메뉴 건너뛰기




Volumn 4, Issue 1, 2014, Pages 18-41

Mechanisms of antimicrobial peptide resistance in gram-negative bacteria

Author keywords

AMP; Antibiotic resistance; Antimicrobial peptide; CAMP; Gram negative

Indexed keywords

AMINOSUGAR; ANTIMICROBIAL CATIONIC PEPTIDE; BACTERIUM LIPOPOLYSACCHARIDE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; LIPID A; O ANTIGEN; PAGP PROTEIN; PATTERN RECOGNITION RECEPTOR; PHOP REGULATORY PROTEIN; PHOSPHOLIPID; POLYMYXIN B; QUINOLINE DERIVED ANTIINFECTIVE AGENT; REGULATOR PROTEIN; SLYA REGULATORY PROTEIN; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG;

EID: 85019777142     PISSN: None     EISSN: 20796382     Source Type: Journal    
DOI: 10.3390/antibiotics4010018     Document Type: Review
Times cited : (131)

References (129)
  • 1
    • 84870506779 scopus 로고    scopus 로고
    • UNMC Department of Pathology and Microbiology
    • UNMC Department of Pathology and Microbiology. The antimicrobial peptide database. 2014. Available online: http://aps.unmc.edu/AP/main.php (accessed on 2 July 2014).
    • (2014) The Antimicrobial Peptide Database
  • 2
    • 84856864352 scopus 로고    scopus 로고
    • Antimicrobial peptides: Old molecules with new ideas
    • Nakatsuji, T.; Gallo, R.L. Antimicrobial peptides: Old molecules with new ideas. J. Invest. Dermatol. 2012, 132, 887–895
    • (2012) J. Invest. Dermatol , vol.132 , pp. 887-895
    • Nakatsuji, T.1    Gallo, R.L.2
  • 3
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley, W.C. Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem. Biol. 2010, 5, 905–917
    • (2010) ACS Chem. Biol , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 4
    • 25144434489 scopus 로고    scopus 로고
    • Antimicrobial peptide resistance mechanisms of human bacterial pathogens
    • Nizet, V. Antimicrobial peptide resistance mechanisms of human bacterial pathogens. Curr. Issues Mol. Biol. 2006, 8, 11–26
    • (2006) Curr. Issues Mol. Biol , vol.8 , pp. 11-26
    • Nizet, V.1
  • 5
    • 36448983944 scopus 로고    scopus 로고
    • Polymyxin b for the treatment of multidrugresistant pathogens: A critical review
    • Zavascki, A.P.; Goldani, L.Z.; Li, J.; Nation, R.L. Polymyxin b for the treatment of multidrugresistant pathogens: A critical review. J. Antimicrob. Chemother. 2007, 60, 1206–1215
    • (2007) J. Antimicrob. Chemother , vol.60 , pp. 1206-1215
    • Zavascki, A.P.1    Goldani, L.Z.2    Li, J.3    Nation, R.L.4
  • 7
    • 0346655236 scopus 로고    scopus 로고
    • PmrAB, a two-component regulatory system of Pseudomonas aeruginosa that modulates resistance to cationic antimicrobial peptides and addition of aminoarabinose to lipid A
    • Moskowitz, S.M.; Ernst, R.K.; Miller, S.I. PmrAB, a two-component regulatory system of Pseudomonas aeruginosa that modulates resistance to cationic antimicrobial peptides and addition of aminoarabinose to lipid A. J. Bacteriol. 2004, 186, 575–579
    • (2004) J. Bacteriol , vol.186 , pp. 575-579
    • Moskowitz, S.M.1    Ernst, R.K.2    Miller, S.I.3
  • 8
    • 0031909562 scopus 로고    scopus 로고
    • Miller, S.I. PmrA-pmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance
    • Gunn, J.S.; Lim, K.B.; Krueger, J.; Kim, K.; Guo, L.; Hackett, M.; Miller, S.I. PmrA-pmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance. Mol. Microbiol. 1998, 27, 1171–1182
    • (1998) Mol. Microbiol , vol.27 , pp. 1171-1182
    • Gunn, J.S.1    Lim, K.B.2    Krueger, J.3    Kim, K.4    Guo, L.5    Hackett, M.6
  • 9
    • 84455202443 scopus 로고    scopus 로고
    • Extreme antimicrobial peptide and polymyxin B resistance in the genus burkholderia
    • Loutet, S.A.; Valvano, M.A. Extreme antimicrobial peptide and polymyxin B resistance in the genus burkholderia. Front. Microbiol. 2011, 2, e159
    • (2011) Front. Microbiol , vol.2
    • Loutet, S.A.1    Valvano, M.A.2
  • 12
    • 84905400756 scopus 로고    scopus 로고
    • Bordetella pertussis lipid A glucosamine modification confers resistance to cationic antimicrobial peptides and increases resistance to outer membrane perturbation
    • Shah, N.R.; Hancock, R.E.; Fernandez, R.C. Bordetella pertussis lipid A glucosamine modification confers resistance to cationic antimicrobial peptides and increases resistance to outer membrane perturbation. Antimicrob. Agents Chemother. 2014, 58, 4931–4934
    • (2014) Antimicrob. Agents Chemother , vol.58 , pp. 4931-4934
    • Shah, N.R.1    Hancock, R.E.2    Fernandez, R.C.3
  • 13
    • 84861879646 scopus 로고    scopus 로고
    • Amino acid addition to Vibrio cholerae LPS establishes a link between surface remodeling in gram-positive and gram-negative bacteria
    • Hankins, J.V.; Madsen, J.A.; Giles, D.K.; Brodbelt, J.S.; Trent, M.S. Amino acid addition to Vibrio cholerae LPS establishes a link between surface remodeling in gram-positive and gram-negative bacteria. Proc. Natl. Acad. Sci. USA 2012, 109, 8722–8727
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8722-8727
    • Hankins, J.V.1    Madsen, J.A.2    Giles, D.K.3    Brodbelt, J.S.4    Trent, M.S.5
  • 15
    • 62449140880 scopus 로고    scopus 로고
    • Phosphoethanolamine substitution of lipid a and resistance of neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum
    • Lewis, L.A.; Choudhury, B.; Balthazar, J.T.; Martin, L.E.; Ram, S.; Rice, P.A.; Stephens, D.S.; Carlson, R.; Shafer, W.M. Phosphoethanolamine substitution of lipid a and resistance of neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum. Infect. Immun. 2009, 77, 1112–1120
    • (2009) Infect. Immun , vol.77 , pp. 1112-1120
    • Lewis, L.A.1    Choudhury, B.2    Balthazar, J.T.3    Martin, L.E.4    Ram, S.5    Rice, P.A.6    Stephens, D.S.7    Carlson, R.8    Shafer, W.M.9
  • 16
    • 84871861234 scopus 로고    scopus 로고
    • Phosphoethanolamine residues on the lipid a moiety of neisseria gonorrhoeae lipooligosaccharide modulate binding of complement inhibitors and resistance to complement killing
    • Lewis, L.A.; Shafer, W.M.; Dutta Ray, T.; Ram, S.; Rice, P.A. Phosphoethanolamine residues on the lipid a moiety of neisseria gonorrhoeae lipooligosaccharide modulate binding of complement inhibitors and resistance to complement killing. Infect. Immun. 2013, 81, 33–42
    • (2013) Infect. Immun , vol.81 , pp. 33-42
    • Lewis, L.A.1    Shafer, W.M.2    Dutta Ray, T.3    Ram, S.4    Rice, P.A.5
  • 17
    • 84884253490 scopus 로고    scopus 로고
    • Unique structural modifications are present in the lipopolysaccharide from colistin-resistant strains of Acinetobacter baumannii. Antimicrob
    • Pelletier, M.R.; Casella, L.G.; Jones, J.W.; Adams, M.D.; Zurawski, D.V.; Hazlett, K.R.; Doi, Y.; Ernst, R.K. Unique structural modifications are present in the lipopolysaccharide from colistin-resistant strains of Acinetobacter baumannii. Antimicrob. Agents Chemother. 2013, 57, 4831–4840
    • (2013) Agents Chemother , vol.57 , pp. 4831-4840
    • Pelletier, M.R.1    Casella, L.G.2    Jones, J.W.3    Adams, M.D.4    Zurawski, D.V.5    Hazlett, K.R.6    Doi, Y.7    Ernst, R.K.8
  • 18
    • 3042513872 scopus 로고    scopus 로고
    • The pmra-regulated pmrc gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica
    • Lee, H.; Hsu, F.F.; Turk, J.; Groisman, E.A. The pmra-regulated pmrc gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica. J. Bacteriol. 2004, 186, 4124–4133
    • (2004) J. Bacteriol , vol.186 , pp. 4124-4133
    • Lee, H.1    Hsu, F.F.2    Turk, J.3    Groisman, E.A.4
  • 19
    • 34247265920 scopus 로고    scopus 로고
    • Attenuated virulence of a Francisella mutant lacking the lipid a 4'-phosphatase
    • Wang, X.; Ribeiro, A.A.; Guan, Z.; Abraham, S.N.; Raetz, C.R. Attenuated virulence of a Francisella mutant lacking the lipid a 4'-phosphatase. Proc. Natl. Acad. Sci. USA 2007, 104, 4136–4141
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4136-4141
    • Wang, X.1    Ribeiro, A.A.2    Guan, Z.3    Abraham, S.N.4    Raetz, C.R.5
  • 20
    • 0036453946 scopus 로고    scopus 로고
    • Structural analysis of francisella tularensis lipopolysaccharide
    • Vinogradov, E.; Perry, M.B.; Conlan, J.W. Structural analysis of francisella tularensis lipopolysaccharide. Eur. J. Biochem. 2002, 269, 6112–6118
    • (2002) Eur. J. Biochem , vol.269 , pp. 6112-6118
    • Vinogradov, E.1    Perry, M.B.2    Conlan, J.W.3
  • 21
    • 77957057898 scopus 로고    scopus 로고
    • Escherichia coli mutants that synthesize dephosphorylated lipid a molecules
    • Ingram, B.O.; Masoudi, A.; Raetz, C.R. Escherichia coli mutants that synthesize dephosphorylated lipid a molecules. Biochemistry 2010, 49, 8325–8337
    • (2010) Biochemistry , vol.49 , pp. 8325-8337
    • Ingram, B.O.1    Masoudi, A.2    Raetz, C.R.3
  • 22
    • 0028907147 scopus 로고
    • Structural study on the free lipid a isolated from lipopolysaccharide of porphyromonas gingivalis
    • Kumada, H.; Haishima, Y.; Umemoto, T.; Tanamoto, K. Structural study on the free lipid a isolated from lipopolysaccharide of porphyromonas gingivalis. J. Bacteriol. 1995, 177, 2098–2106
    • (1995) J. Bacteriol , vol.177 , pp. 2098-2106
    • Kumada, H.1    Haishima, Y.2    Umemoto, T.3    Tanamoto, K.4
  • 23
    • 0024321629 scopus 로고
    • Structural characterization of the lipid a component of bacteroides fragilis strain nctc 9343 lipopolysaccharide
    • Weintraub, A.; Zähringer, U.; Wollenweber, H.W.; Seydel, U.; Rietschel, E.T. Structural characterization of the lipid a component of bacteroides fragilis strain nctc 9343 lipopolysaccharide. Eur. J. Biochem. 1989, 183, 425–431
    • (1989) Eur. J. Biochem , vol.183 , pp. 425-431
    • Weintraub, A.1    Zähringer, U.2    Wollenweber, H.W.3    Seydel, U.4    Rietschel, E.T.5
  • 24
    • 33744975276 scopus 로고    scopus 로고
    • The lipid A 1-phosphatase of helicobacter pylori is required for resistance to the antimicrobial peptide polymyxin
    • Tran, A.X.; Whittimore, J.D.; Wyrick, P.B.; McGrath, S.C.; Cotter, R.J.; Trent, M.S. The lipid A 1-phosphatase of helicobacter pylori is required for resistance to the antimicrobial peptide polymyxin. J. Bacteriol. 2006, 188, 4531–4541
    • (2006) J. Bacteriol , vol.188 , pp. 4531-4541
    • Tran, A.X.1    Whittimore, J.D.2    Wyrick, P.B.3    McGrath, S.C.4    Cotter, R.J.5    Trent, M.S.6
  • 25
    • 84879418353 scopus 로고    scopus 로고
    • Fortifying the barrier: The impact of lipid A remodelling on bacterial pathogenesis
    • Needham, B.D.; Trent, M.S. Fortifying the barrier: The impact of lipid A remodelling on bacterial pathogenesis. Nat. Rev. Microbiol. 2013, 11, 467–481
    • (2013) Nat. Rev. Microbiol , vol.11 , pp. 467-481
    • Needham, B.D.1    Trent, M.S.2
  • 26
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Guo, L.; Lim, K.B.; Poduje, C.M.; Daniel, M.; Gunn, J.S.; Hackett, M.; Miller, S.I. Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell 1998, 95, 189–198
    • (1998) Cell , vol.95 , pp. 189-198
    • Guo, L.1    Lim, K.B.2    Poduje, C.M.3    Daniel, M.4    Gunn, J.S.5    Hackett, M.6    Miller, S.I.7
  • 28
    • 0024601077 scopus 로고
    • A Salmonella locus that controls resistance to microbicidal proteins from phagocytic cells
    • Fields, P.I.; Groisman, E.A.; Heffron, F. A Salmonella locus that controls resistance to microbicidal proteins from phagocytic cells. Science 1989, 243, 1059–1062
    • (1989) Science , vol.243 , pp. 1059-1062
    • Fields, P.I.1    Groisman, E.A.2    Heffron, F.3
  • 29
    • 0003582512 scopus 로고
    • Two-component regulatory system (PhoP phoQ) controls Salmonella typhimurium virulence
    • Miller, S.I.; Kukral, A.M.; Mekalanos, J.J. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc. Natl. Acad. Sci. USA 1989, 86, 5054–5058
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.3
  • 31
    • 0029809576 scopus 로고    scopus 로고
    • PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance
    • Gunn, J.S.; Miller, S.I. PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance. J. Bacteriol. 1996, 178, 6857–6864
    • (1996) J. Bacteriol , vol.178 , pp. 6857-6864
    • Gunn, J.S.1    Miller, S.I.2
  • 32
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo, L.; Lim, K.B.; Gunn, J.S.; Bainbridge, B.; Darveau, R.P.; Hackett, M.; Miller, S.I. Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 1997, 276, 250–253
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 33
    • 0141484326 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa
    • McPhee, J.B.; Lewenza, S.; Hancock, R.E. Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa. Mol. Microbiol. 2003, 50, 205–217
    • (2003) Mol. Microbiol , vol.50 , pp. 205-217
    • McPhee, J.B.1    Lewenza, S.2    Hancock, R.E.3
  • 34
  • 36
    • 0031911836 scopus 로고    scopus 로고
    • Transposon-derived Brucella abortus rough mutants are attenuated and exhibit reduced intracellular survival
    • Allen, C.A.; Adams, L.G.; Ficht, T.A. Transposon-derived Brucella abortus rough mutants are attenuated and exhibit reduced intracellular survival. Infect. Immun. 1998, 66, 1008–1016
    • (1998) Infect. Immun , vol.66 , pp. 1008-1016
    • Allen, C.A.1    Adams, L.G.2    Ficht, T.A.3
  • 37
    • 33644854257 scopus 로고    scopus 로고
    • A complete lipopolysaccharide inner core oligosaccharide is required for resistance of Burkholderia cenocepacia to antimicrobial peptides and bacterial survival in vivo
    • Loutet, S.A.; Flannagan, R.S.; Kooi, C.; Sokol, P.A.; Valvano, M.A. A complete lipopolysaccharide inner core oligosaccharide is required for resistance of Burkholderia cenocepacia to antimicrobial peptides and bacterial survival in vivo. J. Bacteriol. 2006, 188, 2073–2080
    • (2006) J. Bacteriol , vol.188 , pp. 2073-2080
    • Loutet, S.A.1    Flannagan, R.S.2    Kooi, C.3    Sokol, P.A.4    Valvano, M.A.5
  • 38
    • 0034972212 scopus 로고    scopus 로고
    • Identification of Legionella pneumophila rcp, a pagP-like gene that confers resistance to cationic antimicrobial peptides and promotes intracellular infection
    • Robey, M.; O’Connell, W.; Cianciotto, N.P. Identification of Legionella pneumophila rcp, a pagP-like gene that confers resistance to cationic antimicrobial peptides and promotes intracellular infection. Infect. Immun. 2001, 69, 4276–4286
    • (2001) Infect. Immun , vol.69 , pp. 4276-4286
    • Robey, M.1    O’Connell, W.2    Cianciotto, N.P.3
  • 39
    • 0141446140 scopus 로고    scopus 로고
    • A gonococcal efflux pump system enhances bacterial survival in a female mouse model of genital tract infection
    • Jerse, A.E.; Sharma, N.D.; Simms, A.N.; Crow, E.T.; Snyder, L.A.; Shafer, W.M. A gonococcal efflux pump system enhances bacterial survival in a female mouse model of genital tract infection. Infect. Immun. 2003, 71, 5576–5582
    • (2003) Infect. Immun , vol.71 , pp. 5576-5582
    • Jerse, A.E.1    Sharma, N.D.2    Simms, A.N.3    Crow, E.T.4    Snyder, L.A.5    Shafer, W.M.6
  • 40
    • 0032971774 scopus 로고    scopus 로고
    • ZapA, the IgA-degrading metalloprotease of Proteus mirabilis, is a virulence factor expressed specifically in swarmer cells
    • Walker, K.E.; Moghaddame-Jafari, S.; Lockatell, C.V.; Johnson, D.; Belas, R. ZapA, the IgA-degrading metalloprotease of Proteus mirabilis, is a virulence factor expressed specifically in swarmer cells. Mol. Microbiol. 1999, 32, 825–836
    • (1999) Mol. Microbiol , vol.32 , pp. 825-836
    • Walker, K.E.1    Moghaddame-Jafari, S.2    Lockatell, C.V.3    Johnson, D.4    Belas, R.5
  • 42
    • 0007855988 scopus 로고    scopus 로고
    • Syndecan-1 shedding is enhanced by LasA, a secreted virulence factor of Pseudomonas aeruginosa
    • Park, P.W.; Pier, G.B.; Preston, M.J.; Goldberger, O.; Fitzgerald, M.L.; Bernfield, M. Syndecan-1 shedding is enhanced by LasA, a secreted virulence factor of Pseudomonas aeruginosa. J. Biol. Chem. 2000, 275, 3057–3064
    • (2000) J. Biol. Chem , vol.275 , pp. 3057-3064
    • Park, P.W.1    Pier, G.B.2    Preston, M.J.3    Goldberger, O.4    Fitzgerald, M.L.5    Bernfield, M.6
  • 43
    • 0035799627 scopus 로고    scopus 로고
    • Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence
    • Park, P.W.; Pier, G.B.; Hinkes, M.T.; Bernfield, M. Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence. Nature 2001, 411, 98–102
    • (2001) Nature , vol.411 , pp. 98-102
    • Park, P.W.1    Pier, G.B.2    Hinkes, M.T.3    Bernfield, M.4
  • 46
    • 84869232503 scopus 로고    scopus 로고
    • An altered immune response, but not individual cationic antimicrobial peptides, is associated with the oral attenuation of Ara4N-deficient Salmonella enterica serovar typhimurium in mice
    • Strandberg, K.L.; Richards, S.M.; Tamayo, R.; Reeves, L.T.; Gunn, J.S. An altered immune response, but not individual cationic antimicrobial peptides, is associated with the oral attenuation of Ara4N-deficient Salmonella enterica serovar typhimurium in mice. PLoS ONE 2012, 7, e49588
    • (2012) Plos ONE , vol.7
    • Strandberg, K.L.1    Richards, S.M.2    Tamayo, R.3    Reeves, L.T.4    Gunn, J.S.5
  • 47
    • 0033794504 scopus 로고    scopus 로고
    • Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium
    • Gunn, J.S.; Ryan, S.S.; van Velkinburgh, J.C.; Ernst, R.K.; Miller, S.I. Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium. Infect. Immun. 2000, 68, 6139–6146
    • (2000) Infect. Immun , vol.68 , pp. 6139-6146
    • Gunn, J.S.1    Ryan, S.S.2    Van Velkinburgh, J.C.3    Ernst, R.K.4    Miller, S.I.5
  • 48
    • 4644343541 scopus 로고    scopus 로고
    • Transcriptional control of the antimicrobial peptide resistance ugtL gene by the Salmonella PhoP and SlyA regulatory proteins
    • Shi, Y.; Latifi, T.; Cromie, M.J.; Groisman, E.A. Transcriptional control of the antimicrobial peptide resistance ugtL gene by the Salmonella PhoP and SlyA regulatory proteins. J. Biol. Chem. 2004, 279, 38618–38625
    • (2004) J. Biol. Chem. , vol.279 , pp. 38618-38625
    • Shi, Y.1    Latifi, T.2    Cromie, M.J.3    Groisman, E.A.4
  • 50
    • 0029799771 scopus 로고    scopus 로고
    • PhoP/PhoQ-deleted Salmonella typhi (Ty800) is a safe and immunogenic single-dose typhoid fever vaccine in volunteers
    • Hohmann, E.L.; Oletta, C.A.; Killeen, K.P.; Miller, S.I. PhoP/PhoQ-deleted Salmonella typhi (ty800) is a safe and immunogenic single-dose typhoid fever vaccine in volunteers. J. Infect. Dis. 1996, 173, 1408–1414
    • (1996) J. Infect. Dis , vol.173 , pp. 1408-1414
    • Hohmann, E.L.1    Oletta, C.A.2    Killeen, K.P.3    Miller, S.I.4
  • 51
    • 0029833177 scopus 로고    scopus 로고
    • Outer membrane differences between pathogenic and environmental Yersinia enterocolitica biogroups probed with hydrophobic permeants and polycationic peptides
    • Bengoechea, J.A.; Díaz, R.; Moriyón, I. Outer membrane differences between pathogenic and environmental Yersinia enterocolitica biogroups probed with hydrophobic permeants and polycationic peptides. Infect. Immun. 1996, 64, 4891–4899
    • (1996) Infect. Immun , vol.64 , pp. 4891-4899
    • Bengoechea, J.A.1    Díaz, R.2    Moriyón, I.3
  • 54
    • 84903697585 scopus 로고    scopus 로고
    • Lysylated phospholipids stabilize models of bacterial lipid bilayers and protect against antimicrobial peptides
    • Cox, E.; Michalak, A.; Pagentine, S.; Seaton, P.; Pokorny, A. Lysylated phospholipids stabilize models of bacterial lipid bilayers and protect against antimicrobial peptides. Biochim. Biophys. Acta 2014, 1838, 2198–2204
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 2198-2204
    • Cox, E.1    Michalak, A.2    Pagentine, S.3    Seaton, P.4    Pokorny, A.5
  • 55
    • 35349002810 scopus 로고    scopus 로고
    • The lipid lysyl-phosphatidylglycerol is present in membranes of Rhizobium tropici CIAT899 and confers increased resistance to polymyxin B under acidic growth conditions
    • Sohlenkamp, C.; Galindo-Lagunas, K.A.; Guan, Z.; Vinuesa, P.; Robinson, S.; Thomas-Oates, J.; Raetz, C.R.; Geiger, O. The lipid lysyl-phosphatidylglycerol is present in membranes of Rhizobium tropici CIAT899 and confers increased resistance to polymyxin B under acidic growth conditions. Mol. Plant Microbe Interact. 2007, 20, 1421–1430
    • (2007) Mol. Plant Microbe Interact , vol.20 , pp. 1421-1430
    • Sohlenkamp, C.1    Galindo-Lagunas, K.A.2    Guan, Z.3    Vinuesa, P.4    Robinson, S.5    Thomas-Oates, J.6    Raetz, C.R.7    Geiger, O.8
  • 56
    • 0018386984 scopus 로고
    • Phospholipids of the differentiating bacterium Caulobacter crescentus
    • Jones, D.E.; Smith, J.D. Phospholipids of the differentiating bacterium Caulobacter crescentus. Can. J. Biochem. 1979, 57, 424–428
    • (1979) Can. J. Biochem , vol.57 , pp. 424-428
    • Jones, D.E.1    Smith, J.D.2
  • 57
    • 0036188725 scopus 로고    scopus 로고
    • Peptides with indirect in vivo activity against an intracellular pathogen: Selective lysis of infected macrophages
    • Yokum, T.S.; Hammer, R.P.; McLaughlin, M.L.; Elzer, P.H. Peptides with indirect in vivo activity against an intracellular pathogen: Selective lysis of infected macrophages. J. Pept. Res. 2002, 59, 9–17
    • (2002) J. Pept. Res , vol.59 , pp. 9-17
    • Yokum, T.S.1    Hammer, R.P.2    McLaughlin, M.L.3    Elzer, P.H.4
  • 58
    • 30744475282 scopus 로고    scopus 로고
    • The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides
    • Dorschner, R.A.; Lopez-Garcia, B.; Peschel, A.; Kraus, D.; Morikawa, K.; Nizet, V.; Gallo, R.L. The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides. FASEB J. 2006, 20, 35–42
    • (2006) FASEB J , vol.20 , pp. 35-42
    • Dorschner, R.A.1    Lopez-Garcia, B.2    Peschel, A.3    Kraus, D.4    Morikawa, K.5    Nizet, V.6    Gallo, R.L.7
  • 59
    • 84885019160 scopus 로고    scopus 로고
    • Biosynthesis, and function of bacterial capsular polysaccharides synthesized by abc transporter-dependent pathways
    • Willis, L.M.; Whitfield, C. Structure, biosynthesis, and function of bacterial capsular polysaccharides synthesized by abc transporter-dependent pathways. Carbohydr. Res. 2013, 378, 35–44
    • (2013) Carbohydr. Res , vol.378 , pp. 35-44
    • Willis, L.M.1    Whitfield, C.S.2
  • 61
    • 0036117885 scopus 로고    scopus 로고
    • Molecular analysis of the contribution of the capsular polysaccharide and the lipopolysaccharide o side chain to the virulence of Klebsiella pneumoniae in a murine model of pneumonia
    • Cortés, G.; Borrell, N.; de Astorza, B.; Gómez, C.; Sauleda, J.; Albertí, S. Molecular analysis of the contribution of the capsular polysaccharide and the lipopolysaccharide o side chain to the virulence of Klebsiella pneumoniae in a murine model of pneumonia. Infect. Immun. 2002, 70, 2583–2590
    • (2002) Infect. Immun , vol.70 , pp. 2583-2590
    • Cortés, G.1    Borrell, N.2    De Astorza, B.3    Gómez, C.4    Sauleda, J.5    Albertí, S.6
  • 62
    • 67549112496 scopus 로고    scopus 로고
    • Endotoxin, capsule, and bacterial attachment contribute to Neisseria meningitidis resistance to the human antimicrobial peptide LL-37
    • Jones, A.; Geörg, M.; Maudsdotter, L.; Jonsson, A.B. Endotoxin, capsule, and bacterial attachment contribute to Neisseria meningitidis resistance to the human antimicrobial peptide LL-37. J. Bacteriol. 2009, 191, 3861–3868
    • (2009) J. Bacteriol , vol.191 , pp. 3861-3868
    • Jones, A.1    Geörg, M.2    Maudsdotter, L.3    Jonsson, A.B.4
  • 63
    • 58949097012 scopus 로고    scopus 로고
    • Capsule polysaccharide is a bacterial decoy for antimicrobial peptides
    • Llobet, E.; Tomás, J.M.; Bengoechea, J.A. Capsule polysaccharide is a bacterial decoy for antimicrobial peptides. Microbiology 2008, 154, 3877–3886
    • (2008) Microbiology , vol.154 , pp. 3877-3886
    • Llobet, E.1    Tomás, J.M.2    Bengoechea, J.A.3
  • 64
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: A common cause of persistent infections
    • Costerton, J.W.; Stewart, P.S.; Greenberg, E.P. Bacterial biofilms: A common cause of persistent infections. Science 1999, 284, 1318–1322
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 67
    • 0021992199 scopus 로고
    • Tobramycin resistance of Pseudomonas aeruginosa cells growing as a biofilm on urinary catheter material. Antimicrob
    • Nickel, J.C.; Ruseska, I.; Wright, J.B.; Costerton, J.W. Tobramycin resistance of Pseudomonas aeruginosa cells growing as a biofilm on urinary catheter material. Antimicrob. Agents Chemother. 1985, 27, 619–624
    • (1985) Agents Chemother , vol.27 , pp. 619-624
    • Nickel, J.C.1    Ruseska, I.2    Wright, J.B.3    Costerton, J.W.4
  • 70
    • 4644245658 scopus 로고    scopus 로고
    • Helix induction in antimicrobial peptides by alginate in biofilms
    • Chan, C.; Burrows, L.L.; Deber, C.M. Helix induction in antimicrobial peptides by alginate in biofilms. J. Biol. Chem. 2004, 279, 38749–38754
    • (2004) J. Biol. Chem , vol.279 , pp. 38749-38754
    • Chan, C.1    Burrows, L.L.2    Deber, C.M.3
  • 71
    • 16444374940 scopus 로고    scopus 로고
    • Alginate as an auxiliary bacterial membrane: Binding of membrane-active peptides by polysaccharides
    • Chan, C.; Burrows, L.L.; Deber, C.M. Alginate as an auxiliary bacterial membrane: Binding of membrane-active peptides by polysaccharides. J. Pept. Res. 2005, 65, 343–351
    • (2005) J. Pept. Res , vol.65 , pp. 343-351
    • Chan, C.1    Burrows, L.L.2    Deber, C.M.3
  • 72
    • 70349650567 scopus 로고    scopus 로고
    • Activity of antimicrobial peptides in the presence of polysaccharides produced by pulmonary pathogens
    • Benincasa, M.; Mattiuzzo, M.; Herasimenka, Y.; Cescutti, P.; Rizzo, R.; Gennaro, R. Activity of antimicrobial peptides in the presence of polysaccharides produced by pulmonary pathogens. J. Pept. Sci. 2009, 15, 595–600
    • (2009) J. Pept. Sci , vol.15 , pp. 595-600
    • Benincasa, M.1    Mattiuzzo, M.2    Herasimenka, Y.3    Cescutti, P.4    Rizzo, R.5    Gennaro, R.6
  • 73
    • 57149111485 scopus 로고    scopus 로고
    • Extracellular DNA chelates cations and induces antibiotic resistance in Pseudomonas aeruginosa biofilms
    • Mulcahy, H.; Charron-Mazenod, L.; Lewenza, S. Extracellular DNA chelates cations and induces antibiotic resistance in Pseudomonas aeruginosa biofilms. PLoS Pathog. 2008, 4, e1000213
    • (2008) Plos Pathog , vol.4
    • Mulcahy, H.1    Charron-Mazenod, L.2    Lewenza, S.3
  • 75
    • 49449103767 scopus 로고    scopus 로고
    • Induction by cationic antimicrobial peptides and involvement in intrinsic polymyxin and antimicrobial peptide resistance, biofilm formation, and swarming motility of PsrA in Pseudomonas aeruginosa
    • Gooderham, W.J.; Bains, M.; McPhee, J.B.; Wiegand, I.; Hancock, R.E. Induction by cationic antimicrobial peptides and involvement in intrinsic polymyxin and antimicrobial peptide resistance, biofilm formation, and swarming motility of PsrA in Pseudomonas aeruginosa. J. Bacteriol. 2008, 190, 5624–5634
    • (2008) J. Bacteriol , vol.190 , pp. 5624-5634
    • Gooderham, W.J.1    Bains, M.2    McPhee, J.B.3    Wiegand, I.4    Hancock, R.E.5
  • 76
    • 40549126258 scopus 로고    scopus 로고
    • Tolerance to the antimicrobial peptide colistin in Pseudomonas aeruginosa biofilms is linked to metabolically active cells, and depends on the pmr and mexAB-oprM genes
    • Pamp, S.J.; Gjermansen, M.; Johansen, H.K.; Tolker-Nielsen, T. Tolerance to the antimicrobial peptide colistin in Pseudomonas aeruginosa biofilms is linked to metabolically active cells, and depends on the pmr and mexAB-oprM genes. Mol. Microbiol. 2008, 68, 223–240
    • (2008) Mol. Microbiol , vol.68 , pp. 223-240
    • Pamp, S.J.1    Gjermansen, M.2    Johansen, H.K.3    Tolker-Nielsen, T.4
  • 77
    • 34247568394 scopus 로고    scopus 로고
    • Efflux pumps as antimicrobial resistance mechanisms
    • Poole, K. Efflux pumps as antimicrobial resistance mechanisms. Ann. Med. 2007, 39, 162–176
    • (2007) Ann. Med , vol.39 , pp. 162-176
    • Poole, K.1
  • 78
    • 33747154459 scopus 로고    scopus 로고
    • Multidrug-resistance efflux pumps—Not just for resistance
    • Piddock, L.J. Multidrug-resistance efflux pumps—Not just for resistance. Nat. Rev. Microbiol. 2006, 4, 629–636
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 629-636
    • Piddock, L.J.1
  • 80
    • 33645062695 scopus 로고    scopus 로고
    • Virulence and drug resistance roles of multidrug efflux systems of Salmonella enterica serovar Typhimurium
    • Nishino, K.; Latifi, T.; Groisman, E.A. Virulence and drug resistance roles of multidrug efflux systems of Salmonella enterica serovar Typhimurium. Mol. Microbiol. 2006, 59, 126–141
    • (2006) Mol. Microbiol , vol.59 , pp. 126-141
    • Nishino, K.1    Latifi, T.2    Groisman, E.A.3
  • 81
    • 0029051816 scopus 로고
    • Salmonella enteritidis has a homologue of tolC that is required for virulence in BALB/c mice
    • Stone, B.J.; Miller, V.L. Salmonella enteritidis has a homologue of tolC that is required for virulence in BALB/c mice. Mol. Microbiol. 1995, 17, 701–712
    • (1995) Mol. Microbiol , vol.17 , pp. 701-712
    • Stone, B.J.1    Miller, V.L.2
  • 83
    • 40349106166 scopus 로고    scopus 로고
    • An RND-type efflux system in Borrelia burgdorferi is involved in virulence and resistance to antimicrobial compounds
    • Bunikis, I.; Denker, K.; Ostberg, Y.; Andersen, C.; Benz, R.; Bergström, S. An RND-type efflux system in Borrelia burgdorferi is involved in virulence and resistance to antimicrobial compounds. PLoS Pathog. 2008, 4, e1000009
    • (2008) Plos Pathog , vol.4
    • Bunikis, I.1    Denker, K.2    Ostberg, Y.3    Andersen, C.4    Benz, R.5    Bergström, S.6
  • 85
    • 0034967448 scopus 로고    scopus 로고
    • Vibrio cholerae tolC is required for bile resistance and colonization
    • Bina, J.E.; Mekalanos, J.J. Vibrio cholerae tolC is required for bile resistance and colonization. Infect. Immun. 2001, 69, 4681–4685
    • (2001) Infect. Immun. , vol.69 , pp. 4681-4685
    • Bina, J.E.1    Mekalanos, J.J.2
  • 86
    • 0033925707 scopus 로고    scopus 로고
    • Temperature-regulated efflux pump/potassium antiporter system mediates resistance to cationic antimicrobial peptides in Yersinia
    • Bengoechea, J.A.; Skurnik, M. Temperature-regulated efflux pump/potassium antiporter system mediates resistance to cationic antimicrobial peptides in Yersinia. Mol. Microbiol. 2000, 37, 67–80
    • (2000) Mol. Microbiol , vol.37 , pp. 67-80
    • Bengoechea, J.A.1    Skurnik, M.2
  • 87
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • Shafer, W.M.; Qu, X.; Waring, A.J.; Lehrer, R.I. Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family. Proc. Natl. Acad. Sci. USA 1998, 95, 1829–1833
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 88
    • 52649131941 scopus 로고    scopus 로고
    • Clinically relevant mutations that cause derepression of the Neisseria gonorrhoeae MtrC-MtrD-MtrE efflux pump system confer different levels of antimicrobial resistance and in vivo fitness
    • Warner, D.M.; Shafer, W.M.; Jerse, A.E. Clinically relevant mutations that cause derepression of the Neisseria gonorrhoeae MtrC-MtrD-MtrE efflux pump system confer different levels of antimicrobial resistance and in vivo fitness. Mol. Microbiol. 2008, 70, 462–478
    • (2008) Mol. Microbiol. , vol.70 , pp. 462-478
    • Warner, D.M.1    Shafer, W.M.2    Jerse, A.E.3
  • 90
    • 48849102268 scopus 로고    scopus 로고
    • Vibrio cholerae RND family efflux systems are required for antimicrobial resistance, optimal virulence factor production, and colonization of the infant mouse small intestine
    • Bina, X.R.; Provenzano, D.; Nguyen, N.; Bina, J.E. Vibrio cholerae RND family efflux systems are required for antimicrobial resistance, optimal virulence factor production, and colonization of the infant mouse small intestine. Infect. Immun. 2008, 76, 3595–3605
    • (2008) Infect. Immun. , vol.76 , pp. 3595-3605
    • Bina, X.R.1    Provenzano, D.2    Nguyen, N.3    Bina, J.E.4
  • 91
    • 0842327160 scopus 로고    scopus 로고
    • A K+ uptake protein, TrkA, is required for serum, protamine, and polymyxin B resistance in Vibrio vulnificus. Infect
    • Chen, Y.C.; Chuang, Y.C.; Chang, C.C.; Jeang, C.L.; Chang, M.C. A K+ uptake protein, TrkA, is required for serum, protamine, and polymyxin B resistance in Vibrio vulnificus. Infect. Immun. 2004, 72, 629–636
    • (2004) Immun , vol.72 , pp. 629-636
    • Chen, Y.C.1    Chuang, Y.C.2    Chang, C.C.3    Jeang, C.L.4    Chang, M.C.5
  • 93
    • 0242693288 scopus 로고    scopus 로고
    • Structural investigation of chondroitin/ dermatan sulfate oligosaccharides from human skin fibroblast decorin
    • Zamfir, A.; Seidler, D.G.; Kresse, H.; Peter-Katalinić, J. Structural investigation of chondroitin/ dermatan sulfate oligosaccharides from human skin fibroblast decorin. Glycobiology 2003, 13, 733–742
    • (2003) Glycobiology , vol.13 , pp. 733-742
    • Zamfir, A.1    Seidler, D.G.2    Kresse, H.3    Peter-Katalinić, J.4
  • 94
    • 0035131955 scopus 로고    scopus 로고
    • Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin
    • Schmidtchen, A.; Frick, I.M.; Björck, L. Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin. Mol. Microbiol. 2001, 39, 708–713
    • (2001) Mol. Microbiol , vol.39 , pp. 708-713
    • Schmidtchen, A.1    Frick, I.M.2    Björck, L.3
  • 96
    • 33746606073 scopus 로고    scopus 로고
    • Outer membrane vesicle production by Escherichia coli is independent of membrane instability
    • McBroom, A.J.; Johnson, A.P.; Vemulapalli, S.; Kuehn, M.J. Outer membrane vesicle production by Escherichia coli is independent of membrane instability. J. Bacteriol. 2006, 188, 5385–5392
    • (2006) J. Bacteriol , vol.188 , pp. 5385-5392
    • McBroom, A.J.1    Johnson, A.P.2    Vemulapalli, S.3    Kuehn, M.J.4
  • 97
    • 27744480818 scopus 로고    scopus 로고
    • Bacterial outer membrane vesicles and the host-pathogen interaction
    • Kuehn, M.J.; Kesty, N.C. Bacterial outer membrane vesicles and the host-pathogen interaction. Genes Dev. 2005, 19, 2645–2655
    • (2005) Genes Dev , vol.19 , pp. 2645-2655
    • Kuehn, M.J.1    Kesty, N.C.2
  • 98
    • 33846037385 scopus 로고    scopus 로고
    • Release of outer membrane vesicles by gram-negative bacteria is a novel envelope stress response
    • McBroom, A.J.; Kuehn, M.J. Release of outer membrane vesicles by gram-negative bacteria is a novel envelope stress response. Mol. Microbiol. 2007, 63, 545–558
    • (2007) Mol. Microbiol , vol.63 , pp. 545-558
    • McBroom, A.J.1    Kuehn, M.J.2
  • 99
  • 100
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • Peschel, A.; Sahl, H.G. The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 2006, 4, 529–536
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 101
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • Schmidtchen, A.; Frick, I.M.; Andersson, E.; Tapper, H.; Björck, L. Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37. Mol. Microbiol. 2002, 46, 157–168
    • (2002) Mol. Microbiol , vol.46 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.M.2    Andersson, E.3    Tapper, H.4    Björck, L.5
  • 102
    • 0033919460 scopus 로고    scopus 로고
    • PhoP-regulated outer membrane protease of Salmonella enterica serovar Typhimurium promotes resistance to alpha-helical antimicrobial peptides
    • Guina, T.; Yi, E.C.; Wang, H.; Hackett, M.; Miller, S.I. A PhoP-regulated outer membrane protease of Salmonella enterica serovar Typhimurium promotes resistance to alpha-helical antimicrobial peptides. J. Bacteriol. 2000, 182, 4077–4086
    • (2000) J. Bacteriol , vol.182 , pp. 4077-4086
    • Guina, T.1    Yi, E.C.2    Wang, H.3    Hackett, M.4    Miller, S.5
  • 104
    • 0024511945 scopus 로고
    • Determination of the disulfide array in the human defensin HNP-2. A covalently cyclized peptide
    • Selsted, M.E.; Harwig, S.S. Determination of the disulfide array in the human defensin HNP-2. A covalently cyclized peptide. J. Biol. Chem. 1989, 264, 4003–4007
    • (1989) J. Biol. Chem , vol.264 , pp. 4003-4007
    • Selsted, M.E.1    Harwig, S.S.2
  • 106
    • 10344240423 scopus 로고    scopus 로고
    • Structure-activity relationships in defensin dimers: A novel link between beta-defensin tertiary structure and antimicrobial activity
    • Campopiano, D.J.; Clarke, D.J.; Polfer, N.C.; Barran, P.E.; Langley, R.J.; Govan, J.R.; Maxwell, A.; Dorin, J.R. Structure-activity relationships in defensin dimers: A novel link between beta-defensin tertiary structure and antimicrobial activity. J. Biol. Chem. 2004, 279, 48671–48679
    • (2004) J. Biol. Chem , vol.279 , pp. 48671-48679
    • Campopiano, D.J.1    Clarke, D.J.2    Polfer, N.C.3    Barran, P.E.4    Langley, R.J.5    Govan, J.R.6    Maxwell, A.7    Dorin, J.R.8
  • 107
    • 0031831037 scopus 로고    scopus 로고
    • Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli
    • Stumpe, S.; Schmid, R.; Stephens, D.L.; Georgiou, G.; Bakker, E.P. Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli. J. Bacteriol. 1998, 180, 4002–4006
    • (1998) J. Bacteriol , vol.180 , pp. 4002-4006
    • Stumpe, S.1    Schmid, R.2    Stephens, D.L.3    Georgiou, G.4    Bakker, E.P.5
  • 108
    • 33745237318 scopus 로고    scopus 로고
    • The probable structure of the protamine-DNA complex
    • Biegeleisen, K. The probable structure of the protamine-DNA complex. J. Theor. Biol. 2006, 241, 533–540
    • (2006) J. Theor. Biol , vol.241 , pp. 533-540
    • Biegeleisen, K.1
  • 109
    • 3142737933 scopus 로고    scopus 로고
    • The omptin family of enterobacterial surface proteases/adhesins: From housekeeping in Escherichia coli to systemic spread of Yersinia pestis
    • Kukkonen, M.; Korhonen, T.K. The omptin family of enterobacterial surface proteases/adhesins: From housekeeping in Escherichia coli to systemic spread of Yersinia pestis. Int. J. Med. Microbiol. 2004, 294, 7–14
    • (2004) Int. J. Med. Microbiol , vol.294 , pp. 7-14
    • Kukkonen, M.1    Korhonen, T.K.2
  • 110
    • 69949173618 scopus 로고    scopus 로고
    • Burkholderia cenocepacia zinc metalloproteases influence resistance to antimicrobial peptides
    • Kooi, C.; Sokol, P.A. Burkholderia cenocepacia zinc metalloproteases influence resistance to antimicrobial peptides. Microbiology 2009, 155, 2818–2825
    • (2009) Microbiology , vol.155 , pp. 2818-2825
    • Kooi, C.1    Sokol, P.A.2
  • 111
    • 0042008056 scopus 로고    scopus 로고
    • An extracellular zinc metalloprotease gene of Burkholderia cepacia
    • Corbett, C.R.; Burtnick, M.N.; Kooi, C.; Woods, D.E.; Sokol, P.A. An extracellular zinc metalloprotease gene of Burkholderia cepacia. Microbiology 2003, 149, 2263–2271
    • (2003) Microbiology , vol.149 , pp. 2263-2271
    • Corbett, C.R.1    Burtnick, M.N.2    Kooi, C.3    Woods, D.E.4    Sokol, P.A.5
  • 112
    • 33745624324 scopus 로고    scopus 로고
    • Burkholderia cenocepacia ZmpB is a broad-specificity zinc metalloprotease involved in virulence
    • Kooi, C.; Subsin, B.; Chen, R.; Pohorelic, B.; Sokol, P.A. Burkholderia cenocepacia ZmpB is a broad-specificity zinc metalloprotease involved in virulence. Infect. Immun. 2006, 74, 4083–4093
    • (2006) Infect. Immun , vol.74 , pp. 4083-4093
    • Kooi, C.1    Subsin, B.2    Chen, R.3    Pohorelic, B.4    Sokol, P.A.5
  • 113
    • 4544254599 scopus 로고    scopus 로고
    • Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides
    • Belas, R.; Manos, J.; Suvanasuthi, R. Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides. Infect. Immun. 2004, 72, 5159–5167
    • (2004) Infect. Immun , vol.72 , pp. 5159-5167
    • Belas, R.1    Manos, J.2    Suvanasuthi, R.3
  • 115
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415, 389–395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 116
    • 76149111441 scopus 로고    scopus 로고
    • Porphyromonas gingivalis resistance to polymyxin B is determined by the lipid A 4'-phosphatase, PGN_0524
    • Coats, S.R.; To, T.T.; Jain, S.; Braham, P.H.; Darveau, R.P. Porphyromonas gingivalis resistance to polymyxin B is determined by the lipid A 4'-phosphatase, PGN_0524. Int. J. Oral Sci. 2009, 1, 126–135
    • (2009) Int. J. Oral Sci , vol.1 , pp. 126-135
    • Coats, S.R.1    To, T.T.2    Jain, S.3    Braham, P.H.4    Darveau, R.P.5
  • 118
    • 23744436588 scopus 로고    scopus 로고
    • The lipid A palmitoyltransferase PagP: Molecular mechanisms and role in bacterial pathogenesis
    • Bishop, R.E. The lipid A palmitoyltransferase PagP: Molecular mechanisms and role in bacterial pathogenesis. Mol. Microbiol. 2005, 57, 900–912
    • (2005) Mol. Microbiol , vol.57 , pp. 900-912
    • Bishop, R.E.1
  • 119
    • 84880690688 scopus 로고    scopus 로고
    • Recognition of lipid A variants by the TLR4-MD-2 receptor complex
    • Maeshima, N.; Fernandez, R.C. Recognition of lipid A variants by the TLR4-MD-2 receptor complex. Front. Cell. Infect. Microbiol. 2013, 3, e3
    • (2013) Front. Cell. Infect. Microbiol , vol.3
    • Maeshima, N.1    Fernandez, R.C.2
  • 120
    • 0033584935 scopus 로고    scopus 로고
    • Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa
    • Ernst, R.K.; Yi, E.C.; Guo, L.; Lim, K.B.; Burns, J.L.; Hackett, M.; Miller, S.I. Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa. Science 1999, 286, 1561–1565
    • (1999) Science , vol.286 , pp. 1561-1565
    • Ernst, R.K.1    Yi, E.C.2    Guo, L.3    Lim, K.B.4    Burns, J.L.5    Hackett, M.6    Miller, S.I.7
  • 121
    • 84877782955 scopus 로고    scopus 로고
    • A CRISPR/Cas system mediates bacterial innate immune evasion and virulence
    • Sampson, T.R.; Saroj, S.D.; Llewellyn, A.C.; Tzeng, Y.L.; Weiss, D.S. A CRISPR/Cas system mediates bacterial innate immune evasion and virulence. Nature 2013, 497, 254–257
    • (2013) Nature , vol.497 , pp. 254-257
    • Sampson, T.R.1    Saroj, S.D.2    Llewellyn, A.C.3    Tzeng, Y.L.4    Weiss, D.S.5
  • 124
    • 0035126317 scopus 로고    scopus 로고
    • Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
    • Islam, D.; Bandholtz, L.; Nilsson, J.; Wigzell, H.; Christensson, B.; Agerberth, B.; Gudmundsson, G. Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator. Nat. Med. 2001, 7, 180–185
    • (2001) Nat. Med , vol.7 , pp. 180-185
    • Islam, D.1    Bandholtz, L.2    Nilsson, J.3    Wigzell, H.4    Christensson, B.5    Agerberth, B.6    Gudmundsson, G.7
  • 125
    • 43549114552 scopus 로고    scopus 로고
    • Virulent Shigella flexneri subverts the host innate immune response through manipulation of antimicrobial peptide gene expression
    • Sperandio, B.; Regnault, B.; Guo, J.; Zhang, Z.; Stanley, S.L.; Sansonetti, P.J.; Pédron, T. Virulent Shigella flexneri subverts the host innate immune response through manipulation of antimicrobial peptide gene expression. J. Exp. Med. 2008, 205, 1121–1132
    • (2008) J. Exp. Med , vol.205 , pp. 1121-1132
    • Sperandio, B.1    Regnault, B.2    Guo, J.3    Zhang, Z.4    Stanley, S.L.5    Sansonetti, P.J.6    Pédron, T.7
  • 126
    • 0036851306 scopus 로고    scopus 로고
    • Bacterial strategies for overcoming host innate and adaptive immune responses
    • Hornef, M.W.; Wick, M.J.; Rhen, M.; Normark, S. Bacterial strategies for overcoming host innate and adaptive immune responses. Nat. Immunol. 2002, 3, 1033–1040
    • (2002) Nat. Immunol , vol.3 , pp. 1033-1040
    • Hornef, M.W.1    Wick, M.J.2    Rhen, M.3    Normark, S.4
  • 128
    • 84906097341 scopus 로고    scopus 로고
    • Colistin heteroresistance in Enterobacter cloacae is associated with cross-resistance to the host antimicrobial lysozyme
    • Napier, B.A.; Band, V.; Burd, E.M.; Weiss, D.S. Colistin heteroresistance in Enterobacter cloacae is associated with cross-resistance to the host antimicrobial lysozyme. Antimicrob. Agents Chemother. 2014, 58, 5594–5597
    • (2014) Antimicrob. Agents Chemother , vol.58 , pp. 5594-5597
    • Napier, B.A.1    Band, V.2    Burd, E.M.3    Weiss, D.S.4
  • 129
    • 23444437935 scopus 로고    scopus 로고
    • A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs
    • Gordon, Y.J.; Romanowski, E.G.; McDermott, A.M. A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs. Curr. Eye Res. 2005, 30, 505–515.
    • (2005) Curr. Eye Res , vol.30 , pp. 505-515
    • Gordon, Y.J.1    Romanowski, E.G.2    McDermott, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.