Q , vol.8 , pp. 250-251
    • Fyfe, J.1    Govan, J.2
  • 10
    • 0022509744 scopus 로고
    • Transfer of a chromosomal locus responsible for mucoid colony morphology in Pseudomonas aeruginosa isolated from cystic fibrosis patients to P. aeruginosa PAO
    • MacGeorge J, Korolik V, Morgan A, Ashe V, Holloway B, (1986) Transfer of a chromosomal locus responsible for mucoid colony morphology in Pseudomonas aeruginosa isolated from cystic fibrosis patients to P. aeruginosa PAO. J Med Microbiol 21: 331-336.
    • (1986) J Med Microbiol , vol.21 , pp. 331-336
    • MacGeorge, J.1    Korolik, V.2    Morgan, A.3    Ashe, V.4    Holloway, B.5
  • 11
    • 0023885755 scopus 로고
    • Cloning of genes from mucoid Pseudomonas aeruginosa which control spontaneous conversion to the alginate production phenotype
    • Flynn J, Ohman D, (1988) Cloning of genes from mucoid Pseudomonas aeruginosa which control spontaneous conversion to the alginate production phenotype. J Bacteriol 170: 1452-1460.
    • (1988) J Bacteriol , vol.170 , pp. 1452-1460
    • Flynn, J.1    Ohman, D.2
  • 12
    • 0019136294 scopus 로고
    • Alginate synthesis in mucoid Pseudomonas aeruginosa: a chromosomal locus involved in control
    • Fyfe JA, Govan JR, (1980) Alginate synthesis in mucoid Pseudomonas aeruginosa: a chromosomal locus involved in control. J Gen Microbiol 119: 443-450.
    • (1980) J Gen Microbiol , vol.119 , pp. 443-450
    • Fyfe, J.A.1    Govan, J.R.2
  • 13
    • 0033056054 scopus 로고    scopus 로고
    • Mucoid conversion of Pseudomonas aeruginosa by hydrogen peroxide: a mechanism for virulence activation in the cystic fibrosis lung
    • Mathee K, Ciofu O, Sternberg C, Lindum PW, Campbell JI, et al. (1999) Mucoid conversion of Pseudomonas aeruginosa by hydrogen peroxide: a mechanism for virulence activation in the cystic fibrosis lung. Microbiology 145: 1349-1357.
    • (1999) Microbiology , vol.145 , pp. 1349-1357
    • Mathee, K.1    Ciofu, O.2    Sternberg, C.3    Lindum, P.W.4    Campbell, J.I.5
  • 14
    • 34247342240 scopus 로고    scopus 로고
    • MutS deficiency and activity of the error-prone DNA polymerase IV are crucial for determining mucA as the main target for mucoid conversion in Pseudomonas aeruginosa
    • doi:10.1111/j.1365-2958.2007.05675.x
    • Moyano AJ, Luján AM, Argaraña CE, Smania AM, (2007) MutS deficiency and activity of the error-prone DNA polymerase IV are crucial for determining mucA as the main target for mucoid conversion in Pseudomonas aeruginosa. Mol Microbiol 64: 547-559 doi:10.1111/j.1365-2958.2007.05675.x.
    • (2007) Mol Microbiol , vol.64 , pp. 547-559
    • Moyano, A.J.1    Luján, A.M.2    Argaraña, C.E.3    Smania, A.M.4
  • 15
    • 33845446266 scopus 로고    scopus 로고
    • Role of Pseudomonas aeruginosa dinB-encoded DNA polymerase IV in mutagenesis
    • doi:10.1128/JB.01481-06
    • Sanders LH, Rockel A, Lu H, Wozniak DJ, Sutton MD, (2006) Role of Pseudomonas aeruginosa dinB-encoded DNA polymerase IV in mutagenesis. J Bacteriol 188: 8573-8585 doi:10.1128/JB.01481-06.
    • (2006) J Bacteriol , vol.188 , pp. 8573-8585
    • Sanders, L.H.1    Rockel, A.2    Lu, H.3    Wozniak, D.J.4    Sutton, M.D.5
  • 16
    • 77950648700 scopus 로고    scopus 로고
    • Genetic adaptation of Pseudomonas aeruginosa during chronic lung infection of patients with cystic fibrosis: strong and weak mutators with heterogeneous genetic backgrounds emerge in mucA and/or lasR mutants
    • doi:10.1099/mic.0.033993-0
    • Ciofu O, Mandsberg LF, Bjarnsholt T, Wassermann T, Hoiby N, (2010) Genetic adaptation of Pseudomonas aeruginosa during chronic lung infection of patients with cystic fibrosis: strong and weak mutators with heterogeneous genetic backgrounds emerge in mucA and/or lasR mutants. Microbiology 156: 1108-1119 doi:10.1099/mic.0.033993-0.
    • (2010) Microbiology , vol.156 , pp. 1108-1119
    • Ciofu, O.1    Mandsberg, L.F.2    Bjarnsholt, T.3    Wassermann, T.4    Hoiby, N.5
  • 17
    • 78549263685 scopus 로고    scopus 로고
    • Adaptation of Pseudomonas aeruginosa during persistence in the cystic fibrosis lung
    • Hogardt M, Heesemann J, (2010) Adaptation of Pseudomonas aeruginosa during persistence in the cystic fibrosis lung. International Journal of Medical Microbiology 300: 557-562.
    • (2010) International Journal of Medical Microbiology , vol.300 , pp. 557-562
    • Hogardt, M.1    Heesemann, J.2
  • 18
    • 33845623880 scopus 로고    scopus 로고
    • Stage-specific adaptation of hypermutable Pseudomonas aeruginosa isolates during chronic pulmonary infection in patients with cystic fibrosis
    • doi:10.1086/509821
    • Hogardt M, Hoboth C, Schmoldt S, Henke C, Bader L, et al. (2007) Stage-specific adaptation of hypermutable Pseudomonas aeruginosa isolates during chronic pulmonary infection in patients with cystic fibrosis. J Infect Dis 195: 70-80 doi:10.1086/509821.
    • (2007) J Infect Dis , vol.195 , pp. 70-80
    • Hogardt, M.1    Hoboth, C.2    Schmoldt, S.3    Henke, C.4    Bader, L.5
  • 19
    • 42949094250 scopus 로고    scopus 로고
    • Dynamics of Pseudomonas aeruginosa genome evolution
    • doi:10.1073/pnas.0711982105
    • Mathee K, Narasimhan G, Valdes C, Qiu X, Matewish JM, et al. (2008) Dynamics of Pseudomonas aeruginosa genome evolution. Proc Natl Acad Sci U S A 105: 3100-3105 doi:10.1073/pnas.0711982105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3100-3105
    • Mathee, K.1    Narasimhan, G.2    Valdes, C.3    Qiu, X.4    Matewish, J.M.5
  • 20
    • 33749181103 scopus 로고    scopus 로고
    • Cell wall-inhibitory antibiotics activate the alginate biosynthesis operon in Pseudomonas aeruginosa: Roles of sigma (AlgT) and the AlgW and Prc proteases
    • doi:10.1111/j.1365-2958.2006.05390.x
    • Wood LF, Leech AJ, Ohman DE, (2006) Cell wall-inhibitory antibiotics activate the alginate biosynthesis operon in Pseudomonas aeruginosa: Roles of sigma (AlgT) and the AlgW and Prc proteases. Mol Microbiol 62: 412-426 doi:10.1111/j.1365-2958.2006.05390.x.
    • (2006) Mol Microbiol , vol.62 , pp. 412-426
    • Wood, L.F.1    Leech, A.J.2    Ohman, D.E.3
  • 21
    • 0026013571 scopus 로고
    • Pseudomonas aeruginosa AlgB, a two-component response regulator of the NtrC-family, is required for algD transcription
    • Wozniak D, Ohman D, (1991) Pseudomonas aeruginosa AlgB, a two-component response regulator of the NtrC-family, is required for algD transcription. J Bacteriol 173: 1406-1413.
    • (1991) J Bacteriol , vol.173 , pp. 1406-1413
    • Wozniak, D.1    Ohman, D.2
  • 22
    • 79955146435 scopus 로고    scopus 로고
    • Epistatic Roles for Pseudomonas aeruginosa MutS and DinB (DNA Pol IV) in Coping with Reactive Oxygen Species-Induced DNA Damage
    • doi:10.1371/journal.pone.0018824
    • Sanders LH, Devadoss B, Raja GV, O'Connor J, Shengchang S, et al. (2011) Epistatic Roles for Pseudomonas aeruginosa MutS and DinB (DNA Pol IV) in Coping with Reactive Oxygen Species-Induced DNA Damage. PLoS ONE 6: e18824 doi:10.1371/journal.pone.0018824.
    • (2011) PLoS ONE , vol.6
    • Sanders, L.H.1    Devadoss, B.2    Raja, G.V.3    O'Connor, J.4    Shengchang, S.5
  • 23
    • 0036167851 scopus 로고    scopus 로고
    • Effects of reduced mucus oxygen concentration in airway Pseudomonas infections of cystic fibrosis patients
    • Worlitzsch D, Tarran R, Ulrich M, Schwab U, Cekici A, et al. (2002) Effects of reduced mucus oxygen concentration in airway Pseudomonas infections of cystic fibrosis patients. J Clin Inves 109: 317-325.
    • (2002) J Clin Inves , vol.109 , pp. 317-325
    • Worlitzsch, D.1    Tarran, R.2    Ulrich, M.3    Schwab, U.4    Cekici, A.5
  • 24
    • 78549290620 scopus 로고    scopus 로고
    • Anaerobic physiology of Pseudomonas aeruginosa in the cystic fibrosis lung
    • doi:10.1016/j.ijmm.2010.08.007
    • Schobert M, Jahn D, (2010) Anaerobic physiology of Pseudomonas aeruginosa in the cystic fibrosis lung. Int J Med Microbiol 300: 549-556 doi:10.1016/j.ijmm.2010.08.007.
    • (2010) Int J Med Microbiol , vol.300 , pp. 549-556
    • Schobert, M.1    Jahn, D.2
  • 25
    • 27144462218 scopus 로고    scopus 로고
    • Sputum Cathelicidin, Urokinase Plasminogen Activation System Components, and Cytokines Discriminate Cystic Fibrosis, COPD, and Asthma Inflammation
    • doi:10.1378/chest.128.4.2316
    • Xiao W, (2005) Sputum Cathelicidin, Urokinase Plasminogen Activation System Components, and Cytokines Discriminate Cystic Fibrosis, COPD, and Asthma Inflammation. Chest 128: 2316-2326 doi:10.1378/chest.128.4.2316.
    • (2005) Chest , vol.128 , pp. 2316-2326
    • Xiao, W.1
  • 26
    • 51949104801 scopus 로고    scopus 로고
    • Human host defense peptide LL-37 prevents bacterial biofilm formation
    • doi:10.1128/IAI.00318-08
    • Overhage J, Campisano A, Bains M, Torfs ECW, Rehm BHA, et al. (2008) Human host defense peptide LL-37 prevents bacterial biofilm formation. Infect Immun 76: 4176-4182 doi:10.1128/IAI.00318-08.
    • (2008) Infect Immun , vol.76 , pp. 4176-4182
    • Overhage, J.1    Campisano, A.2    Bains, M.3    Torfs, E.C.W.4    Rehm, B.H.A.5
  • 27
    • 84857411069 scopus 로고    scopus 로고
    • Designing antimicrobial peptides: form follows function
    • doi:10.1038/nrd3591
    • Fjell CD, Hiss JA, Hancock REW, Schneider G, (2011) Designing antimicrobial peptides: form follows function. Nat Rev Drug Discov 11: 37-51 doi:10.1038/nrd3591.
    • (2011) Nat Rev Drug Discov , vol.11 , pp. 37-51
    • Fjell, C.D.1    Hiss, J.A.2    Hancock, R.E.W.3    Schneider, G.4
  • 28
    • 84871027267 scopus 로고    scopus 로고
    • A comprehensive summary of LL-37, the factotum human cathelicidin peptide
    • doi:10.1016/j.cellimm.2012.11.009
    • Vandamme D, Landuyt B, Luyten W, Schoofs L, (2012) A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cellular Immunology 280: 22-35 doi:10.1016/j.cellimm.2012.11.009.
    • (2012) Cellular Immunology , vol.280 , pp. 22-35
    • Vandamme, D.1    Landuyt, B.2    Luyten, W.3    Schoofs, L.4
  • 29
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sørensen OE, Follin P, Johnsen AH, Calafat J, Tjabringa GS, et al. (2001) Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97: 3951-3959.
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sørensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5
  • 30
  • 31
    • 33750944535 scopus 로고    scopus 로고
    • The antimicrobial peptide cathelicidin interacts with airway mucus
    • doi:10.1016/j.peptides.2006.07.018
    • Felgentreff K, Beisswenger C, Griese M, Gulder T, Bringmann G, et al. (2006) The antimicrobial peptide cathelicidin interacts with airway mucus. Peptides 27: 3100-3106 doi:10.1016/j.peptides.2006.07.018.
    • (2006) Peptides , vol.27 , pp. 3100-3106
    • Felgentreff, K.1    Beisswenger, C.2    Griese, M.3    Gulder, T.4    Bringmann, G.5
  • 32
    • 34147139491 scopus 로고    scopus 로고
    • Release of the antimicrobial peptide LL-37 from DNA/F-actin bundles in cystic fibrosis sputum
    • doi:10.1183/09031936.00080806
    • Bucki R, Byfield FJ, Janmey PA, (2007) Release of the antimicrobial peptide LL-37 from DNA/F-actin bundles in cystic fibrosis sputum. Eur Respir J 29: 624-632 doi:10.1183/09031936.00080806.
    • (2007) Eur Respir J , vol.29 , pp. 624-632
    • Bucki, R.1    Byfield, F.J.2    Janmey, P.A.3
  • 33
    • 0037315058 scopus 로고    scopus 로고
    • Whole-Genome Sequence Variation among Multiple Isolates of Pseudomonas aeruginosa
    • doi:10.1128/JB.185.4.1316-1325.2003
    • Spencer DH, Kas A, Smith EE, Raymond CK, Sims EH, et al. (2003) Whole-Genome Sequence Variation among Multiple Isolates of Pseudomonas aeruginosa. J Bacteriol 185: 1316-1325 doi:10.1128/JB.185.4.1316-1325.2003.
    • (2003) J Bacteriol , vol.185 , pp. 1316-1325
    • Spencer, D.H.1    Kas, A.2    Smith, E.E.3    Raymond, C.K.4    Sims, E.H.5
  • 34
    • 0036702244 scopus 로고    scopus 로고
    • Genetic Analysis of Pseudomonas aeruginosa Isolates from the Sputa of Australian Adult Cystic Fibrosis Patients
    • doi:10.1128/JCM.40.8.2772-2778.2002
    • Anthony M, Rose B, Pegler MB, Elkins M, Service H, et al. (2002) Genetic Analysis of Pseudomonas aeruginosa Isolates from the Sputa of Australian Adult Cystic Fibrosis Patients. Journal of Clinical Microbiology 40: 2772-2778 doi:10.1128/JCM.40.8.2772-2778.2002.
    • (2002) Journal of Clinical Microbiology , vol.40 , pp. 2772-2778
    • Anthony, M.1    Rose, B.2    Pegler, M.B.3    Elkins, M.4    Service, H.5
  • 35
    • 33750962335 scopus 로고    scopus 로고
    • Sequence diversity of the mucABD locus in Pseudomonas aeruginosa isolates from patients with cystic fibrosis
    • doi:10.1099/mic.0.29175-0
    • Bragonzi A, Wiehlmann L, Klockgether J, Cramer N, Worlitzsch D, et al. (2006) Sequence diversity of the mucABD locus in Pseudomonas aeruginosa isolates from patients with cystic fibrosis. Microbiology 152: 3261-3269 doi:10.1099/mic.0.29175-0.
    • (2006) Microbiology , vol.152 , pp. 3261-3269
    • Bragonzi, A.1    Wiehlmann, L.2    Klockgether, J.3    Cramer, N.4    Worlitzsch, D.5
  • 36
    • 0030931824 scopus 로고    scopus 로고
    • Mucoid Pseudomonas aeruginosa in cystic fibrosis: characterization of muc mutations in clinical isolates and analysis of clearance in a mouse model of respiratory infection
    • Boucher J, Yu H, Mudd M, Deretic V, (1997) Mucoid Pseudomonas aeruginosa in cystic fibrosis: characterization of muc mutations in clinical isolates and analysis of clearance in a mouse model of respiratory infection. Infection and Immunity 65: 3838-3846.
    • (1997) Infection and Immunity , vol.65 , pp. 3838-3846
    • Boucher, J.1    Yu, H.2    Mudd, M.3    Deretic, V.4
  • 37
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • doi:10.1146/annurev.biochem.77.061606.161055
    • Imlay JA, (2008) Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77: 755-776 doi:10.1146/annurev.biochem.77.061606.161055.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 38
    • 0000918686 scopus 로고    scopus 로고
    • The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis
    • Wagner J, Gruz P, Kim S, Yamada M, Matsui K, et al. (1999) The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis. Molecular Cell 4: 281-286.
    • (1999) Molecular Cell , vol.4 , pp. 281-286
    • Wagner, J.1    Gruz, P.2    Kim, S.3    Yamada, M.4    Matsui, K.5
  • 39
    • 4644351908 scopus 로고    scopus 로고
    • SOS Response Induction by Beta-Lactams and Bacterial Defense Against Antibiotic Lethality
    • doi:10.1126/science.1101630
    • Miller C, (2004) SOS Response Induction by Beta-Lactams and Bacterial Defense Against Antibiotic Lethality. Science 305: 1629-1631 doi:10.1126/science.1101630.
    • (2004) Science , vol.305 , pp. 1629-1631
    • Miller, C.1
  • 40
    • 0028910517 scopus 로고
    • Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA
    • doi:10.1038/373721a0
    • He J, Furmanski P, (1995) Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature 373: 721-724 doi:10.1038/373721a0.
    • (1995) Nature , vol.373 , pp. 721-724
    • He, J.1    Furmanski, P.2
  • 41
    • 23044452974 scopus 로고    scopus 로고
    • Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA
    • doi:10.1093/nar/gki725
    • Hsu CH, (2005) Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA. Nucleic Acids Research 33: 4053-4064 doi:10.1093/nar/gki725.
    • (2005) Nucleic Acids Research , vol.33 , pp. 4053-4064
    • Hsu, C.H.1
  • 42
    • 33750971755 scopus 로고    scopus 로고
    • Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites
    • doi:10.1093/nar/gkl667
    • Marchand C, Krajewski K, Lee HF, Antony S, Johnson AA, et al. (2006) Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites. Nucleic Acids Research 34: 5157-5165 doi:10.1093/nar/gkl667.
    • (2006) Nucleic Acids Research , vol.34 , pp. 5157-5165
    • Marchand, C.1    Krajewski, K.2    Lee, H.F.3    Antony, S.4    Johnson, A.A.5
  • 43
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • doi:10.1006/bbrc.1998.8159
    • Park CB, Kim HS, Kim SC, (1998) Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem Biophys Res Commun 244: 253-257 doi:10.1006/bbrc.1998.8159.
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 44
    • 0032031434 scopus 로고    scopus 로고
    • Mechanism of antimicrobial action of indolicidin
    • Subbalakshmi C, Sitaram N, (1998) Mechanism of antimicrobial action of indolicidin. FEMS Microbiol Lett 160: 91-96.
    • (1998) FEMS Microbiol Lett , vol.160 , pp. 91-96
    • Subbalakshmi, C.1    Sitaram, N.2
  • 45
    • 78650338718 scopus 로고    scopus 로고
    • Spotlight on human LL-37, an immunomodulatory peptide with promising cell-penetrating properties
    • Seil M, Nagant C, Dehaye JP, Vandenbranden M, Lensink MF, (2010) Spotlight on human LL-37, an immunomodulatory peptide with promising cell-penetrating properties. Pharmaceuticals 3: 3435-3460.
    • (2010) Pharmaceuticals , vol.3 , pp. 3435-3460
    • Seil, M.1    Nagant, C.2    Dehaye, J.P.3    Vandenbranden, M.4    Lensink, M.F.5
  • 46
    • 34948862264 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide
    • doi:10.1038/nature06116
    • Lande R, Gregorio J, Facchinetti V, Chatterjee B, Wang Y-H, et al. (2007) Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature 449: 564-569 doi:10.1038/nature06116.
    • (2007) Nature , vol.449 , pp. 564-569
    • Lande, R.1    Gregorio, J.2    Facchinetti, V.3    Chatterjee, B.4    Wang, Y.-H.5
  • 47
    • 79955637689 scopus 로고    scopus 로고
    • Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37
    • doi:10.1073/pnas.1101130108
    • Sochacki KA, Barns KJ, Bucki R, Weisshaar JC, (2011) Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37. Proc Natl Acad Sci U S A 108: E77-E81 doi:10.1073/pnas.1101130108.
    • (2011) Proc Natl Acad Sci U S A , vol.108
    • Sochacki, K.A.1    Barns, K.J.2    Bucki, R.3    Weisshaar, J.C.4
  • 48
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • doi:10.1038/415389a
    • Zasloff M, (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395 doi:10.1038/415389a.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 49
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • doi:10.1016/S0005-2736(99)00200-X
    • Shai Y, (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochimica et Biophysica Acta (BBA)- Biomembranes 1462: 55-70 doi:10.1016/S0005-2736(99)00200-X.
    • (1999) Biochimica Et Biophysica Acta (BBA) - Biomembranes , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 50
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • doi:10.1016/S0005-2736(99)00197-2
    • Matsuzaki K, (1999) Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochimica et Biophysica Acta (BBA)- Biomembranes 1462: 1-10 doi:10.1016/S0005-2736(99)00197-2.
    • (1999) Biochimica Et Biophysica Acta (BBA) - Biomembranes , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 51
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: magainin and protegrin
    • doi:10.1016/S0006-3495(00)76448-4
    • Yang L, Weiss TM, Lehrer RI, Huang HW, (2000) Crystallization of antimicrobial pores in membranes: magainin and protegrin. Biophys J 79: 2002-2009 doi:10.1016/S0006-3495(00)76448-4.
    • (2000) Biophys J , vol.79 , pp. 2002-2009
    • Yang, L.1    Weiss, T.M.2    Lehrer, R.I.3    Huang, H.W.4
  • 52
    • 84874380157 scopus 로고    scopus 로고
    • Antibacterial activity and dual mechanisms of peptide analog derived from cell-penetrating peptide against Salmonella typhimurium and Streptococcus pyogenes
    • doi:10.1007/s00253-012-4352-1
    • Li L, Shi Y, Cheserek MJ, Su G, Le G, (2013) Antibacterial activity and dual mechanisms of peptide analog derived from cell-penetrating peptide against Salmonella typhimurium and Streptococcus pyogenes. Appl Microbiol Biotechnol 97: 1711-1723 doi:10.1007/s00253-012-4352-1.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 1711-1723
    • Li, L.1    Shi, Y.2    Cheserek, M.J.3    Su, G.4    Le, G.5
  • 53
    • 19444383801 scopus 로고
    • Trading Places: How Do DNA Polymerases Switch During Translesion DNA Synthesis
    • doi:10.1016/j.molcel.2005.03.032
    • Friedberg E, Lehmann A, Fuchs R, (1995) Trading Places: How Do DNA Polymerases Switch During Translesion DNA Synthesis? Molecular Cell 18: 499-505 doi:10.1016/j.molcel.2005.03.032.
    • (1995) Molecular Cell , vol.18 , pp. 499-505
    • Friedberg, E.1    Lehmann, A.2    Fuchs, R.3
  • 54
    • 52649093934 scopus 로고    scopus 로고
    • Interactions between branched DNAs and peptide inhibitors of DNA repair
    • doi:10.1093/nar/gkn512
    • Kepple KV, Patel N, Salamon P, Segall AM, (2008) Interactions between branched DNAs and peptide inhibitors of DNA repair. Nucleic Acids Research 36: 5319-5334 doi:10.1093/nar/gkn512.
    • (2008) Nucleic Acids Research , vol.36 , pp. 5319-5334
    • Kepple, K.V.1    Patel, N.2    Salamon, P.3    Segall, A.M.4
  • 55
    • 77951224521 scopus 로고    scopus 로고
    • An Antimicrobial Peptide That Targets DNA Repair Intermediates In Vitro Inhibits Salmonella Growth within Murine Macrophages
    • doi:10.1128/AAC.01610-09
    • Su DLWAMS Leo Y, (2010) An Antimicrobial Peptide That Targets DNA Repair Intermediates In Vitro Inhibits Salmonella Growth within Murine Macrophages. Antimicrobial Agents and Chemotherapy 54: 1888 doi:10.1128/AAC.01610-09.
    • (2010) Antimicrobial Agents and Chemotherapy , vol.54 , pp. 1888
    • Su, D.L.W.A.M.S.1    Leo, Y.2
  • 56
    • 55949099388 scopus 로고    scopus 로고
    • Induction of group A Streptococcus virulence by a human antimicrobial peptide
    • Induction of group A Streptococcus virulence by a human antimicrobial peptide
    • Induction of group A Streptococcus virulence by a human antimicrobial peptide (2008) Induction of group A Streptococcus virulence by a human antimicrobial peptide. 105: 16755-16760.
    • (2008) , vol.105 , pp. 16755-16760
  • 57
    • 0036264599 scopus 로고    scopus 로고
    • Neutrophils and the Pathogenesis of COPD
    • doi:10.1378/chest.121.5_suppl.151S
    • Stockley RA, (2002) Neutrophils and the Pathogenesis of COPD. Chest 121: 151S-155S doi:_10.1378/chest.121.5_suppl.151S.
    • (2002) Chest , vol.121
    • Stockley, R.A.1
  • 58
    • 84879291920 scopus 로고    scopus 로고
    • The Neutrophil in Chronic Obstructive Pulmonary Disease. Too Little, Too Late or Too Much, Too Soon
    • 0.1165/rcmb.2012-0492TR
    • Hoenderdos K, Condliffe A, The Neutrophil in Chronic Obstructive Pulmonary Disease. Too Little, Too Late or Too Much, Too Soon? Am J Respir Cell Mol Biol 48: 531-539 doi:0.1165/rcmb.2012-0492TR.
    • Am J Respir Cell Mol Biol , vol.48 , pp. 531-539
    • Hoenderdos, K.1    Condliffe, A.2
  • 59
    • 42649133154 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa in Chronic Obstructive Pulmonary Disease
    • doi:10.1164/rccm.200709-1413OC
    • Murphy TF, Brauer AL, Eschberger K, Lobbins P, Grove L, et al. (2008) Pseudomonas aeruginosa in Chronic Obstructive Pulmonary Disease. Am J Respir Crit Care Med 177: 853-860 doi:10.1164/rccm.200709-1413OC.
    • (2008) Am J Respir Crit Care Med , vol.177 , pp. 853-860
    • Murphy, T.F.1    Brauer, A.L.2    Eschberger, K.3    Lobbins, P.4    Grove, L.5
  • 60
    • 0028015883 scopus 로고
    • Bronchoalveolar lavage findings in cystic fibrosis patients with stable, clinically mild lung disease suggest ongoing infection and inflammation
    • doi:10.1164/ajrccm.150.2.8049828
    • Konstan MW, Hilliard KA, Norvell TM, Berger M, (1994) Bronchoalveolar lavage findings in cystic fibrosis patients with stable, clinically mild lung disease suggest ongoing infection and inflammation. Am J Respir Crit Care Med 150: 448-454 doi:10.1164/ajrccm.150.2.8049828.
    • (1994) Am J Respir Crit Care Med , vol.150 , pp. 448-454
    • Konstan, M.W.1    Hilliard, K.A.2    Norvell, T.M.3    Berger, M.4
  • 61
    • 84900315796 scopus 로고    scopus 로고
    • Lung inflammation in Cystic Fibrosis: Pathogenesis and novel therapies
    • doi:10.1016/j.clinbiochem.2013.12.020
    • Dhooghe B, Noël S, Huaux F, Leal T, (2013) Lung inflammation in Cystic Fibrosis: Pathogenesis and novel therapies. Clin Biochem piiS0009-9120(13)00605-X doi:10.1016/j.clinbiochem.2013.12.020.
    • (2013) Clin Biochem
    • Dhooghe, B.1    Noël, S.2    Huaux, F.3    Leal, T.4
  • 62
    • 84887728119 scopus 로고    scopus 로고
    • The future of antimicrobial therapy in the era of antibiotic resistance in cystic fibrosis pulmonary infection
    • McCaughey G, Gilpin DF, Elborn JS, Tunney MM, (2013) The future of antimicrobial therapy in the era of antibiotic resistance in cystic fibrosis pulmonary infection. Expert Review of Respiratory Medicine 7: 385-396.
    • (2013) Expert Review of Respiratory Medicine , vol.7 , pp. 385-396
    • McCaughey, G.1    Gilpin, D.F.2    Elborn, J.S.3    Tunney, M.M.4
  • 63
    • 84874687957 scopus 로고    scopus 로고
    • Peptides as the next generation of anti-infectives
    • doi:10.4155/fmc.12.213
    • Mercer DK, O'Neil DA, (2013) Peptides as the next generation of anti-infectives. Future Medicinal Chemistry 5: 315-337 doi:10.4155/fmc.12.213.
    • (2013) Future Medicinal Chemistry , vol.5 , pp. 315-337
    • Mercer, D.K.1    O'Neil, D.A.2
  • 64
    • 83655163672 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa Psl polysaccharide reduces neutrophil phagocytosis and the oxidative response by limiting complement-mediated opsonization
    • doi:10.1111/j.1462-5822.2011.01704.x
    • Mishra M, Byrd MS, Sergeant S, Azad AK, Parsek MR, et al. (2012) Pseudomonas aeruginosa Psl polysaccharide reduces neutrophil phagocytosis and the oxidative response by limiting complement-mediated opsonization. Cell Microbiol 14: 95-106 doi:10.1111/j.1462-5822.2011.01704.x.
    • (2012) Cell Microbiol , vol.14 , pp. 95-106
    • Mishra, M.1    Byrd, M.S.2    Sergeant, S.3    Azad, A.K.4    Parsek, M.R.5
  • 65
    • 57149099185 scopus 로고    scopus 로고
    • PBAD-Based Shuttle Vectors for Functional Analysis of Toxic and Highly Regulated Genes in Pseudomonas and Burkholderia spp. and Other Bacteria
    • doi:10.1128/AEM.01369-08
    • Qiu D, Damron FH, Mima T, Schweizer HP, Yu HD, (2008) PBAD-Based Shuttle Vectors for Functional Analysis of Toxic and Highly Regulated Genes in Pseudomonas and Burkholderia spp. and Other Bacteria. Appl Environ Microbiol 74: 7422-7426 doi:10.1128/AEM.01369-08.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 7422-7426
    • Qiu, D.1    Damron, F.H.2    Mima, T.3    Schweizer, H.P.4    Yu, H.D.5
  • 66
    • 0014330073 scopus 로고
    • A new modification of the carbazole analysis: application to heteropolysaccharides
    • Knutson C, Jeanes A, (1968) A new modification of the carbazole analysis: application to heteropolysaccharides. Anal Biochem 24: 470-481.
    • (1968) Anal Biochem , vol.24 , pp. 470-481
    • Knutson, C.1    Jeanes, A.2
  • 67
    • 0031931507 scopus 로고    scopus 로고
    • Phosphorylation-independent activity of the response regulators AlgB and AlgR in promoting alginate biosynthesis in mucoid Pseudomonas aeruginosa
    • Ma S, Selvaraj U, Ohman DE, Quarless R, Hassett DJ, et al. (1998) Phosphorylation-independent activity of the response regulators AlgB and AlgR in promoting alginate biosynthesis in mucoid Pseudomonas aeruginosa. J Bacteriol 180: 956-968.
    • (1998) J Bacteriol , vol.180 , pp. 956-968
    • Ma, S.1    Selvaraj, U.2    Ohman, D.E.3    Quarless, R.4    Hassett, D.J.5
  • 68
    • 0032524465 scopus 로고    scopus 로고
    • Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 å resolution
    • doi:10.1016/S0969-2126(98)00067-7
    • Parraga A, Bellsolell L, Ferré-D'Amaré AR, Burley SK, (1998) Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 å resolution. Structure 6: 661-672 doi:10.1016/S0969-2126(98)00067-7.
    • (1998) Structure , vol.6 , pp. 661-672
    • Parraga, A.1    Bellsolell, L.2    Ferré-D'Amaré, A.R.3    Burley, S.K.4
  • 69
    • 0001641514 scopus 로고
    • Mutations of Bacteria from Virus Sensitivity to Virus Resistance
    • Luria SE, Delbrück M, (1943) Mutations of Bacteria from Virus Sensitivity to Virus Resistance. Genetics 28: 491-511.
    • (1943) Genetics , vol.28 , pp. 491-511
    • Luria, S.E.1    Delbrück, M.2


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