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Volumn 1848, Issue 11, 2015, Pages 3089-3100

Defensive remodeling: How bacterial surface properties and biofilm formation promote resistance to antimicrobial peptides

Author keywords

Antimicrobial peptides; Biochemical properties; Biofilm; Biophysical properties; Cross resistance; Resistance; Surface

Indexed keywords

BACTERIAL POLYSACCHARIDE; BACTERIAL PROTEIN; FATTY ACID; GLYCINE; LIPID A; PHOSPHATIDYLGLYCEROL; PHOSPHOETHANOLAMINE; POLYPEPTIDE ANTIBIOTIC AGENT; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE;

EID: 84943816958     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2015.05.022     Document Type: Article
Times cited : (71)

References (200)
  • 1
    • 39449103059 scopus 로고    scopus 로고
    • The epidemic of antibiotic-resistant infections: a call to action for the medical community from the Infectious Diseases Society of America
    • B. Spellberg, R. Guidos, D. Gilbert, J. Bradley, H.W. Boucher, W.M. Scheld, J.G. Bartlett, and J. Edwards Jr. The epidemic of antibiotic-resistant infections: a call to action for the medical community from the Infectious Diseases Society of America Clin. Infect. Dis. 46 2008 155 164
    • (2008) Clin. Infect. Dis. , vol.46 , pp. 155-164
    • Spellberg, B.1    Guidos, R.2    Gilbert, D.3    Bradley, J.4    Boucher, H.W.5    Scheld, W.M.6    Bartlett, J.G.7    Edwards, J.8
  • 2
    • 84864055383 scopus 로고    scopus 로고
    • Antimicrobial resistance: a complex issue
    • J.F. Acar, and G. Moulin Antimicrobial resistance: a complex issue Rev. Sci. Tech. 31 2012 23 31
    • (2012) Rev. Sci. Tech. , vol.31 , pp. 23-31
    • Acar, J.F.1    Moulin, G.2
  • 3
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • H.G. Boman Peptide antibiotics and their role in innate immunity Annu. Rev. Immunol. 13 1995 61 92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 4
    • 79960938721 scopus 로고    scopus 로고
    • Bacterial resistance mechanisms against host defense peptides
    • T. Koprivnjak, and A. Peschel Bacterial resistance mechanisms against host defense peptides Cell. Mol. Life Sci. 68 2011 2243 2254
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2243-2254
    • Koprivnjak, T.1    Peschel, A.2
  • 5
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 6
    • 33845373255 scopus 로고    scopus 로고
    • Host defense peptides and lipopeptides: modes of action and potential candidates for the treatment of bacterial and fungal infections
    • Y. Shai, A. Makovitzky, and D. Avrahami Host defense peptides and lipopeptides: modes of action and potential candidates for the treatment of bacterial and fungal infections Curr. Protein Pept. Sci. 7 2006 479 486
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 479-486
    • Shai, Y.1    Mky, A.2    Avrahami, D.3
  • 7
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • L.T. Nguyen, E.F. Haney, and H.J. Vogel The expanding scope of antimicrobial peptide structures and their modes of action Trends Biotechnol. 29 2011 464 472
    • (2011) Trends Biotechnol. , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 9
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • G.H. Gudmundsson, B. Agerberth, J. Odeberg, T. Bergman, B. Olsson, and R. Salcedo The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes Eur. J. Biochem. 238 1996 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
  • 10
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta 1462 1999 55 70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 11
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • U.H. Durr, U.S. Sudheendra, and A. Ramamoorthy LL-37, the only human member of the cathelicidin family of antimicrobial peptides Biochim. Biophys. Acta 1758 2006 1408 1425
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1408-1425
    • Durr, U.H.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 13
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: obstacles and realistic outlook
    • A.K. Marr, W.J. Gooderham, and R.E. Hancock Antibacterial peptides for therapeutic use: obstacles and realistic outlook Curr. Opin. Pharmacol. 6 2006 468 472
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.3
  • 14
    • 46749108538 scopus 로고    scopus 로고
    • Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides
    • Z. Jiang, A.I. Vasil, J.D. Hale, R.E. Hancock, M.L. Vasil, and R.S. Hodges Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides Biopolymers 90 2008 369 383
    • (2008) Biopolymers , vol.90 , pp. 369-383
    • Jiang, Z.1    Vasil, A.I.2    Hale, J.D.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 15
    • 84856870696 scopus 로고    scopus 로고
    • Effect of PhoP-PhoQ activation by broad repertoire of antimicrobial peptides on bacterial resistance
    • T. Shprung, A. Peleg, Y. Rosenfeld, P. Trieu-Cuot, and Y. Shai Effect of PhoP-PhoQ activation by broad repertoire of antimicrobial peptides on bacterial resistance J. Biol. Chem. 287 2012 4544 4551
    • (2012) J. Biol. Chem. , vol.287 , pp. 4544-4551
    • Shprung, T.1    Peleg, A.2    Rosenfeld, Y.3    Trieu-Cuot, P.4    Shai, Y.5
  • 16
    • 84863230302 scopus 로고    scopus 로고
    • Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions
    • L.M. Yin, M.A. Edwards, J. Li, C.M. Yip, and C.M. Deber Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions J. Biol. Chem. 287 2012 7738 7745
    • (2012) J. Biol. Chem. , vol.287 , pp. 7738-7745
    • Yin, L.M.1    Edwards, M.A.2    Li, J.3    Yip, C.M.4    Deber, C.M.5
  • 18
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • J.P. Powers, and R.E. Hancock The relationship between peptide structure and antibacterial activity Peptides 24 2003 1681 1691
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 19
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • R.E. Hancock, and G. Diamond The role of cationic antimicrobial peptides in innate host defences Trends Microbiol. 8 2000 402 410
    • (2000) Trends Microbiol. , vol.8 , pp. 402-410
    • Hancock, R.E.1    Diamond, G.2
  • 20
    • 0026754487 scopus 로고
    • Model ion channels: gramicidin and alamethicin
    • G.A. Woolley, and B.A. Wallace Model ion channels: gramicidin and alamethicin J. Membr. Biol. 129 1992 109 136
    • (1992) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 21
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Y. Shai Mode of action of membrane active antimicrobial peptides Biopolymers 66 2002 236 248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 22
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self defense? Magainins and tachyplesins as archetypes
    • K. Matsuzaki Why and how are peptide-lipid interactions utilized for self defense? Magainins and tachyplesins as archetypes Biochim. Biophys. Acta 1462 1999 1 10
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 23
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • L. Yang, T.A. Harroun, T.M. Weiss, L. Ding, and H.W. Huang Barrel-stave model or toroidal model? A case study on melittin pores Biophys. J. 81 2001 1475 1485
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 24
    • 0027963281 scopus 로고
    • The role of the PhoP/PhoQ regulon in Salmonella virulence
    • E. Garcia Vescovi, F.C. Soncini, and E.A. Groisman The role of the PhoP/PhoQ regulon in Salmonella virulence Res. Microbiol. 145 1994 473 480
    • (1994) Res. Microbiol. , vol.145 , pp. 473-480
    • Garcia Vescovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 25
    • 0031909562 scopus 로고    scopus 로고
    • PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance
    • J.S. Gunn, K.B. Lim, J. Krueger, K. Kim, L. Guo, M. Hackett, and S.I. Miller PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance Mol. Microbiol. 27 1998 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    Miller, S.I.7
  • 26
    • 25144434489 scopus 로고    scopus 로고
    • Antimicrobial peptide resistance mechanisms of human bacterial pathogens
    • V. Nizet Antimicrobial peptide resistance mechanisms of human bacterial pathogens Curr. Issues Mol. Biol. 8 2006 11 26
    • (2006) Curr. Issues Mol. Biol. , vol.8 , pp. 11-26
    • Nizet, V.1
  • 28
    • 85019669882 scopus 로고    scopus 로고
    • Antimicrobial peptide resistance mechanisms of gram-positive bacteria
    • K.L. Nawrocki, E.K. Crispell, and S.M. McBride Antimicrobial peptide resistance mechanisms of gram-positive bacteria Antibiotics (Basel) 3 2014 461 492
    • (2014) Antibiotics (Basel) , vol.3 , pp. 461-492
    • Nawrocki, K.L.1    Crispell, E.K.2    McBride, S.M.3
  • 29
    • 84908137882 scopus 로고    scopus 로고
    • Antimicrobial peptide resistance of Vibrio cholerae results from an LPS modification pathway related to nonribosomal peptide synthetases
    • J.C. Henderson, C.D. Fage, J.R. Cannon, J.S. Brodbelt, A.T. Keatinge-Clay, and M.S. Trent Antimicrobial peptide resistance of Vibrio cholerae results from an LPS modification pathway related to nonribosomal peptide synthetases ACS Chem. Biol. 9 2014 2382 2392
    • (2014) ACS Chem. Biol. , vol.9 , pp. 2382-2392
    • Henderson, J.C.1    Fage, C.D.2    Cannon, J.R.3    Brodbelt, J.S.4    Keatinge-Clay, A.T.5    Trent, M.S.6
  • 30
    • 33744975276 scopus 로고    scopus 로고
    • The lipid A 1-phosphatase of Helicobacter pylori is required for resistance to the antimicrobial peptide polymyxin
    • A.X. Tran, J.D. Whittimore, P.B. Wyrick, S.C. McGrath, R.J. Cotter, and M.S. Trent The lipid A 1-phosphatase of Helicobacter pylori is required for resistance to the antimicrobial peptide polymyxin J. Bacteriol. 188 2006 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
  • 32
    • 0141484326 scopus 로고    scopus 로고
    • Ca+tionic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa
    • J.B. McPhee, S. Lewenza, and R.E. Hancock 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. 50 2003 205 217
    • (2003) Mol. Microbiol. , vol.50 , pp. 205-217
    • McPhee, J.B.1    Lewenza, S.2    Hancock, R.E.3
  • 33
    • 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
    • S.M. Moskowitz, R.K. Ernst, and S.I. Miller 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. 186 2004 575 579
    • (2004) J. Bacteriol. , vol.186 , pp. 575-579
    • Moskowitz, S.M.1    Ernst, R.K.2    Miller, S.I.3
  • 34
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • A. Peschel How do bacteria resist human antimicrobial peptides? Trends Microbiol. 10 2002 179 186
    • (2002) Trends Microbiol. , vol.10 , pp. 179-186
    • Peschel, A.1
  • 35
    • 84866951984 scopus 로고    scopus 로고
    • D-alanylation of lipoteichoic acids confers resistance to cationic peptides in group B streptococcus by increasing the cell wall density
    • R. Saar-Dover, A. Bitler, R. Nezer, L. Shmuel-Galia, A. Firon, E. Shimoni, P. Trieu-Cuot, and Y. Shai D-alanylation of lipoteichoic acids confers resistance to cationic peptides in group B streptococcus by increasing the cell wall density PLoS Pathog. 8 2012 e1002891
    • (2012) PLoS Pathog. , vol.8
    • Saar-Dover, R.1    Bitler, A.2    Nezer, R.3    Shmuel-Galia, L.4    Firon, A.5    Shimoni, E.6    Trieu-Cuot, P.7    Shai, Y.8
  • 37
    • 43549114552 scopus 로고    scopus 로고
    • Virulent Shigella flexneri subverts the host innate immune response through manipulation of antimicrobial peptide gene expression
    • B. Sperandio, B. Regnault, J. Guo, Z. Zhang, S.L. Stanley Jr., P.J. Sansonetti, and T. Pedron Virulent Shigella flexneri subverts the host innate immune response through manipulation of antimicrobial peptide gene expression J. Exp. Med. 205 2008 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    Pedron, T.7
  • 38
    • 57149111485 scopus 로고    scopus 로고
    • Extracellular DNA chelates cations and induces antibiotic resistance in Pseudomonas aeruginosa biofilms
    • H. Mulcahy, L. Charron-Mazenod, and S. Lewenza Extracellular DNA chelates cations and induces antibiotic resistance in Pseudomonas aeruginosa biofilms PLoS Pathog. 4 2008 e1000213
    • (2008) PLoS Pathog. , vol.4
    • Mulcahy, H.1    Charron-Mazenod, L.2    Lewenza, S.3
  • 39
    • 4644245658 scopus 로고    scopus 로고
    • Helix induction in antimicrobial peptides by alginate in biofilms
    • C. Chan, L.L. Burrows, and C.M. Deber Helix induction in antimicrobial peptides by alginate in biofilms J. Biol. Chem. 279 2004 38749 38754
    • (2004) J. Biol. Chem. , vol.279 , pp. 38749-38754
    • Chan, C.1    Burrows, L.L.2    Deber, C.M.3
  • 41
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • A. Schmidtchen, I.M. Frick, E. Andersson, H. Tapper, and L. Bjorck Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37 Mol. Microbiol. 46 2002 157 168
    • (2002) Mol. Microbiol. , vol.46 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.M.2    Andersson, E.3    Tapper, H.4    Bjorck, L.5
  • 42
    • 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
    • D.M. Warner, W.M. Shafer, and A.E. Jerse 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. 70 2008 462 478
    • (2008) Mol. Microbiol. , vol.70 , pp. 462-478
    • Warner, D.M.1    Shafer, W.M.2    Jerse, A.E.3
  • 43
    • 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
    • W.M. Shafer, X. Qu, A.J. Waring, and R.I. Lehrer 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. U. S. A. 95 1998 1829 1833
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 44
    • 44949183563 scopus 로고    scopus 로고
    • A group B streptococcal pilus protein promotes phagocyte resistance and systemic virulence
    • H.C. Maisey, D. Quach, M.E. Hensler, G.Y. Liu, R.L. Gallo, V. Nizet, and K.S. Doran A group B streptococcal pilus protein promotes phagocyte resistance and systemic virulence FASEB J. 22 2008 1715 1724
    • (2008) FASEB J. , vol.22 , pp. 1715-1724
    • Maisey, H.C.1    Quach, D.2    Hensler, M.E.3    Liu, G.Y.4    Gallo, R.L.5    Nizet, V.6    Doran, K.S.7
  • 46
    • 0037930850 scopus 로고    scopus 로고
    • SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides
    • I.M. Frick, P. Akesson, M. Rasmussen, A. Schmidtchen, and L. Bjorck SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides J. Biol. Chem. 278 2003 16561 16566
    • (2003) J. Biol. Chem. , vol.278 , pp. 16561-16566
    • Frick, I.M.1    Akesson, P.2    Rasmussen, M.3    Schmidtchen, A.4    Bjorck, L.5
  • 47
    • 82355160892 scopus 로고    scopus 로고
    • Contribution of bacterial outer membrane vesicles to innate bacterial defense
    • A.J. Manning, and M.J. Kuehn Contribution of bacterial outer membrane vesicles to innate bacterial defense BMC Microbiol. 11 2011 258
    • (2011) BMC Microbiol. , vol.11 , pp. 258
    • Manning, A.J.1    Kuehn, M.J.2
  • 49
    • 44649203366 scopus 로고    scopus 로고
    • The Salmonella PmrAB regulon: lipopolysaccharide modifications, antimicrobial peptide resistance and more
    • J.S. Gunn The Salmonella PmrAB regulon: lipopolysaccharide modifications, antimicrobial peptide resistance and more Trends Microbiol. 16 2008 284 290
    • (2008) Trends Microbiol. , vol.16 , pp. 284-290
    • Gunn, J.S.1
  • 50
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • M.R. Yeaman, and N.Y. Yount Mechanisms of antimicrobial peptide action and resistance Pharmacol. Rev. 55 2003 27 55
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 51
    • 84987804431 scopus 로고    scopus 로고
    • Mechanisms of polymyxin resistance: acquired and intrinsic resistance in bacteria
    • A.O. Olaitan, S. Morand, and J.M. Rolain Mechanisms of polymyxin resistance: acquired and intrinsic resistance in bacteria Front. Microbiol. 5 2014 643
    • (2014) Front. Microbiol. , vol.5 , pp. 643
    • Olaitan, A.O.1    Morand, S.2    Rolain, J.M.3
  • 52
    • 67549112496 scopus 로고    scopus 로고
    • Endotoxin, capsule, and bacterial attachment contribute to Neisseria meningitidis resistance to the human antimicrobial peptide LL-37
    • A. Jones, M. Georg, L. Maudsdotter, and A.B. Jonsson Endotoxin, capsule, and bacterial attachment contribute to Neisseria meningitidis resistance to the human antimicrobial peptide LL-37 J. Bacteriol. 191 2009 3861 3868
    • (2009) J. Bacteriol. , vol.191 , pp. 3861-3868
    • Jones, A.1    Georg, M.2    Maudsdotter, L.3    Jonsson, A.B.4
  • 53
    • 84899983124 scopus 로고    scopus 로고
    • Bacterial self-defence: how Escherichia coli evades serum killing
    • H. Miajlovic, and S.G. Smith Bacterial self-defence: how Escherichia coli evades serum killing FEMS Microbiol. Lett. 354 2014 1 9
    • (2014) FEMS Microbiol. Lett. , vol.354 , pp. 1-9
    • Miajlovic, H.1    Smith, S.G.2
  • 54
    • 58949097012 scopus 로고    scopus 로고
    • Capsule polysaccharide is a bacterial decoy for antimicrobial peptides
    • E. Llobet, J.M. Tomas, and J.A. Bengoechea Capsule polysaccharide is a bacterial decoy for antimicrobial peptides Microbiology 154 2008 3877 3886
    • (2008) Microbiology , vol.154 , pp. 3877-3886
    • Llobet, E.1    Tomas, J.M.2    Bengoechea, J.A.3
  • 56
    • 84924188257 scopus 로고    scopus 로고
    • The lipid-modifying multiple peptide resistance factor is an oligomer consisting of distinct interacting synthase and flippase subunits
    • C.M. Ernst, S. Kuhn, C.J. Slavetinsky, B. Krismer, S. Heilbronner, C. Gekeler, D. Kraus, S. Wagner, and A. Peschel The lipid-modifying multiple peptide resistance factor is an oligomer consisting of distinct interacting synthase and flippase subunits MBio 6 2015
    • (2015) MBio , vol.6
    • Ernst, C.M.1    Kuhn, S.2    Slavetinsky, C.J.3    Krismer, B.4    Heilbronner, S.5    Gekeler, C.6    Kraus, D.7    Wagner, S.8    Peschel, A.9
  • 57
    • 73549084991 scopus 로고    scopus 로고
    • The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion
    • C.M. Ernst, P. Staubitz, N.N. Mishra, S.J. Yang, G. Hornig, H. Kalbacher, A.S. Bayer, D. Kraus, and A. Peschel The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion PLoS Pathog. 5 2009 e1000660
    • (2009) PLoS Pathog. , vol.5
    • Ernst, C.M.1    Staubitz, P.2    Mishra, N.N.3    Yang, S.J.4    Hornig, G.5    Kalbacher, H.6    Bayer, A.S.7    Kraus, D.8    Peschel, A.9
  • 59
    • 84885944661 scopus 로고    scopus 로고
    • Causal role of single nucleotide polymorphisms within the mprF gene of Staphylococcus aureus in daptomycin resistance
    • S.J. Yang, N.N. Mishra, A. Rubio, and A.S. Bayer Causal role of single nucleotide polymorphisms within the mprF gene of Staphylococcus aureus in daptomycin resistance Antimicrob. Agents Chemother. 57 2013 5658 5664
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 5658-5664
    • Yang, S.J.1    Mishra, N.N.2    Rubio, A.3    Bayer, A.S.4
  • 60
    • 79953886272 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial peptide resistance by MprF-mediated aminoacylation and flipping of phospholipids
    • C.M. Ernst, and A. Peschel Broad-spectrum antimicrobial peptide resistance by MprF-mediated aminoacylation and flipping of phospholipids Mol. Microbiol. 80 2011 290 299
    • (2011) Mol. Microbiol. , vol.80 , pp. 290-299
    • Ernst, C.M.1    Peschel, A.2
  • 61
    • 84912121163 scopus 로고    scopus 로고
    • Heterogeneity of mprF sequences in methicillin-resistant Staphylococcus aureus clinical isolates: role in cross-resistance between daptomycin and host defense antimicrobial peptides
    • A.S. Bayer, N.N. Mishra, G. Sakoulas, P. Nonejuie, C.C. Nast, J. Pogliano, K.T. Chen, S.N. Ellison, M.R. Yeaman, and S.J. Yang Heterogeneity of mprF sequences in methicillin-resistant Staphylococcus aureus clinical isolates: role in cross-resistance between daptomycin and host defense antimicrobial peptides Antimicrob. Agents Chemother. 58 2014 7462 7467
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 7462-7467
    • Bayer, A.S.1    Mishra, N.N.2    Sakoulas, G.3    Nonejuie, P.4    Nast, C.C.5    Pogliano, J.6    Chen, K.T.7    Ellison, S.N.8    Yeaman, M.R.9    Yang, S.J.10
  • 63
    • 84855730184 scopus 로고    scopus 로고
    • Characterization of daptomycin oligomerization with perylene excimer fluorescence: stoichiometric binding of phosphatidylglycerol triggers oligomer formation
    • J.K. Muraih, J. Harris, S.D. Taylor, and M. Palmer Characterization of daptomycin oligomerization with perylene excimer fluorescence: stoichiometric binding of phosphatidylglycerol triggers oligomer formation Biochim. Biophys. Acta 1818 2012 673 678
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 673-678
    • Muraih, J.K.1    Harris, J.2    Taylor, S.D.3    Palmer, M.4
  • 64
    • 0034128095 scopus 로고    scopus 로고
    • In vitro resistance of Staphylococcus aureus to thrombin-induced platelet microbicidal protein is associated with alterations in cytoplasmic membrane fluidity
    • A.S. Bayer, R. Prasad, J. Chandra, A. Koul, M. Smriti, A. Varma, R.A. Skurray, N. Firth, M.H. Brown, S.P. Koo, and M.R. Yeaman In vitro resistance of Staphylococcus aureus to thrombin-induced platelet microbicidal protein is associated with alterations in cytoplasmic membrane fluidity Infect. Immun. 68 2000 3548 3553
    • (2000) Infect. Immun. , vol.68 , pp. 3548-3553
    • Bayer, A.S.1    Prasad, R.2    Chandra, J.3    Koul, A.4    Smriti, M.5    Varma, A.6    Skurray, R.A.7    Firth, N.8    Brown, M.H.9    Koo, S.P.10    Yeaman, M.R.11
  • 65
    • 84872836267 scopus 로고    scopus 로고
    • Correlation of cell membrane lipid profiles with daptomycin resistance in methicillin-resistant Staphylococcus aureus
    • N.N. Mishra, and A.S. Bayer Correlation of cell membrane lipid profiles with daptomycin resistance in methicillin-resistant Staphylococcus aureus Antimicrob. Agents Chemother. 57 2013 1082 1085
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 1082-1085
    • Mishra, N.N.1    Bayer, A.S.2
  • 66
    • 37849042483 scopus 로고    scopus 로고
    • Failures in clinical treatment of Staphylococcus aureus Infection with daptomycin are associated with alterations in surface charge, membrane phospholipid asymmetry, and drug binding
    • T. Jones, M.R. Yeaman, G. Sakoulas, S.J. Yang, R.A. Proctor, H.G. Sahl, J. Schrenzel, Y.Q. Xiong, and A.S. Bayer Failures in clinical treatment of Staphylococcus aureus Infection with daptomycin are associated with alterations in surface charge, membrane phospholipid asymmetry, and drug binding Antimicrob. Agents Chemother. 52 2008 269 278
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 269-278
    • Jones, T.1    Yeaman, M.R.2    Sakoulas, G.3    Yang, S.J.4    Proctor, R.A.5    Sahl, H.G.6    Schrenzel, J.7    Xiong, Y.Q.8    Bayer, A.S.9
  • 67
    • 80051824106 scopus 로고    scopus 로고
    • In vitro cross-resistance to daptomycin and host defense cationic antimicrobial peptides in clinical methicillin-resistant Staphylococcus aureus isolates
    • N.N. Mishra, J. McKinnell, M.R. Yeaman, A. Rubio, C.C. Nast, L. Chen, B.N. Kreiswirth, and A.S. Bayer In vitro cross-resistance to daptomycin and host defense cationic antimicrobial peptides in clinical methicillin-resistant Staphylococcus aureus isolates Antimicrob. Agents Chemother. 55 2011 4012 4018
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 4012-4018
    • Mishra, N.N.1    McKinnell, J.2    Yeaman, M.R.3    Rubio, A.4    Nast, C.C.5    Chen, L.6    Kreiswirth, B.N.7    Bayer, A.S.8
  • 68
    • 84884243344 scopus 로고    scopus 로고
    • Differential adaptive responses of Staphylococcus aureus to in vitro selection with different antimicrobial peptides
    • T. Shireen, M. Singh, T. Das, and K. Mukhopadhyay Differential adaptive responses of Staphylococcus aureus to in vitro selection with different antimicrobial peptides Antimicrob. Agents Chemother. 57 2013 5134 5137
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 5134-5137
    • Shireen, T.1    Singh, M.2    Das, T.3    Mukhopadhyay, K.4
  • 69
    • 84925690312 scopus 로고    scopus 로고
    • Increased membrane surface positive charge and altered membrane fluidity leads to cationic antimicrobial peptide resistance in Enterococcus faecalis
    • R. Kumariya, S.K. Sood, Y.S. Rajput, N. Saini, and A.K. Garsa Increased membrane surface positive charge and altered membrane fluidity leads to cationic antimicrobial peptide resistance in Enterococcus faecalis Biochim. Biophys. Acta 1848 2015 1367 1375
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 1367-1375
    • Kumariya, R.1    Sood, S.K.2    Rajput, Y.S.3    Saini, N.4    Garsa, A.K.5
  • 70
    • 0030775040 scopus 로고    scopus 로고
    • Modifications of membrane phospholipid composition in nisin-resistant Listeria monocytogenes Scott A
    • A. Verheul, N.J. Russell, T.H.R. Van, F.M. Rombouts, and T. Abee Modifications of membrane phospholipid composition in nisin-resistant Listeria monocytogenes Scott A Appl. Environ. Microbiol. 63 1997 3451 3457
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3451-3457
    • Verheul, A.1    Russell, N.J.2    Van, T.H.R.3    Rombouts, F.M.4    Abee, T.5
  • 71
    • 84901636564 scopus 로고    scopus 로고
    • Mechanisms of nisin resistance in Gram-positive bacteria
    • H. Zhou, J. Fang, Y. Tian, and X.Y. Lu Mechanisms of nisin resistance in Gram-positive bacteria Ann. Microbiol. 64 2014 413 420
    • (2014) Ann. Microbiol. , vol.64 , pp. 413-420
    • Zhou, H.1    Fang, J.2    Tian, Y.3    Lu, X.Y.4
  • 72
    • 84894104284 scopus 로고    scopus 로고
    • Salmonellae PhoPQ regulation of the outer membrane to resist innate immunity
    • Z.D. Dalebroux, and S.I. Miller Salmonellae PhoPQ regulation of the outer membrane to resist innate immunity Curr. Opin. Microbiol. 17 2014 106 113
    • (2014) Curr. Opin. Microbiol. , vol.17 , pp. 106-113
    • Dalebroux, Z.D.1    Miller, S.I.2
  • 73
    • 84903697585 scopus 로고    scopus 로고
    • Lysylated phospholipids stabilize models of bacterial lipid bilayers and protect against antimicrobial peptides
    • E. Cox, A. Michalak, S. Pagentine, P. Seaton, and A. Pokorny Lysylated phospholipids stabilize models of bacterial lipid bilayers and protect against antimicrobial peptides Biochim. Biophys. Acta 1838 2014 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
  • 74
    • 79955769157 scopus 로고    scopus 로고
    • The dlt operon confers resistance to cationic antimicrobial peptides in Clostridium difficile
    • S.M. McBride, and A.L. Sonenshein The dlt operon confers resistance to cationic antimicrobial peptides in Clostridium difficile Microbiology 157 2011 1457 1465
    • (2011) Microbiology , vol.157 , pp. 1457-1465
    • McBride, S.M.1    Sonenshein, A.L.2
  • 76
    • 25144519572 scopus 로고    scopus 로고
    • D-alanylation of teichoic acids promotes group a streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion
    • S.A. Kristian, V. Datta, C. Weidenmaier, R. Kansal, I. Fedtke, A. Peschel, R.L. Gallo, and V. Nizet D-alanylation of teichoic acids promotes group a streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion J. Bacteriol. 187 2005 6719 6725
    • (2005) J. Bacteriol. , vol.187 , pp. 6719-6725
    • Kristian, S.A.1    Datta, V.2    Weidenmaier, C.3    Kansal, R.4    Fedtke, I.5    Peschel, A.6    Gallo, R.L.7    Nizet, V.8
  • 77
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria
    • F.C. Neuhaus, and J. Baddiley A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria Microbiol. Mol. Biol. Rev. 67 2003 686 723
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 78
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • A. Peschel, and H.G. Sahl The co-evolution of host cationic antimicrobial peptides and microbial resistance Nat. Rev. Microbiol. 4 2006 529 536
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 79
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • A. Peschel, M. Otto, R.W. Jack, H. Kalbacher, G. Jung, and F. Gotz Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides J. Biol. Chem. 274 1999 8405 8410
    • (1999) J. Biol. Chem. , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Gotz, F.6
  • 80
    • 77955352834 scopus 로고    scopus 로고
    • Cell wall thickening is not a universal accompaniment of the daptomycin nonsusceptibility phenotype in Staphylococcus aureus: evidence for multiple resistance mechanisms
    • S.J. Yang, C.C. Nast, N.N. Mishra, M.R. Yeaman, P.D. Fey, and A.S. Bayer Cell wall thickening is not a universal accompaniment of the daptomycin nonsusceptibility phenotype in Staphylococcus aureus: evidence for multiple resistance mechanisms Antimicrob. Agents Chemother. 54 2010 3079 3085
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 3079-3085
    • Yang, S.J.1    Nast, C.C.2    Mishra, N.N.3    Yeaman, M.R.4    Fey, P.D.5    Bayer, A.S.6
  • 81
    • 33644655658 scopus 로고    scopus 로고
    • Correlation between reduced daptomycin susceptibility and vancomycin resistance in vancomycin-intermediate Staphylococcus aureus
    • L. Cui, E. Tominaga, H.M. Neoh, and K. Hiramatsu Correlation between reduced daptomycin susceptibility and vancomycin resistance in vancomycin-intermediate Staphylococcus aureus Antimicrob. Agents Chemother. 50 2006 1079 1082
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1079-1082
    • Cui, L.1    Tominaga, E.2    Neoh, H.M.3    Hiramatsu, K.4
  • 82
    • 0029998451 scopus 로고    scopus 로고
    • Cell wall changes in nisin-resistant variants of Listeria innocua grown in the presence of high nisin concentrations
    • S. Maisnier-Patin, and J. Richard Cell wall changes in nisin-resistant variants of Listeria innocua grown in the presence of high nisin concentrations FEMS Microbiol. Lett. 140 1996 29 35
    • (1996) FEMS Microbiol. Lett. , vol.140 , pp. 29-35
    • Maisnier-Patin, S.1    Richard, J.2
  • 83
    • 84907487882 scopus 로고    scopus 로고
    • Lipoteichoic acid synthesis and function in gram-positive bacteria
    • M.G. Percy, and A. Grundling Lipoteichoic acid synthesis and function in gram-positive bacteria Annu. Rev. Microbiol. 68 2014 81 100
    • (2014) Annu. Rev. Microbiol. , vol.68 , pp. 81-100
    • Percy, M.G.1    Grundling, A.2
  • 84
    • 0035065254 scopus 로고    scopus 로고
    • The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix
    • X. Zogaj, M. Nimtz, M. Rohde, W. Bokranz, and U. Romling The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix Mol. Microbiol. 39 2001 1452 1463
    • (2001) Mol. Microbiol. , vol.39 , pp. 1452-1463
    • Zogaj, X.1    Nimtz, M.2    Rohde, M.3    Bokranz, W.4    Romling, U.5
  • 85
    • 0041335452 scopus 로고    scopus 로고
    • Extracellular polysaccharides associated with thin aggregative fimbriae of Salmonella enterica serovar enteritidis
    • A.P. White, D.L. Gibson, S.K. Collinson, P.A. Banser, and W.W. Kay Extracellular polysaccharides associated with thin aggregative fimbriae of Salmonella enterica serovar enteritidis J. Bacteriol. 185 2003 5398 5407
    • (2003) J. Bacteriol. , vol.185 , pp. 5398-5407
    • White, A.P.1    Gibson, D.L.2    Collinson, S.K.3    Banser, P.A.4    Kay, W.W.5
  • 86
    • 32044472091 scopus 로고    scopus 로고
    • Capsular polysaccharide surrounds smooth and rugose types of Salmonella enterica serovar Typhimurium DT104
    • C.E. de Rezende, Y. Anriany, L.E. Carr, S.W. Joseph, and R.M. Weiner Capsular polysaccharide surrounds smooth and rugose types of Salmonella enterica serovar Typhimurium DT104 Appl. Environ. Microbiol. 71 2005 7345 7351
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 7345-7351
    • De Rezende, C.E.1    Anriany, Y.2    Carr, L.E.3    Joseph, S.W.4    Weiner, R.M.5
  • 87
    • 0034820507 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharides and innate immunity
    • C. Alexander, and E.T. Rietschel Bacterial lipopolysaccharides and innate immunity J. Endotoxin Res. 7 2001 167 202
    • (2001) J. Endotoxin Res. , vol.7 , pp. 167-202
    • Alexander, C.1    Rietschel, E.T.2
  • 89
    • 15444370838 scopus 로고    scopus 로고
    • A molecular mechanism for lipopolysaccharide protection of Gram-negative bacteria from antimicrobial peptides
    • N. Papo, and Y. Shai A molecular mechanism for lipopolysaccharide protection of Gram-negative bacteria from antimicrobial peptides J. Biol. Chem. 280 2005 10378 10387
    • (2005) J. Biol. Chem. , vol.280 , pp. 10378-10387
    • Papo, N.1    Shai, Y.2
  • 90
    • 0034596969 scopus 로고    scopus 로고
    • Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria
    • R.E. Bishop, H.S. Gibbons, T. Guina, M.S. Trent, S.I. Miller, and C.R. Raetz Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria EMBO J. 19 2000 5071 5080
    • (2000) EMBO J. , vol.19 , pp. 5071-5080
    • Bishop, R.E.1    Gibbons, H.S.2    Guina, T.3    Trent, M.S.4    Miller, S.I.5    Raetz, C.R.6
  • 91
    • 64649088018 scopus 로고    scopus 로고
    • Outer membrane permeability and antibiotic resistance
    • A.H. Delcour Outer membrane permeability and antibiotic resistance Biochim. Biophys. Acta 1794 2009 808 816
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 808-816
    • Delcour, A.H.1
  • 92
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • L. Guo, K.B. Lim, C.M. Poduje, M. Daniel, J.S. Gunn, M. Hackett, and S.I. Miller Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides Cell 95 1998 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
  • 93
    • 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
    • M. Robey, W. O'Connell, and N.P. Cianciotto Identification of Legionella pneumophila rcp, a pagP-like gene that confers resistance to cationic antimicrobial peptides and promotes intracellular infection Infect. Immun. 69 2001 4276 4286
    • (2001) Infect. Immun. , vol.69 , pp. 4276-4286
    • Robey, M.1    O'Connell, W.2    Cianciotto, N.P.3
  • 94
    • 0035937824 scopus 로고    scopus 로고
    • A PhoP/PhoQ-induced Lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium
    • M.S. Trent, W. Pabich, C.R. Raetz, and S.I. Miller A PhoP/PhoQ-induced Lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium J. Biol. Chem. 276 2001 9083 9092
    • (2001) J. Biol. Chem. , vol.276 , pp. 9083-9092
    • Trent, M.S.1    Pabich, W.2    Raetz, C.R.3    Miller, S.I.4
  • 95
    • 15244348949 scopus 로고    scopus 로고
    • Inhibition of Salmonella enterica serovar Typhimurium lipopolysaccharide deacylation by aminoarabinose membrane modification
    • K. Kawasaki, R.K. Ernst, and S.I. Miller Inhibition of Salmonella enterica serovar Typhimurium lipopolysaccharide deacylation by aminoarabinose membrane modification J. Bacteriol. 187 2005 2448 2457
    • (2005) J. Bacteriol. , vol.187 , pp. 2448-2457
    • Kawasaki, K.1    Ernst, R.K.2    Miller, S.I.3
  • 96
    • 78049370418 scopus 로고    scopus 로고
    • Latency of the lipid A deacylase PagL is involved in producing a robust permeation barrier in the outer membrane of Salmonella enterica
    • K. Kawasaki, and T. Manabe Latency of the lipid A deacylase PagL is involved in producing a robust permeation barrier in the outer membrane of Salmonella enterica J. Bacteriol. 192 2010 5837 5840
    • (2010) J. Bacteriol. , vol.192 , pp. 5837-5840
    • Kawasaki, K.1    Manabe, T.2
  • 97
    • 34347387346 scopus 로고    scopus 로고
    • Release of the lipopolysaccharide deacylase PagL from latency compensates for a lack of lipopolysaccharide aminoarabinose modification-dependent resistance to the antimicrobial peptide polymyxin B in Salmonella enterica
    • K. Kawasaki, K. China, and M. Nishijima Release of the lipopolysaccharide deacylase PagL from latency compensates for a lack of lipopolysaccharide aminoarabinose modification-dependent resistance to the antimicrobial peptide polymyxin B in Salmonella enterica J. Bacteriol. 189 2007 4911 4919
    • (2007) J. Bacteriol. , vol.189 , pp. 4911-4919
    • Kawasaki, K.1    China, K.2    Nishijima, M.3
  • 98
    • 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
    • J.V. Hankins, J.A. Madsen, D.K. Giles, J.S. Brodbelt, and M.S. Trent Amino acid addition to Vibrio cholerae LPS establishes a link between surface remodeling in gram-positive and gram-negative bacteria Proc. Natl. Acad. Sci. U. S. A. 109 2012 8722 8727
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 99
    • 84855288788 scopus 로고    scopus 로고
    • Helicobacter pylori versus the host: remodeling of the bacterial outer membrane is required for survival in the gastric mucosa
    • T.W. Cullen, D.K. Giles, L.N. Wolf, C. Ecobichon, I.G. Boneca, and M.S. Trent Helicobacter pylori versus the host: remodeling of the bacterial outer membrane is required for survival in the gastric mucosa PLoS Pathog. 7 2011 e1002454
    • (2011) PLoS Pathog. , vol.7
    • Cullen, T.W.1    Giles, D.K.2    Wolf, L.N.3    Ecobichon, C.4    Boneca, I.G.5    Trent, M.S.6
  • 100
    • 0029010091 scopus 로고
    • Lipopolysaccharides of polymyxin B-resistant mutants of Escherichia coli are extensively substituted by 2-aminoethyl pyrophosphate and contain aminoarabinose in lipid A
    • K. Nummila, I. Kilpelainen, U. Zahringer, M. Vaara, and I.M. Helander Lipopolysaccharides of polymyxin B-resistant mutants of Escherichia coli are extensively substituted by 2-aminoethyl pyrophosphate and contain aminoarabinose in lipid A Mol. Microbiol. 16 1995 271 278
    • (1995) Mol. Microbiol. , vol.16 , pp. 271-278
    • Nummila, K.1    Kilpelainen, I.2    Zahringer, U.3    Vaara, M.4    Helander, I.M.5
  • 101
    • 3042513872 scopus 로고    scopus 로고
    • The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica
    • H. Lee, F.F. Hsu, J. Turk, and E.A. Groisman The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica J. Bacteriol. 186 2004 4124 4133
    • (2004) J. Bacteriol. , vol.186 , pp. 4124-4133
    • Lee, H.1    Hsu, F.F.2    Turk, J.3    Groisman, E.A.4
  • 102
    • 20444383858 scopus 로고    scopus 로고
    • A phosphoethanolamine transferase specific for the outer 3-deoxy-d-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca2 + hypersensitivity of an eptB deletion mutant
    • C.M. Reynolds, S.R. Kalb, R.J. Cotter, and C.R. Raetz A phosphoethanolamine transferase specific for the outer 3-deoxy-d-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca2 + hypersensitivity of an eptB deletion mutant J. Biol. Chem. 280 2005 21202 21211
    • (2005) J. Biol. Chem. , vol.280 , pp. 21202-21211
    • Reynolds, C.M.1    Kalb, S.R.2    Cotter, R.J.3    Raetz, C.R.4
  • 104
    • 0037797311 scopus 로고    scopus 로고
    • Phosphorylation of the lipid A region of meningococcal lipopolysaccharide: identification of a family of transferases that add phosphoethanolamine to lipopolysaccharide
    • A.D. Cox, J.C. Wright, J. Li, D.W. Hood, E.R. Moxon, and J.C. Richards Phosphorylation of the lipid A region of meningococcal lipopolysaccharide: identification of a family of transferases that add phosphoethanolamine to lipopolysaccharide J. Bacteriol. 185 2003 3270 3277
    • (2003) J. Bacteriol. , vol.185 , pp. 3270-3277
    • Cox, A.D.1    Wright, J.C.2    Li, J.3    Hood, D.W.4    Moxon, E.R.5    Richards, J.C.6
  • 105
    • 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
    • L.A. Lewis, B. Choudhury, J.T. Balthazar, L.E. Martin, S. Ram, P.A. Rice, D.S. Stephens, R. Carlson, and W.M. Shafer Phosphoethanolamine substitution of lipid A and resistance of Neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum Infect. Immun. 77 2009 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
  • 107
    • 35048828537 scopus 로고    scopus 로고
    • PhoPQ-mediated regulation produces a more robust permeability barrier in the outer membrane of Salmonella enterica serovar typhimurium
    • T. Murata, W. Tseng, T. Guina, S.I. Miller, and H. Nikaido PhoPQ-mediated regulation produces a more robust permeability barrier in the outer membrane of Salmonella enterica serovar typhimurium J. Bacteriol. 189 2007 7213 7222
    • (2007) J. Bacteriol. , vol.189 , pp. 7213-7222
    • Murata, T.1    Tseng, W.2    Guina, T.3    Miller, S.I.4    Nikaido, H.5
  • 108
    • 0035900775 scopus 로고    scopus 로고
    • An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-l-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor
    • M.S. Trent, A.A. Ribeiro, S. Lin, R.J. Cotter, and C.R. Raetz An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-l-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor J. Biol. Chem. 276 2001 43122 43131
    • (2001) J. Biol. Chem. , vol.276 , pp. 43122-43131
    • Trent, M.S.1    Ribeiro, A.A.2    Lin, S.3    Cotter, R.J.4    Raetz, C.R.5
  • 109
    • 84865569883 scopus 로고    scopus 로고
    • Aminoarabinose is essential for lipopolysaccharide export and intrinsic antimicrobial peptide resistance in Burkholderia cenocepacia
    • M.A. Hamad, F. Di Lorenzo, A. Molinaro, and M.A. Valvano Aminoarabinose is essential for lipopolysaccharide export and intrinsic antimicrobial peptide resistance in Burkholderia cenocepacia Mol. Microbiol. 85 2012 962 974
    • (2012) Mol. Microbiol. , vol.85 , pp. 962-974
    • Hamad, M.A.1    Di Lorenzo, F.2    Molinaro, A.3    Valvano, M.A.4
  • 110
    • 44949245096 scopus 로고    scopus 로고
    • Glucosamine found as a substituent of both phosphate groups in Bordetella lipid A backbones: role of a BvgAS-activated ArnT ortholog
    • N. Marr, A. Tirsoaga, D. Blanot, R. Fernandez, and M. Caroff Glucosamine found as a substituent of both phosphate groups in Bordetella lipid A backbones: role of a BvgAS-activated ArnT ortholog J. Bacteriol. 190 2008 4281 4290
    • (2008) J. Bacteriol. , vol.190 , pp. 4281-4290
    • Marr, N.1    Tirsoaga, A.2    Blanot, D.3    Fernandez, R.4    Caroff, M.5
  • 111
    • 84876909495 scopus 로고    scopus 로고
    • Minor modifications to the phosphate groups and the C3′ acyl chain length of lipid A in two Bordetella pertussis strains, BP338 and 18-323, independently affect Toll-like receptor 4 protein activation
    • N.R. Shah, S. Albitar-Nehme, E. Kim, N. Marr, A. Novikov, M. Caroff, and R.C. Fernandez Minor modifications to the phosphate groups and the C3′ acyl chain length of lipid A in two Bordetella pertussis strains, BP338 and 18-323, independently affect Toll-like receptor 4 protein activation J. Biol. Chem. 288 2013 11751 11760
    • (2013) J. Biol. Chem. , vol.288 , pp. 11751-11760
    • Shah, N.R.1    Albitar-Nehme, S.2    Kim, E.3    Marr, N.4    Novikov, A.5    Caroff, M.6    Fernandez, R.C.7
  • 112
    • 84905400756 scopus 로고    scopus 로고
    • Bordetella pertussis lipid A glucosamine modification confers resistance to cationic antimicrobial peptides and increases resistance to outer membrane perturbation
    • N.R. Shah, R.E. Hancock, and R.C. Fernandez Bordetella pertussis lipid A glucosamine modification confers resistance to cationic antimicrobial peptides and increases resistance to outer membrane perturbation Antimicrob. Agents Chemother. 58 2014 4931 4934
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 4931-4934
    • Shah, N.R.1    Hancock, R.E.2    Fernandez, R.C.3
  • 113
    • 33845256842 scopus 로고    scopus 로고
    • Structure and biosynthesis of free lipid A molecules that replace lipopolysaccharide in Francisella tularensis subsp. novicida
    • X. Wang, A.A. Ribeiro, Z. Guan, S.C. McGrath, R.J. Cotter, and C.R. Raetz Structure and biosynthesis of free lipid A molecules that replace lipopolysaccharide in Francisella tularensis subsp. novicida Biochemistry 45 2006 14427 14440
    • (2006) Biochemistry , vol.45 , pp. 14427-14440
    • Wang, X.1    Ribeiro, A.A.2    Guan, Z.3    McGrath, S.C.4    Cotter, R.J.5    Raetz, C.R.6
  • 115
    • 64349107708 scopus 로고    scopus 로고
    • Identification of undecaprenyl phosphate-beta-D-galactosamine in Francisella novicida and its function in lipid A modification
    • X. Wang, A.A. Ribeiro, Z. Guan, and C.R. Raetz Identification of undecaprenyl phosphate-beta-D-galactosamine in Francisella novicida and its function in lipid A modification Biochemistry 48 2009 1162 1172
    • (2009) Biochemistry , vol.48 , pp. 1162-1172
    • Wang, X.1    Ribeiro, A.A.2    Guan, Z.3    Raetz, C.R.4
  • 117
    • 66549099729 scopus 로고    scopus 로고
    • O-antigen-negative Salmonella enterica serovar Typhimurium is attenuated in intestinal colonization but elicits colitis in streptomycin-treated mice
    • K. Ilg, K. Endt, B. Misselwitz, B. Stecher, M. Aebi, and W.D. Hardt O-antigen-negative Salmonella enterica serovar Typhimurium is attenuated in intestinal colonization but elicits colitis in streptomycin-treated mice Infect. Immun. 77 2009 2568 2575
    • (2009) Infect. Immun. , vol.77 , pp. 2568-2575
    • Ilg, K.1    Endt, K.2    Misselwitz, B.3    Stecher, B.4    Aebi, M.5    Hardt, W.D.6
  • 119
    • 80052345809 scopus 로고    scopus 로고
    • The PmrA/PmrB regulatory system controls the expression of the wzzfepE gene involved in the O-antigen synthesis of Salmonella enterica serovar Typhimurium
    • L. Pescaretti Mde, F.E. Lopez, R.D. Morero, and M.A. Delgado The PmrA/PmrB regulatory system controls the expression of the wzzfepE gene involved in the O-antigen synthesis of Salmonella enterica serovar Typhimurium Microbiology 157 2011 2515 2521
    • (2011) Microbiology , vol.157 , pp. 2515-2521
    • Pescaretti Mde, L.1    Lopez, F.E.2    Morero, R.D.3    Delgado, M.A.4
  • 120
    • 0038215392 scopus 로고    scopus 로고
    • Genetic modulation of Shigella flexneri 2a lipopolysaccharide O antigen modal chain length reveals that it has been optimized for virulence
    • R. Morona, C. Daniels, and L. Van Den Bosch Genetic modulation of Shigella flexneri 2a lipopolysaccharide O antigen modal chain length reveals that it has been optimized for virulence Microbiology 149 2003 925 939
    • (2003) Microbiology , vol.149 , pp. 925-939
    • Morona, R.1    Daniels, C.2    Van Den Bosch, L.3
  • 123
    • 11144308980 scopus 로고    scopus 로고
    • Timing and localization of rhamnolipid synthesis gene expression in Pseudomonas aeruginosa biofilms
    • Y. Lequette, and E.P. Greenberg Timing and localization of rhamnolipid synthesis gene expression in Pseudomonas aeruginosa biofilms J. Bacteriol. 187 2005 37 44
    • (2005) J. Bacteriol. , vol.187 , pp. 37-44
    • Lequette, Y.1    Greenberg, E.P.2
  • 124
    • 0037307874 scopus 로고    scopus 로고
    • Rhamnolipid surfactant production affects biofilm architecture in Pseudomonas aeruginosa PAO1
    • M.E. Davey, N.C. Caiazza, and G.A. O'Toole Rhamnolipid surfactant production affects biofilm architecture in Pseudomonas aeruginosa PAO1 J. Bacteriol. 185 2003 1027 1036
    • (2003) J. Bacteriol. , vol.185 , pp. 1027-1036
    • Davey, M.E.1    Caiazza, N.C.2    O'Toole, G.A.3
  • 125
    • 1842612577 scopus 로고    scopus 로고
    • Bacterial biofilms: from the natural environment to infectious diseases
    • L. Hall-Stoodley, J.W. Costerton, and P. Stoodley Bacterial biofilms: from the natural environment to infectious diseases Nat. Rev. Microbiol. 2 2004 95 108
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 95-108
    • Hall-Stoodley, L.1    Costerton, J.W.2    Stoodley, P.3
  • 126
    • 84875058635 scopus 로고    scopus 로고
    • Small regulatory RNAs in the control of motility and biofilm formation in E. coli and Salmonella
    • F. Mika, and R. Hengge Small regulatory RNAs in the control of motility and biofilm formation in E. coli and Salmonella Int. J. Mol. Sci. 14 2013 4560 4579
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 4560-4579
    • Mika, F.1    Hengge, R.2
  • 127
    • 84887628130 scopus 로고    scopus 로고
    • Bacterial biofilm development as a multicellular adaptation: antibiotic resistance and new therapeutic strategies
    • C. de la Fuente-Nunez, F. Reffuveille, L. Fernandez, and R.E. Hancock Bacterial biofilm development as a multicellular adaptation: antibiotic resistance and new therapeutic strategies Curr. Opin. Microbiol. 16 2013 580 589
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 580-589
    • De La Fuente-Nunez, C.1    Reffuveille, F.2    Fernandez, L.3    Hancock, R.E.4
  • 131
    • 33845938063 scopus 로고    scopus 로고
    • Differentiation and distribution of colistin- and sodium dodecyl sulfate-tolerant cells in Pseudomonas aeruginosa biofilms
    • J.A. Haagensen, M. Klausen, R.K. Ernst, S.I. Miller, A. Folkesson, T. Tolker-Nielsen, and S. Molin Differentiation and distribution of colistin- and sodium dodecyl sulfate-tolerant cells in Pseudomonas aeruginosa biofilms J. Bacteriol. 189 2007 28 37
    • (2007) J. Bacteriol. , vol.189 , pp. 28-37
    • Haagensen, J.A.1    Klausen, M.2    Ernst, R.K.3    Miller, S.I.4    Folkesson, A.5    Tolker-Nielsen, T.6    Molin, S.7
  • 132
    • 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
    • S.J. Pamp, M. Gjermansen, H.K. Johansen, and T. Tolker-Nielsen 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. 68 2008 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
  • 133
    • 0038820050 scopus 로고    scopus 로고
    • Gene transfer occurs with enhanced efficiency in biofilms and induces enhanced stabilisation of the biofilm structure
    • S. Molin, and T. Tolker-Nielsen Gene transfer occurs with enhanced efficiency in biofilms and induces enhanced stabilisation of the biofilm structure Curr. Opin. Biotechnol. 14 2003 255 261
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 255-261
    • Molin, S.1    Tolker-Nielsen, T.2
  • 134
    • 46049083393 scopus 로고    scopus 로고
    • Involvement of a novel efflux system in biofilm-specific resistance to antibiotics
    • L. Zhang, and T.F. Mah Involvement of a novel efflux system in biofilm-specific resistance to antibiotics J. Bacteriol. 190 2008 4447 4452
    • (2008) J. Bacteriol. , vol.190 , pp. 4447-4452
    • Zhang, L.1    Mah, T.F.2
  • 137
    • 84875955724 scopus 로고    scopus 로고
    • Role of efflux pumps in the antibiotic resistance of bacteria embedded in a biofilm
    • S.M. Soto Role of efflux pumps in the antibiotic resistance of bacteria embedded in a biofilm Virulence 4 2013 223 229
    • (2013) Virulence , vol.4 , pp. 223-229
    • Soto, S.M.1
  • 138
    • 0031012387 scopus 로고    scopus 로고
    • Measurement of local diffusion coefficients in biofilms by microinjection and confocal microscopy
    • D. de Beer, P. Stoodley, and Z. Lewandowski Measurement of local diffusion coefficients in biofilms by microinjection and confocal microscopy Biotechnol. Bioeng. 53 1997 151 158
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 151-158
    • De Beer, D.1    Stoodley, P.2    Lewandowski, Z.3
  • 139
    • 0344011974 scopus 로고    scopus 로고
    • A genetic basis for Pseudomonas aeruginosa biofilm antibiotic resistance
    • T.F. Mah, B. Pitts, B. Pellock, G.C. Walker, P.S. Stewart, and G.A. O'Toole A genetic basis for Pseudomonas aeruginosa biofilm antibiotic resistance Nature 426 2003 306 310
    • (2003) Nature , vol.426 , pp. 306-310
    • Mah, T.F.1    Pitts, B.2    Pellock, B.3    Walker, G.C.4    Stewart, P.S.5    O'Toole, G.A.6
  • 140
    • 84943817547 scopus 로고    scopus 로고
    • Antibiotic resistance related to biofilm formation in Klebsiella pneumoniae
    • C. Vuotto, F. Longo, M.P. Balice, G. Donelli, and P.E. Varaldo Antibiotic resistance related to biofilm formation in Klebsiella pneumoniae Pathogens 3 2014 743 758
    • (2014) Pathogens , vol.3 , pp. 743-758
    • Vuotto, C.1    Longo, F.2    Balice, M.P.3    Donelli, G.4    Varaldo, P.E.5
  • 141
    • 0242569490 scopus 로고    scopus 로고
    • Antimicrobial resistance of Pseudomonas aeruginosa biofilms
    • E. Drenkard Antimicrobial resistance of Pseudomonas aeruginosa biofilms Microbes Infect. 5 2003 1213 1219
    • (2003) Microbes Infect. , vol.5 , pp. 1213-1219
    • Drenkard, E.1
  • 142
    • 53349169264 scopus 로고    scopus 로고
    • Comparison of acids on the induction of an Acid Tolerance Response in Salmonella typhimurium, consequences for food safety
    • A. Alvarez-Ordonez, A. Fernandez, A. Bernardo, and M. Lopez Comparison of acids on the induction of an Acid Tolerance Response in Salmonella typhimurium, consequences for food safety Meat Sci. 81 2009 65 70
    • (2009) Meat Sci. , vol.81 , pp. 65-70
    • Alvarez-Ordonez, A.1    Fernandez, A.2    Bernardo, A.3    Lopez, M.4
  • 143
    • 0003582512 scopus 로고
    • A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence
    • S.I. Miller, A.M. Kukral, and J.J. Mekalanos A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence Proc. Natl. Acad. Sci. U. S. A. 86 1989 5054 5058
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3
  • 144
    • 0025318414 scopus 로고
    • Constitutive expression of the phoP regulon attenuates Salmonella virulence and survival within macrophages
    • S.I. Miller, and J.J. Mekalanos Constitutive expression of the phoP regulon attenuates Salmonella virulence and survival within macrophages J. Bacteriol. 172 1990 2485 2490
    • (1990) J. Bacteriol. , vol.172 , pp. 2485-2490
    • Miller, S.I.1    Mekalanos, J.J.2
  • 146
    • 0027201144 scopus 로고
    • Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence
    • K.L. Roland, L.E. Martin, C.R. Esther, and J.K. Spitznagel Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence J. Bacteriol. 175 1993 4154 4164
    • (1993) J. Bacteriol. , vol.175 , pp. 4154-4164
    • Roland, K.L.1    Martin, L.E.2    Esther, C.R.3    Spitznagel, J.K.4
  • 147
    • 0029809576 scopus 로고    scopus 로고
    • PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance
    • J.S. Gunn, and S.I. Miller PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance J. Bacteriol. 178 1996 6857 6864
    • (1996) J. Bacteriol. , vol.178 , pp. 6857-6864
    • Gunn, J.S.1    Miller, S.I.2
  • 150
    • 0033759942 scopus 로고    scopus 로고
    • Role of Pseudomonas aeruginosa PhoP-phoQ in resistance to antimicrobial cationic peptides and aminoglycosides
    • E.L. Macfarlane, A. Kwasnicka, and R.E. Hancock Role of Pseudomonas aeruginosa PhoP-phoQ in resistance to antimicrobial cationic peptides and aminoglycosides Microbiology 146 Pt 10 2000 2543 2554
    • (2000) Microbiology , vol.146 , pp. 2543-2554
    • Macfarlane, E.L.1    Kwasnicka, A.2    Hancock, R.E.3
  • 151
    • 0037447083 scopus 로고    scopus 로고
    • Closing the loop: the PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD
    • A. Kato, T. Latifi, and E.A. Groisman Closing the loop: the PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD Proc. Natl. Acad. Sci. U. S. A. 100 2003 4706 4711
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4706-4711
    • Kato, A.1    Latifi, T.2    Groisman, E.A.3
  • 154
    • 72049086558 scopus 로고    scopus 로고
    • Activated by different signals, the PhoP/PhoQ two-component system differentially regulates metal uptake
    • E. Choi, E.A. Groisman, and D. Shin Activated by different signals, the PhoP/PhoQ two-component system differentially regulates metal uptake J. Bacteriol. 191 2009 7174 7181
    • (2009) J. Bacteriol. , vol.191 , pp. 7174-7181
    • Choi, E.1    Groisman, E.A.2    Shin, D.3
  • 155
    • 77956643439 scopus 로고    scopus 로고
    • Salmonella-regulated lipopolysaccharide modifications
    • S.M. Richards, K.L. Strandberg, and J.S. Gunn Salmonella-regulated lipopolysaccharide modifications Subcell. Biochem. 53 2010 101 122
    • (2010) Subcell. Biochem. , vol.53 , pp. 101-122
    • Richards, S.M.1    Strandberg, K.L.2    Gunn, J.S.3
  • 156
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence Cell 84 1996 165 174
    • (1996) Cell , vol.84 , pp. 165-174
    • Garcia Vescovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 157
    • 67651215875 scopus 로고    scopus 로고
    • Bacterial sensing of antimicrobial peptides
    • M. Otto Bacterial sensing of antimicrobial peptides Contrib. Microbiol. 16 2009 136 149
    • (2009) Contrib. Microbiol. , vol.16 , pp. 136-149
    • Otto, M.1
  • 158
    • 84869228820 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides serve as activation signals for the Salmonella Typhimurium PhoPQ and PmrAB regulons in vitro and in vivo
    • S.M. Richards, K.L. Strandberg, M. Conroy, and J.S. Gunn Cationic antimicrobial peptides serve as activation signals for the Salmonella Typhimurium PhoPQ and PmrAB regulons in vitro and in vivo Front. Cell. Infect. Microbiol. 2 2012 102
    • (2012) Front. Cell. Infect. Microbiol. , vol.2 , pp. 102
    • Richards, S.M.1    Strandberg, K.L.2    Conroy, M.3    Gunn, J.S.4
  • 159
    • 84891147511 scopus 로고    scopus 로고
    • Signal-specific temporal response by the Salmonella PhoP/PhoQ regulatory system
    • S.Y. Park, and E.A. Groisman Signal-specific temporal response by the Salmonella PhoP/PhoQ regulatory system Mol. Microbiol. 91 2014 135 144
    • (2014) Mol. Microbiol. , vol.91 , pp. 135-144
    • Park, S.Y.1    Groisman, E.A.2
  • 160
    • 84928910513 scopus 로고    scopus 로고
    • Making the connection: PmrD is required for modifications to Escherichia coli endotoxin that promote antimicrobial resistance
    • E.J. Rubin, C.M. Herrera, A.A. Crofts, and M.S. Trent Making the connection: PmrD is required for modifications to Escherichia coli endotoxin that promote antimicrobial resistance Antimicrob. Agents Chemother. 59 4 2015 2051 2061
    • (2015) Antimicrob. Agents Chemother. , vol.59 , Issue.4 , pp. 2051-2061
    • Rubin, E.J.1    Herrera, C.M.2    Crofts, A.A.3    Trent, M.S.4
  • 161
    • 0034518521 scopus 로고    scopus 로고
    • The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella flexneri
    • J.E. Moss, P.E. Fisher, B. Vick, E.A. Groisman, and A. Zychlinsky The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella flexneri Cell. Microbiol. 2 2000 443 452
    • (2000) Cell. Microbiol. , vol.2 , pp. 443-452
    • Moss, J.E.1    Fisher, P.E.2    Vick, B.3    Groisman, E.A.4    Zychlinsky, A.5
  • 162
    • 0038162593 scopus 로고    scopus 로고
    • The Erwinia chrysanthemi phoP-phoQ operon plays an important role in growth at low pH, virulence and bacterial survival in plant tissue
    • A. Llama-Palacios, E. Lopez-Solanilla, C. Poza-Carrion, F. Garcia-Olmedo, and P. Rodriguez-Palenzuela The Erwinia chrysanthemi phoP-phoQ operon plays an important role in growth at low pH, virulence and bacterial survival in plant tissue Mol. Microbiol. 49 2003 347 357
    • (2003) Mol. Microbiol. , vol.49 , pp. 347-357
    • Llama-Palacios, A.1    Lopez-Solanilla, E.2    Poza-Carrion, C.3    Garcia-Olmedo, F.4    Rodriguez-Palenzuela, P.5
  • 163
    • 79959811246 scopus 로고    scopus 로고
    • Investigation of the Staphylococcus aureus GraSR regulon reveals novel links to virulence, stress response and cell wall signal transduction pathways
    • M. Falord, U. Mader, A. Hiron, M. Debarbouille, and T. Msadek Investigation of the Staphylococcus aureus GraSR regulon reveals novel links to virulence, stress response and cell wall signal transduction pathways PLoS ONE 6 2011 e21323
    • (2011) PLoS ONE , vol.6
    • Falord, M.1    Mader, U.2    Hiron, A.3    Debarbouille, M.4    Msadek, T.5
  • 165
    • 84887605559 scopus 로고    scopus 로고
    • Two unique phosphorylation-driven signaling pathways crosstalk in Staphylococcus aureus to modulate the cell-wall charge: Stk1/Stp1 meets GraSR
    • M. Fridman, G.D. Williams, U. Muzamal, H. Hunter, K.W. Siu, and D. Golemi-Kotra Two unique phosphorylation-driven signaling pathways crosstalk in Staphylococcus aureus to modulate the cell-wall charge: Stk1/Stp1 meets GraSR Biochemistry 52 2013 7975 7986
    • (2013) Biochemistry , vol.52 , pp. 7975-7986
    • Fridman, M.1    Williams, G.D.2    Muzamal, U.3    Hunter, H.4    Siu, K.W.5    Golemi-Kotra, D.6
  • 166
    • 84889850708 scopus 로고    scopus 로고
    • Modulation of cell wall synthesis and susceptibility to vancomycin by the two-component system AirSR in Staphylococcus aureus NCTC8325
    • H. Sun, Y. Yang, T. Xue, and B. Sun Modulation of cell wall synthesis and susceptibility to vancomycin by the two-component system AirSR in Staphylococcus aureus NCTC8325 BMC Microbiol. 13 2013 286
    • (2013) BMC Microbiol. , vol.13 , pp. 286
    • Sun, H.1    Yang, Y.2    Xue, T.3    Sun, B.4
  • 167
    • 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
    • M. Pietiainen, P. Francois, H.L. Hyyrylainen, M. Tangomo, V. Sass, H.G. Sahl, J. Schrenzel, and V.P. Kontinen 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 2009 429
    • (2009) BMC Genomics , vol.10 , pp. 429
    • 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
  • 170
    • 79959953597 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of Salmonella enterica serovar Typhimurium under PhoP/PhoQ activation conditions
    • J.L. Yu, and L. Guo Quantitative proteomic analysis of Salmonella enterica serovar Typhimurium under PhoP/PhoQ activation conditions J. Proteome Res. 10 2011 2992 3002
    • (2011) J. Proteome Res. , vol.10 , pp. 2992-3002
    • Yu, J.L.1    Guo, L.2
  • 171
    • 0035105303 scopus 로고    scopus 로고
    • The pleiotropic two-component regulatory system PhoP-PhoQ
    • E.A. Groisman The pleiotropic two-component regulatory system PhoP-PhoQ J. Bacteriol. 183 2001 1835 1842
    • (2001) J. Bacteriol. , vol.183 , pp. 1835-1842
    • Groisman, E.A.1
  • 172
    • 0035678319 scopus 로고    scopus 로고
    • Salmonella typhimurium outer membrane remodeling: role in resistance to host innate immunity
    • R.K. Ernst, T. Guina, and S.I. Miller Salmonella typhimurium outer membrane remodeling: role in resistance to host innate immunity Microbes Infect. 3 2001 1327 1334
    • (2001) Microbes Infect. , vol.3 , pp. 1327-1334
    • Ernst, R.K.1    Guina, T.2    Miller, S.I.3
  • 173
    • 0025924754 scopus 로고
    • 2+ transport locus of Salmonella typhimurium encodes a P-type ATPase
    • 2+ transport locus of Salmonella typhimurium encodes a P-type ATPase J. Biol. Chem. 266 1991 815 823
    • (1991) J. Biol. Chem. , vol.266 , pp. 815-823
    • Snavely, M.D.1    Miller, C.G.2    Maguire, M.E.3
  • 174
    • 18244379035 scopus 로고    scopus 로고
    • Identification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core
    • R. Tamayo, B. Choudhury, A. Septer, M. Merighi, R. Carlson, and J.S. Gunn Identification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core J. Bacteriol. 187 2005 3391 3399
    • (2005) J. Bacteriol. , vol.187 , pp. 3391-3399
    • Tamayo, R.1    Choudhury, B.2    Septer, A.3    Merighi, M.4    Carlson, R.5    Gunn, J.S.6
  • 175
    • 23344452474 scopus 로고    scopus 로고
    • Resistance to the antimicrobial peptide polymyxin requires myristoylation of Escherichia coli and Salmonella typhimurium lipid A
    • A.X. Tran, M.E. Lester, C.M. Stead, C.R. Raetz, D.J. Maskell, S.C. McGrath, R.J. Cotter, and M.S. Trent Resistance to the antimicrobial peptide polymyxin requires myristoylation of Escherichia coli and Salmonella typhimurium lipid A J. Biol. Chem. 280 2005 28186 28194
    • (2005) J. Biol. Chem. , vol.280 , pp. 28186-28194
    • Tran, A.X.1    Lester, M.E.2    Stead, C.M.3    Raetz, C.R.4    Maskell, D.J.5    McGrath, S.C.6    Cotter, R.J.7    Trent, M.S.8
  • 176
    • 33748294219 scopus 로고    scopus 로고
    • Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III)
    • K. Nishino, F.F. Hsu, J. Turk, M.J. Cromie, M.M. Wosten, and E.A. Groisman Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III) Mol. Microbiol. 61 2006 645 654
    • (2006) Mol. Microbiol. , vol.61 , pp. 645-654
    • Nishino, K.1    Hsu, F.F.2    Turk, J.3    Cromie, M.J.4    Wosten, M.M.5    Groisman, E.A.6
  • 178
    • 79960309927 scopus 로고    scopus 로고
    • The pmrCAB operon mediates polymyxin resistance in Acinetobacter baumannii ATCC 17978 and clinical isolates through phosphoethanolamine modification of lipid A
    • L.A. Arroyo, C.M. Herrera, L. Fernandez, J.V. Hankins, M.S. Trent, and R.E. Hancock The pmrCAB operon mediates polymyxin resistance in Acinetobacter baumannii ATCC 17978 and clinical isolates through phosphoethanolamine modification of lipid A Antimicrob. Agents Chemother. 55 2011 3743 3751
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 3743-3751
    • Arroyo, L.A.1    Herrera, C.M.2    Fernandez, L.3    Hankins, J.V.4    Trent, M.S.5    Hancock, R.E.6
  • 180
    • 77955545870 scopus 로고    scopus 로고
    • Molecular characterization of the PhoPQ-PmrD-PmrAB mediated pathway regulating polymyxin B resistance in Klebsiella pneumoniae CG43
    • H.Y. Cheng, Y.F. Chen, and H.L. Peng Molecular characterization of the PhoPQ-PmrD-PmrAB mediated pathway regulating polymyxin B resistance in Klebsiella pneumoniae CG43 J. Biomed. Sci. 17 2010 60
    • (2010) J. Biomed. Sci. , vol.17 , pp. 60
    • Cheng, H.Y.1    Chen, Y.F.2    Peng, H.L.3
  • 181
    • 77949912181 scopus 로고    scopus 로고
    • The PmrAB system in Erwinia amylovora renders the pathogen more susceptible to polymyxin B and more resistant to excess iron
    • S. Nakka, M. Qi, and Y. Zhao The PmrAB system in Erwinia amylovora renders the pathogen more susceptible to polymyxin B and more resistant to excess iron Res. Microbiol. 161 2010 153 157
    • (2010) Res. Microbiol. , vol.161 , pp. 153-157
    • Nakka, S.1    Qi, M.2    Zhao, Y.3
  • 183
    • 84861108467 scopus 로고    scopus 로고
    • Impact of two-component regulatory systems PhoP-PhoQ and PmrA-PmrB on colistin pharmacodynamics in Pseudomonas aeruginosa
    • N.S. Ly, J. Yang, J.B. Bulitta, and B.T. Tsuji Impact of two-component regulatory systems PhoP-PhoQ and PmrA-PmrB on colistin pharmacodynamics in Pseudomonas aeruginosa Antimicrob. Agents Chemother. 56 2012 3453 3456
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 3453-3456
    • Ly, N.S.1    Yang, J.2    Bulitta, J.B.3    Tsuji, B.T.4
  • 184
    • 12844262283 scopus 로고    scopus 로고
    • Identification and functional analysis of Salmonella enterica serovar Typhimurium PmrA-regulated genes
    • R. Tamayo, A.M. Prouty, and J.S. Gunn Identification and functional analysis of Salmonella enterica serovar Typhimurium PmrA-regulated genes FEMS Immunol. Med. Microbiol. 43 2005 249 258
    • (2005) FEMS Immunol. Med. Microbiol. , vol.43 , pp. 249-258
    • Tamayo, R.1    Prouty, A.M.2    Gunn, J.S.3
  • 185
    • 33644928491 scopus 로고    scopus 로고
    • Role of Salmonella enterica serovar Typhimurium two-component system PreA/PreB in modulating PmrA-regulated gene transcription
    • M. Merighi, A. Carroll-Portillo, A.N. Septer, A. Bhatiya, and J.S. Gunn Role of Salmonella enterica serovar Typhimurium two-component system PreA/PreB in modulating PmrA-regulated gene transcription J. Bacteriol. 188 2006 141 149
    • (2006) J. Bacteriol. , vol.188 , pp. 141-149
    • Merighi, M.1    Carroll-Portillo, A.2    Septer, A.N.3    Bhatiya, A.4    Gunn, J.S.5
  • 186
    • 46249116492 scopus 로고    scopus 로고
    • The GraRS regulatory system controls Staphylococcus aureus susceptibility to antimicrobial host defenses
    • D. Kraus, S. Herbert, S.A. Kristian, A. Khosravi, V. Nizet, F. Gotz, and A. Peschel The GraRS regulatory system controls Staphylococcus aureus susceptibility to antimicrobial host defenses BMC Microbiol. 8 2008 85
    • (2008) BMC Microbiol. , vol.8 , pp. 85
    • Kraus, D.1    Herbert, S.2    Kristian, S.A.3    Khosravi, A.4    Nizet, V.5    Gotz, F.6    Peschel, A.7
  • 187
    • 34547622874 scopus 로고    scopus 로고
    • Interaction of the GraRS two-component system with the VraFG ABC transporter to support vancomycin-intermediate resistance in Staphylococcus aureus
    • M. Meehl, S. Herbert, F. Gotz, and A. Cheung Interaction of the GraRS two-component system with the VraFG ABC transporter to support vancomycin-intermediate resistance in Staphylococcus aureus Antimicrob. Agents Chemother. 51 2007 2679 2689
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2679-2689
    • Meehl, M.1    Herbert, S.2    Gotz, F.3    Cheung, A.4
  • 188
    • 84859444332 scopus 로고    scopus 로고
    • Resistance to antimicrobial peptides in Gram-negative bacteria
    • S. Gruenheid, and H. Le Moual Resistance to antimicrobial peptides in Gram-negative bacteria FEMS Microbiol. Lett. 330 2012 81 89
    • (2012) FEMS Microbiol. Lett. , vol.330 , pp. 81-89
    • Gruenheid, S.1    Le Moual, H.2
  • 189
    • 84861491736 scopus 로고    scopus 로고
    • Therapeutic antimicrobial peptides may compromise natural immunity
    • M.G. Habets, and M.A. Brockhurst Therapeutic antimicrobial peptides may compromise natural immunity Biol. Lett. 8 2012 416 418
    • (2012) Biol. Lett. , vol.8 , pp. 416-418
    • Habets, M.G.1    Brockhurst, M.A.2
  • 191
    • 79551476589 scopus 로고    scopus 로고
    • Substantiation in Enterococcus faecalis of dose-dependent resistance and cross-resistance to pore-forming antimicrobial peptides by use of a polydiacetylene-based colorimetric assay
    • J. Mehla, and S.K. Sood Substantiation in Enterococcus faecalis of dose-dependent resistance and cross-resistance to pore-forming antimicrobial peptides by use of a polydiacetylene-based colorimetric assay Appl. Environ. Microbiol. 77 2011 786 793
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 786-793
    • Mehla, J.1    Sood, S.K.2
  • 194
    • 84929517735 scopus 로고    scopus 로고
    • The lipooligosaccharide modifying enzyme LptA enhances gonococcal defense against human neutrophils
    • J.W. Handing, and A.K. Criss The lipooligosaccharide modifying enzyme LptA enhances gonococcal defense against human neutrophils Cell. Microbiol. 17 6 2014 910 921
    • (2014) Cell. Microbiol. , vol.17 , Issue.6 , pp. 910-921
    • Handing, J.W.1    Criss, A.K.2
  • 195
    • 80051917501 scopus 로고    scopus 로고
    • Elucidation of a novel Vibrio cholerae lipid A secondary hydroxy-acyltransferase and its role in innate immune recognition
    • J.V. Hankins, J.A. Madsen, D.K. Giles, B.M. Childers, K.E. Klose, J.S. Brodbelt, and M.S. Trent Elucidation of a novel Vibrio cholerae lipid A secondary hydroxy-acyltransferase and its role in innate immune recognition Mol. Microbiol. 81 2011 1313 1329
    • (2011) Mol. Microbiol. , vol.81 , pp. 1313-1329
    • Hankins, J.V.1    Madsen, J.A.2    Giles, D.K.3    Childers, B.M.4    Klose, K.E.5    Brodbelt, J.S.6    Trent, M.S.7
  • 196
    • 2442544458 scopus 로고    scopus 로고
    • 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through Toll-like receptor 4
    • K. Kawasaki, R.K. Ernst, and S.I. Miller 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through Toll-like receptor 4 J. Biol. Chem. 279 2004 20044 20048
    • (2004) J. Biol. Chem. , vol.279 , pp. 20044-20048
    • Kawasaki, K.1    Ernst, R.K.2    Miller, S.I.3
  • 198
    • 84894312287 scopus 로고    scopus 로고
    • Lipoteichoic acids, phosphate-containing polymers in the envelope of gram-positive bacteria
    • O. Schneewind, and D. Missiakas Lipoteichoic acids, phosphate-containing polymers in the envelope of gram-positive bacteria J. Bacteriol. 196 2014 1133 1142
    • (2014) J. Bacteriol. , vol.196 , pp. 1133-1142
    • Schneewind, O.1    Missiakas, D.2
  • 199
    • 0028244076 scopus 로고
    • Lipoteichoic acid and lipids in the membrane of Staphylococcus aureus
    • W. Fischer Lipoteichoic acid and lipids in the membrane of Staphylococcus aureus Med. Microbiol. Immunol. 183 1994 61 76
    • (1994) Med. Microbiol. Immunol. , vol.183 , pp. 61-76
    • Fischer, W.1
  • 200


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