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Volumn 57, Issue 10, 2013, Pages 4707-4716

Effect of intracellular expression of antimicrobial peptide LL-37 on growth of escherichia coli strain TOP10 under aerobic and anaerobic conditions

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; REACTIVE OXYGEN METABOLITE;

EID: 84884241544     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00825-13     Document Type: Article
Times cited : (24)

References (33)
  • 1
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • Hale JD, Hancock RE. 2007. Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev. Anti Infect. Ther. 5:951-959.
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.1    Hancock, R.E.2
  • 2
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki K. 1999. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1462:1-10.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 3
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • Oren Z, Shai Y. 1998. Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers 47:451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 4
    • 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
  • 5
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. 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
  • 6
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman HG, Agerberth B, Boman A. 1993. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect. Immun. 61:2978-2984.
    • (1993) Infect. Immun. , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 7
    • 0026550672 scopus 로고
    • Binding of tachyplesin i to DNA revealed by footprinting analysis: Significant contribution of secondary structure toDNAbinding and implication for biological action
    • Yonezawa A, Kuwahara J, Fujii N, Sugiura Y. 1992. Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure toDNAbinding and implication for biological action. Biochemistry 31:2998-3004.
    • (1992) Biochemistry , vol.31 , pp. 2998-3004
    • Yonezawa, A.1    Kuwahara, J.2    Fujii, N.3    Sugiura, Y.4
  • 9
    • 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
    • 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.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 10
    • 0025066842 scopus 로고
    • Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins
    • Skerlavaj B, Romeo D, Gennaro R. 1990. Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins. Infect. Immun. 58:3724-3730.
    • (1990) Infect. Immun. , vol.58 , pp. 3724-3730
    • Skerlavaj, B.1    Romeo, D.2    Gennaro, R.3
  • 12
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson GH, Agerberth B, Odeberg J, Bergman T, Olsson B, Salcedo R. 1996. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238:325-332.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 14
    • 33748949579 scopus 로고    scopus 로고
    • Lipopolysaccharide (endotoxin)-host defense antibacterial peptides interactions: Role in bacterial resistance and prevention of sepsis
    • Rosenfeld Y, Shai Y. 2006. Lipopolysaccharide (endotoxin)-host defense antibacterial peptides interactions: role in bacterial resistance and prevention of sepsis. Biochim. Biophys. Acta 1758:1513-1522.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1513-1522
    • Rosenfeld, Y.1    Shai, Y.2
  • 15
    • 79959644039 scopus 로고    scopus 로고
    • Transmembrane pores formed by human antimicrobial peptide LL-37
    • Lee CC, Sun Y, Qian S, Huang HW. 2011. Transmembrane pores formed by human antimicrobial peptide LL-37. Biophys. J. 100:1688-1696.
    • (2011) Biophys. J. , vol.100 , pp. 1688-1696
    • Lee, C.C.1    Sun, Y.2    Qian, S.3    Huang, H.W.4
  • 16
    • 1542513868 scopus 로고    scopus 로고
    • Human betadefensins 2 and 3 demonstrate strain-selective activity against oral microorganisms
    • Joly S, Maze C, McCray PB, Jr, Guthmiller JM. 2004. Human betadefensins 2 and 3 demonstrate strain-selective activity against oral microorganisms. J. Clin. Microbiol. 42:1024-1029.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 1024-1029
    • Joly, S.1    Maze, C.2    McCray Jr., P.B.3    Guthmiller, J.M.4
  • 18
    • 57149099185 scopus 로고    scopus 로고
    • PBAD-based shuttle vectors for functional analysis of toxic and highly regulated genes in Pseudomonas and Burkholderia spp
    • 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.
    • (2008) And Other Bacteria. 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
  • 19
    • 1442330405 scopus 로고    scopus 로고
    • Interplay between antibacterial effectors: A macrophage antimicrobial peptide impairs intracellular Salmonella replication
    • Rosenberger CM, Gallo RL, Finlay BB. 2004. Interplay between antibacterial effectors: a macrophage antimicrobial peptide impairs intracellular Salmonella replication. Proc. Natl. Acad. Sci. U. S. A. 101:2422-2427.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2422-2427
    • Rosenberger, C.M.1    Gallo, R.L.2    Finlay, B.B.3
  • 20
    • 55449126342 scopus 로고    scopus 로고
    • Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death
    • Kohanski MA, Dwyer DJ, Wierzbowski J, Cottarel G, Collins JJ. 2008. Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death. Cell 135:679-690.
    • (2008) Cell , vol.135 , pp. 679-690
    • Kohanski, M.A.1    Dwyer, D.J.2    Wierzbowski, J.3    Cottarel, G.4    Collins, J.J.5
  • 22
    • 0030681260 scopus 로고    scopus 로고
    • The significance of digital gene expression profiles
    • Audic S, Claverie JM. 1997. The significance of digital gene expression profiles. Genome Res. 7:986-995.
    • (1997) Genome Res. , vol.7 , pp. 986-995
    • Audic, S.1    Claverie, J.M.2
  • 23
    • 0037228233 scopus 로고    scopus 로고
    • Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A
    • Hong RW, Shchepetov M, Weiser JN, Axelsen PH. 2003. Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A. Antimicrob. Agents Chemother. 47:1-6.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 1-6
    • Hong, R.W.1    Shchepetov, M.2    Weiser, J.N.3    Axelsen, P.H.4
  • 24
    • 33748693942 scopus 로고    scopus 로고
    • Prior antibacterial peptide-mediated inhibition of protein folding in bacteria mutes resistance enzymes
    • Otvos L, Jr, de Olivier Inacio V, Wade JD, Cudic P. 2006. Prior antibacterial peptide-mediated inhibition of protein folding in bacteria mutes resistance enzymes. Antimicrob. Agents Chemother. 50:3146-3149.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 3146-3149
    • Otvos Jr., L.1    De Olivier Inacio, V.2    Wade, J.D.3    Cudic, P.4
  • 25
    • 70349737935 scopus 로고    scopus 로고
    • Transcriptome analysis of the responses of Staphylococcus aureus to antimicrobial peptides and characterization of the roles of vraDE and vraSR in antimicrobial resistance
    • Pietiainen M, Francois P, Hyyrylainen HL, Tangomo M, Sass V, Sahl HG, Schrenzel J, Kontinen VP. 2009. Transcriptome analysis of the responses of Staphylococcus aureus to antimicrobial peptides and characterization of the roles of vraDE and vraSR in antimicrobial resistance. BMC Genomics 10:429-443.
    • (2009) BMC Genomics , vol.10 , pp. 429-443
    • Pietiainen, M.1    Francois, P.2    Hyyrylainen, H.L.3    Tangomo, M.4    Sass, V.5    Sahl, H.G.6    Schrenzel, J.7    Kontinen, V.P.8
  • 26
    • 79957835563 scopus 로고    scopus 로고
    • ITRAQ-coupled 2-D LC-MS/MS analysis of membrane protein profile in Escherichia coli incubated with apidaecin IB
    • doi:10.1371/journal.pone.0020442
    • Zhou Y, Chen WN. 2011. iTRAQ-coupled 2-D LC-MS/MS analysis of membrane protein profile in Escherichia coli incubated with apidaecin IB. PLoS One 6:e20442. doi:10.1371/journal.pone.0020442.
    • (2011) PLoS One , vol.6
    • Zhou, Y.1    Chen, W.N.2
  • 27
    • 82455212285 scopus 로고    scopus 로고
    • ITRAQ-coupled 2-D LC-MS/MS analysis of cytoplasmic protein profile in Escherichia coli incubated with apidaecin IB
    • Zhou Y, Chen WN. 2011. iTRAQ-coupled 2-D LC-MS/MS analysis of cytoplasmic protein profile in Escherichia coli incubated with apidaecin IB. J. Proteomics 75:511-516.
    • (2011) J. Proteomics , vol.75 , pp. 511-516
    • Zhou, Y.1    Chen, W.N.2
  • 29
    • 0032482980 scopus 로고    scopus 로고
    • The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface
    • Bals R, Wang X, Zasloff M, Wilson JM. 1998. The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. Proc. Natl. Acad. Sci. U. S. A. 95:9541-9546.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3    Wilson, J.M.4
  • 30
    • 34248356762 scopus 로고    scopus 로고
    • Mechanisms of decreased susceptibility to-defensins by Treponema denticola
    • Brissette CA, Lukehart SA. 2007. Mechanisms of decreased susceptibility to-defensins by Treponema denticola. Infect. Immun. 75:2307-2315.
    • (2007) Infect. Immun. , vol.75 , pp. 2307-2315
    • Brissette, C.A.1    Lukehart, S.A.2
  • 31
    • 84866009218 scopus 로고    scopus 로고
    • Selectivity for and destruction of Salmonella typhimurium via a membrane damage mechanism of a cell-penetrating peptide ppTG20 analogue
    • Li L, Shi Y, Su G, Le G. 2012. Selectivity for and destruction of Salmonella typhimurium via a membrane damage mechanism of a cell-penetrating peptide ppTG20 analogue. Int. J. Antimicrob. Agents 40:337-343.
    • (2012) Int. J. Antimicrob. Agents , vol.40 , pp. 337-343
    • Li, L.1    Shi, Y.2    Su, G.3    Le, G.4
  • 32
    • 77955377305 scopus 로고    scopus 로고
    • Damage of the bacterial cell envelope by antimicrobial peptides gramicidin S and PGLa as revealed by transmission and scanning electron microscopy
    • Hartmann M, Berditsch M, Hawecker J, Ardakani MF, Gerthsen D, Ulrich AS. 2010. Damage of the bacterial cell envelope by antimicrobial peptides gramicidin S and PGLa as revealed by transmission and scanning electron microscopy. Antimicrob. Agents Chemother. 54:3132-3142.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 3132-3142
    • Hartmann, M.1    Berditsch, M.2    Hawecker, J.3    Ardakani, M.F.4    Gerthsen, D.5    Ulrich, A.S.6
  • 33
    • 79955886933 scopus 로고    scopus 로고
    • Metabolite-enabled eradication of bacterial persisters by aminoglycosides
    • Allison KR, Brynildsen MP, Collins JJ. 2011. Metabolite-enabled eradication of bacterial persisters by aminoglycosides. Nature 473:216-220.
    • (2011) Nature , vol.473 , pp. 216-220
    • Allison, K.R.1    Brynildsen, M.P.2    Collins, J.J.3


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