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Volumn 61, Issue 10, 2009, Pages 940-953

Tuning the properties of the bacterial membrane with aminoacylated phosphatidylglycerol

Author keywords

Aminoacyl tRNA synthetases; Membrane permeability; Membrane proteins; Phospholipids; Transfer RNAs

Indexed keywords

AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; CEFOXITIN; CEFSULODIN; DAPTOMYCIN; GENTAMICIN; GRAMICIDIN D; GRAMICIDIN S; IMIPENEM; METICILLIN; OXACILLIN; PHOSPHATIDYLGLYCEROL; PHOSPHOLIPID; POLYPEPTIDE ANTIBIOTIC AGENT; VANCOMYCIN; VIRULENCE FACTOR; BACTERIAL PROTEIN; LIGASE; TRANSFER RNA;

EID: 71549148798     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.240     Document Type: Review
Times cited : (90)

References (107)
  • 1
    • 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
    • Trent, M. S., Ribeiro, A. A., Lin, S., Cotter, R. J., and Raetz, C. R. (2001) 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, 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
  • 3
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • Peschel, A. and Sahl, H. G. (2006) The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 4, 529-536.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 4
    • 0036589242 scopus 로고    scopus 로고
    • Mode of action of modified and unmodified bacteriocins from gram-positive bacteria
    • Hechard, Y. and Sahl, H. G. (2002) Mode of action of modified and unmodified bacteriocins from gram-positive bacteria. Biochimie 84, 545-557.
    • (2002) Biochimie , vol.84 , pp. 545-557
    • Hechard, Y.1    Sahl, H.G.2
  • 5
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 6
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • Peschel, A. (2002) How do bacteria resist human antimicrobial peptides? Trends Microbiol. 10, 179-186.
    • (2002) Trends Microbiol. , vol.10 , pp. 179-186
    • Peschel, A.1
  • 8
    • 33750691343 scopus 로고    scopus 로고
    • The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes
    • Thedieck, K., Hain, T., Mohamed, W., Tindall, B. J., Nimtz, M., Chakraborty, T., Wehland, J., and Jansch, L. (2006) The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes. Mol. Microbiol. 62, 1325-1339.
    • (2006) Mol. Microbiol. , vol.62 , pp. 1325-1339
    • Thedieck, K.1    Hain, T.2    Mohamed, W.3    Tindall, B.J.4    Nimtz, M.5    Chakraborty, T.6    Wehland, J.7    Jansch, L.8
  • 9
    • 42449118064 scopus 로고    scopus 로고
    • RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors
    • Roy, H. and Ibba, M. (2008) RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors. Proc. Natl. Acad. Sci. USA 105, 4667-4672.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4667-4672
    • Roy, H.1    Ibba, M.2
  • 10
    • 72949128835 scopus 로고
    • Lipo-amino acid complexes from Bacillus megaterium and their possible role in protein synthesis
    • Hunter, G. D. and Goodsall, R. A. (1961) Lipo-amino acid complexes from Bacillus megaterium and their possible role in protein synthesis. Biochem. J. 78, 564-570.
    • (1961) Biochem. J. , vol.78 , pp. 564-570
    • Hunter, G.D.1    Goodsall, R.A.2
  • 11
    • 1642355674 scopus 로고
    • Characterization of lipoamino-acids as Oamino-acid esters of phosphatidyl-glycerol
    • Macfarlane, M. G. (1962) Characterization of lipoamino-acids as Oamino-acid esters of phosphatidyl-glycerol. Nature 196, 136-138.
    • (1962) Nature , vol.196 , pp. 136-138
    • Macfarlane, M.G.1
  • 12
    • 0013898140 scopus 로고
    • The participation of sRNA in the enzymatic synthesis of O-L-lysyl phosphatidylgylcerol in Staphylococcus aureus
    • Lennarz, W. J., Nesbitt, J. A. III, and Reiss, J. (1966) The participation of sRNA in the enzymatic synthesis of O-L-lysyl phosphatidylgylcerol in Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 55, 934-941.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 934-941
    • Lennarz, W.J.1    Nesbitt III, J.A.2    Reiss, J.3
  • 13
    • 0014544376 scopus 로고
    • Phospholipid composition of Bacillus subtilis
    • den Kamp, J. A., Redai, I., and van Deenen, L. L. (1969) Phospholipid composition of Bacillus subtilis. J. Bacteriol. 99, 298-303.
    • (1969) J. Bacteriol. , vol.99 , pp. 298-303
    • Den Kamp, J.A.1    Redai, I.2    Van Deenen, L.L.3
  • 14
    • 60849121077 scopus 로고    scopus 로고
    • The Bacillus anthracis protein MprF is required for synthesis of lysylphosphatidylglycerols and for resistance to cationic antimicrobial peptides
    • Samant, S., Hsu, F. F., Neyfakh, A. A., and Lee, H. (2009) The Bacillus anthracis protein MprF is required for synthesis of lysylphosphatidylglycerols and for resistance to cationic antimicrobial peptides. J. Bacteriol. 191, 1311-1319.
    • (2009) J. Bacteriol. , vol.191 , pp. 1311-1319
    • Samant, S.1    Hsu, F.F.2    Neyfakh, A.A.3    Lee, H.4
  • 15
    • 33744594351 scopus 로고
    • On the accumulation of amino acid derivatives of phosphatidylglycerol in bacteria
    • Houtsmuller, U. M. and Van, D. (1964) On the accumulation of amino acid derivatives of phosphatidylglycerol in bacteria. Biochim. Biophys. Acta 84, 96-98.
    • (1964) Biochim. Biophys. Acta , vol.84 , pp. 96-98
    • Houtsmuller, U.M.1    Van, D.2
  • 16
    • 38649136233 scopus 로고    scopus 로고
    • Monitoring Lys-tRNA (Lys) phosphatidylglycerol transferase activity
    • Roy, H. and Ibba, M. (2008) Monitoring Lys-tRNA (Lys) phosphatidylglycerol transferase activity. Methods 44, 164-169.
    • (2008) Methods , vol.44 , pp. 164-169
    • Roy, H.1    Ibba, M.2
  • 17
    • 0018386984 scopus 로고
    • Phospholipids of the differentiating bacterium Caulobacter crescentus
    • Jones, D. E. and Smith, J. D. (1979) Phospholipids of the differentiating bacterium Caulobacter crescentus. Can. J. Biochem. 57, 424-428.
    • (1979) Can. J. Biochem. , vol.57 , pp. 424-428
    • Jones, D.E.1    Smith, J.D.2
  • 18
    • 33646190989 scopus 로고    scopus 로고
    • Cohnella thermotolerans gen. nov., sp. nov., and classification of 'Paenibacillus hongkongensis' as Cohnella hongkongensis sp. nov.
    • Kampfer, P., Rossello-Mora, R., Falsen, E., Busse, H. J., and Tindall, B. J. (2006) Cohnella thermotolerans gen. nov., sp. nov., and classification of 'Paenibacillus hongkongensis' as Cohnella hongkongensis sp. nov. Int. J. Syst. Evol. Microbiol. 56, 781-786.
    • (2006) Int. J. Syst. Evol. Microbiol. , vol.56 , pp. 781-786
    • Kampfer, P.1    Rossello-Mora, R.2    Falsen, E.3    Busse, H.J.4    Tindall, B.J.5
  • 19
    • 0017348664 scopus 로고
    • The polar lipids of group B Streptococci. II. Composition and positional distribution of fatty acids
    • Fischer, W. (1977) The polar lipids of group B Streptococci. II. Composition and positional distribution of fatty acids. Biochim. Biophys. Acta 487, 89-104.
    • (1977) Biochim. Biophys. Acta , vol.487 , pp. 89-104
    • Fischer, W.1
  • 21
    • 0013842288 scopus 로고
    • On the amino acid esters of phosphatidyl glycerol from bacteria
    • Houtsmuller, U. M. and van Deenen, L. L. (1965) On the amino acid esters of phosphatidyl glycerol from bacteria. Biochim. Biophys. Acta 106, 564-576.
    • (1965) Biochim. Biophys. Acta , vol.106 , pp. 564-576
    • Houtsmuller, U.M.1    Van Deenen, L.L.2
  • 22
    • 0015082484 scopus 로고
    • Comparison of the phospholipid composition of Bifidobacterium and Lactobacillus strains
    • Exterkate, F. A., Otten, B. J., Wassenberg, H. W., and Veerkamp, J. H. (1971) Comparison of the phospholipid composition of Bifidobacterium and Lactobacillus strains. J. Bacteriol. 106, 824-829.
    • (1971) J. Bacteriol. , vol.106 , pp. 824-829
    • Exterkate, F.A.1    Otten, B.J.2    Wassenberg, H.W.3    Veerkamp, J.H.4
  • 23
    • 0019170696 scopus 로고
    • A phosphatidylinositol-containing derivative of Lactobacillus casei ATCC 7469
    • Smith, M. W. and Steim, J. M. (1980) A phosphatidylinositol-containing derivative of Lactobacillus casei ATCC 7469. Biochim. Biophys. Acta 619, 515-521.
    • (1980) Biochim. Biophys. Acta , vol.619 , pp. 515-521
    • Smith, M.W.1    Steim, J.M.2
  • 24
    • 0019200745 scopus 로고
    • Lipid activation of undecaprenol kinase from Lactobacillus plantarum
    • Kalin, J. R. and Allen, C. M. (1980) Lipid activation of undecaprenol kinase from Lactobacillus plantarum. Biochim. Biophys. Acta 619, 76-89.
    • (1980) Biochim. Biophys. Acta , vol.619 , pp. 76-89
    • Kalin, J.R.1    Allen, C.M.2
  • 25
    • 0032947342 scopus 로고    scopus 로고
    • Polar lipids of four Listeria species containing L-lysylcardiolipin, a novel lipid structure, and other unique phospholipids
    • Fischer, W. and Leopold, K. (1999) Polar lipids of four Listeria species containing L-lysylcardiolipin, a novel lipid structure, and other unique phospholipids. Int. J. Syst. Bacteriol. 49 (Part 2), 653-662.
    • (1999) Int. J. Syst. Bacteriol. , vol.49 , Issue.PART 2 , pp. 653-662
    • Fischer, W.1    Leopold, K.2
  • 26
    • 0024005988 scopus 로고
    • Undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26: Essential factors for the enzymatic activity
    • Koyama, T., Yoshida, I., and Ogura, K. (1988) Undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26: essential factors for the enzymatic activity. J. Biochem. 103, 867-871.
    • (1988) J. Biochem. , vol.103 , pp. 867-871
    • Koyama, T.1    Yoshida, I.2    Ogura, K.3
  • 27
    • 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., and Geiger, O. (2007) 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. 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
  • 28
    • 0021200946 scopus 로고
    • Polar lipid and isoprenoid quinone composition in the classification of Staphylococcus
    • Nahaie, M. R., Goodfellow, M., Minnikin, D. E., and Hajek, V. (1984) Polar lipid and isoprenoid quinone composition in the classification of Staphylococcus. J. Gen. Microbiol. 130, 2427-2437.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2427-2437
    • Nahaie, M.R.1    Goodfellow, M.2    Minnikin, D.E.3    Hajek, V.4
  • 29
    • 0015137521 scopus 로고
    • Metabolism of phosphatidylglycerol, lysylphosphatidylglycerol, and cardiolipin of Staphylococcus aureus
    • Short, S. A. and White, D. C. (1971) Metabolism of phosphatidylglycerol, lysylphosphatidylglycerol, and cardiolipin of Staphylococcus aureus. J. Bacteriol. 108, 219-226.
    • (1971) J. Bacteriol. , vol.108 , pp. 219-226
    • Short, S.A.1    White, D.C.2
  • 30
    • 0014409327 scopus 로고
    • Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. I. Specificity of lysyl phosphatidylglycerol synthetase
    • Nesbitt, J. A. III and Lennarz, W. J. (1968) Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. I. Specificity of lysyl phosphatidylglycerol synthetase. J. Biol. Chem. 243, 3088-3095.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3088-3095
    • Nesbitt III, J.A.1    Lennarz, W.J.2
  • 31
    • 1642555530 scopus 로고    scopus 로고
    • Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol
    • Oku, Y., Kurokawa, K., Ichihashi, N., and Sekimizu, K. (2004) Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol. Microbiology 150, 45-51.
    • (2004) Microbiology , vol.150 , pp. 45-51
    • Oku, Y.1    Kurokawa, K.2    Ichihashi, N.3    Sekimizu, K.4
  • 32
    • 0032467466 scopus 로고    scopus 로고
    • D-Alanylcardiolipin, a major component of the unique lipid pattern of Vagococcus fluvialis
    • Fischer, W. and Arneth-Seifert, D. (1998) D-Alanylcardiolipin, a major component of the unique lipid pattern of Vagococcus fluvialis. J. Bacteriol. 180, 2950-2957.
    • (1998) J. Bacteriol. , vol.180 , pp. 2950-2957
    • Fischer, W.1    Arneth-Seifert, D.2
  • 33
    • 0014409296 scopus 로고
    • Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. II. Specificity of alanyl phosphatidylglycerol synthetase
    • Gould, R. M., Thornton, M. P., Liepkalns, V., and Lennarz, W. J. (1968) Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. II. Specificity of alanyl phosphatidylglycerol synthetase. J. Biol. Chem. 243, 3096-3104.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3096-3104
    • Gould, R.M.1    Thornton, M.P.2    Liepkalns, V.3    Lennarz, W.J.4
  • 34
    • 1642400478 scopus 로고    scopus 로고
    • Phospholipids of Clostridium perfringens: A reexamination
    • Johnston, N. C., Baker, J. K., and Goldfine H. (2004) Phospholipids of Clostridium perfringens: a reexamination. FEMS Microbiol. Lett. 233, 65-68.
    • (2004) FEMS Microbiol. Lett. , vol.233 , pp. 65-68
    • Johnston, N.C.1    Baker, J.K.2    Goldfine, H.3
  • 35
    • 0009705221 scopus 로고
    • Structural composition of polar lipid-amino acid complex in Pseudomonas aeruginosa
    • Sinha, D. B. and Gaby, W. L. (1964) Structural composition of polar lipid-amino acid complex in Pseudomonas aeruginosa. J. Biol. Chem. 239, 3668-3673.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3668-3673
    • Sinha, D.B.1    Gaby, W.L.2
  • 37
    • 0014939253 scopus 로고
    • Amino acid containing phospholipids as major components of the phospholipids of Streptococcus faecalis 10C1
    • Kocun, F. J. (1970) Amino acid containing phospholipids as major components of the phospholipids of Streptococcus faecalis 10C1. Biochim. Biophys. Acta 202, 277-282.
    • (1970) Biochim. Biophys. Acta , vol.202 , pp. 277-282
    • Kocun, F.J.1
  • 38
    • 2942516966 scopus 로고
    • Identification of a bacterial phospholipid as an O-ornithine ester of phosphatidyl glycerol
    • Houtsmuller, U. M. and van, D. L. (1963) Identification of a bacterial phospholipid as an O-ornithine ester of phosphatidyl glycerol. Biochim. Biophys. Acta 70, 211-213.
    • (1963) Biochim. Biophys. Acta , vol.70 , pp. 211-213
    • Houtsmuller, U.M.1    Van, D.L.2
  • 39
    • 0014734120 scopus 로고
    • On the ornithinyl ester of phosphatidylglycerol of Mycobacterium 607
    • Khuller, G. K. and Subrahmanyam, D. (1970) On the ornithinyl ester of phosphatidylglycerol of Mycobacterium 607. J. Bacteriol. 101, 654-656.
    • (1970) J. Bacteriol. , vol.101 , pp. 654-656
    • Khuller, G.K.1    Subrahmanyam, D.2
  • 40
    • 0842325226 scopus 로고    scopus 로고
    • MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance
    • Staubitz, P., Neumann, H., Schneider, T., Wiedemann, I., and Peschel, A. (2004) MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance. FEMS Microbiol. Lett. 231, 67-71.
    • (2004) FEMS Microbiol. Lett. , vol.231 , pp. 67-71
    • Staubitz, P.1    Neumann, H.2    Schneider, T.3    Wiedemann, I.4    Peschel, A.5
  • 41
    • 0032833024 scopus 로고    scopus 로고
    • TRNA glycylation system from Thermus thermophilus, tRNAGly identity and functional interrelation with the glycylation systems from other phylae
    • Mazauric, M. H., Roy, H., and Kern, D. (1999) tRNA glycylation system from Thermus thermophilus, tRNAGly identity and functional interrelation with the glycylation systems from other phylae. Biochemistry 38, 13094-13105.
    • (1999) Biochemistry , vol.38 , pp. 13094-13105
    • Mazauric, M.H.1    Roy, H.2    Kern, D.3
  • 42
    • 0037416970 scopus 로고    scopus 로고
    • FemABX peptidyl transferases: A link between branched-chain cell wall peptide formation and betalactam resistance in gram-positive cocci
    • Rohrer, S. and Berger-Bachi, B. (2003) FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and betalactam resistance in gram-positive cocci. Antimicrob. Agents Chemother. 47, 837-846.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 837-846
    • Rohrer, S.1    Berger-Bachi, B.2
  • 43
    • 18944398046 scopus 로고    scopus 로고
    • Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide- binding cavity of the FemX alanyl transferase from Weissella viridescens
    • Maillard, A. P., Biarrotte-Sorin, S., Villet, R., Mesnage, S., Bouhss, A., Sougakoff, W., Mayer, C., and Arthur, M. (2005) Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens. J. Bacteriol. 187, 3833-3838.
    • (2005) J. Bacteriol. , vol.187 , pp. 3833-3838
    • Maillard, A.P.1    Biarrotte-Sorin, S.2    Villet, R.3    Mesnage, S.4    Bouhss, A.5    Sougakoff, W.6    Mayer, C.7    Arthur, M.8
  • 45
    • 0014429135 scopus 로고
    • Biosynthesis of peptidoglycan of bacterial cell walls. Further, X. study of the glycyl transfer ribonucleic acids active in peptidoglycan synthesis in Staphylococcus aureus
    • Bumsted, R. M., Dahl, J. L., Söll, D., and Strominger, J. L. (1968) Biosynthesis of peptidoglycan of bacterial cell walls. Further, X. study of the glycyl transfer ribonucleic acids active in peptidoglycan synthesis in Staphylococcus aureus. J. Biol. Chem. 243, 779-782.
    • (1968) J. Biol. Chem. , vol.243 , pp. 779-782
    • Bumsted, R.M.1    Dahl, J.L.2    Söll, D.3    Strominger, J.L.4
  • 48
    • 0014115960 scopus 로고
    • Substrate specificity of O-L-lysylphosphatidylglycerol synthetase. Enzymatic studies on the structure of O-L-lysylphosphatidylglycerol
    • Lennarz, W. J., Bonsen, P. P., and van Deenen, L. L. (1967) Substrate specificity of O-L-lysylphosphatidylglycerol synthetase. Enzymatic studies on the structure of O-L-lysylphosphatidylglycerol. Biochemistry 6, 2307-2312.
    • (1967) Biochemistry , vol.6 , pp. 2307-2312
    • Lennarz, W.J.1    Bonsen, P.P.2    Van Deenen, L.L.3
  • 49
    • 0014072242 scopus 로고
    • Synthetic and structural investigations on 3-phosphatidyl-10-(30-O-L- lysyl)glycerol
    • Bonsen, P. P., de Haas, G. H., and van Deenen, L. L. (1967) Synthetic and structural investigations on 3-phosphatidyl-10-(30-O-L-lysyl)glycerol. Biochemistry 6, 1114-1120.
    • (1967) Biochemistry , vol.6 , pp. 1114-1120
    • Bonsen, P.P.1    De Haas, G.H.2    Van Deenen, L.L.3
  • 50
    • 0016142888 scopus 로고
    • Chemical and physicochemical studies of lysylphosphatidylglycerol derivatives. Occurrence of a 20 yields 30 lysyl migration
    • Tocanne, J. F., Verheij, H. M., den Kamp, J. A., and van Deenen, L. L. (1974) Chemical and physicochemical studies of lysylphosphatidylglycerol derivatives. Occurrence of a 20 yields 30 lysyl migration. Chem. Phys. Lipids 13, 389-403.
    • (1974) Chem. Phys. Lipids , vol.13 , pp. 389-403
    • Tocanne, J.F.1    Verheij, H.M.2    Den Kamp, J.A.3    Van Deenen, L.L.4
  • 51
    • 39149115737 scopus 로고    scopus 로고
    • Membrane lipid homeostasis in bacteria
    • Zhang, Y. M. and Rock, C. O. (2008) Membrane lipid homeostasis in bacteria. Nat. Rev. Microbiol. 6, 222-233.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 222-233
    • Zhang, Y.M.1    Rock, C.O.2
  • 52
    • 4644364774 scopus 로고    scopus 로고
    • Identification of a gene required for the formation of lyso-ornithine lipid, an intermediate in the biosynthesis of ornithine-containing lipids
    • Gao, J. L., Weissenmayer, B., Taylor, A. M., Thomas-Oates, J., Lopez-Lara, I. M., and Geiger, O. (2004) Identification of a gene required for the formation of lyso-ornithine lipid, an intermediate in the biosynthesis of ornithine-containing lipids. Mol. Microbiol. 53, 1757-1770.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1757-1770
    • Gao, J.L.1    Weissenmayer, B.2    Taylor, A.M.3    Thomas-Oates, J.4    Lopez-Lara, I.M.5    Geiger, O.6
  • 53
    • 0014212809 scopus 로고
    • Biosynthesis of aminoacyl derivatives of phosphatidylglycerol
    • Gould, R. M. and Lennarz, W. J. (1967) Biosynthesis of aminoacyl derivatives of phosphatidylglycerol. Biochem. Biophys. Res. Commun. 26, 512-515.
    • (1967) Biochem. Biophys. Res. Commun. , vol.26 , pp. 512-515
    • Gould, R.M.1    Lennarz, W.J.2
  • 54
    • 0015513499 scopus 로고
    • Changes in permeability of Staphylococcus aureus and derived liposomes with varying lipid composition
    • Haest, C. W., de Gier, J., den Kamp, J. O., Bartels, P., and van Deenen, L. L. (1972) Changes in permeability of Staphylococcus aureus and derived liposomes with varying lipid composition. Biochim. Biophys. Acta 255, 720-733.
    • (1972) Biochim. Biophys. Acta , vol.255 , pp. 720-733
    • Haest, C.W.1    De Gier, J.2    Den Kamp, J.O.3    Bartels, P.4    Van Deenen, L.L.5
  • 55
    • 57349161246 scopus 로고    scopus 로고
    • Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition
    • Salzberg, L. I. and Helmann, J. D. (2008) Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition. J. Bacteriol 190, 7797-7807.
    • (2008) J. Bacteriol , vol.190 , pp. 7797-7807
    • Salzberg, L.I.1    Helmann, J.D.2
  • 56
    • 14644412812 scopus 로고    scopus 로고
    • Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes
    • Nishibori, A., Kusaka, J., Hara, H., Umeda, M., and Matsumoto, K. (2005) Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes. J. Bacteriol. 187, 2163-2174.
    • (2005) J. Bacteriol. , vol.187 , pp. 2163-2174
    • Nishibori, A.1    Kusaka, J.2    Hara, H.3    Umeda, M.4    Matsumoto, K.5
  • 58
    • 0023239664 scopus 로고
    • Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function
    • Boggs, J. M. (1987) Lipid intermolecular hydrogen bonding: influence on structural organization and membrane function. Biochim. Biophys. Acta 906, 353-404.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 353-404
    • Boggs, J.M.1
  • 59
    • 0017632624 scopus 로고
    • A monolayer (pi,deltaV) study of the ionic properties of alanylphosphatidylglycerol: Effects of pH and ions
    • Sacre, M. M., El Mashak, E. M., and Tocanne, J. F. (1977) A monolayer (pi,deltaV) study of the ionic properties of alanylphosphatidylglycerol: effects of pH and ions. Chem. Phys. Lipids 20, 305-318.
    • (1977) Chem. Phys. Lipids , vol.20 , pp. 305-318
    • Sacre, M.M.1    El Mashak, E.M.2    Tocanne, J.F.3
  • 60
    • 0016063701 scopus 로고
    • A monolayer and freeze-etching study of charged phospholipids. I. Effects of ions and pH on the ionic properties of phosphatidylglycerol and lysylphosphatidylglycerol
    • Tocanne, J. F., Ververgaert, P. H., Verkleij, A. J., and van Deenen, L. L. (1974) A monolayer and freeze-etching study of charged phospholipids. I. Effects of ions and pH on the ionic properties of phosphatidylglycerol and lysylphosphatidylglycerol. Chem. Phys. Lipids 12, 201-219.
    • (1974) Chem. Phys. Lipids , vol.12 , pp. 201-219
    • Tocanne, J.F.1    Ververgaert, P.H.2    Verkleij, A.J.3    Van Deenen, L.L.4
  • 61
    • 0016065635 scopus 로고
    • A monolayer and freeze-etching study of charged phospholipids. II. Ionic properties of mixtures of phosphatidylglycerol and lysylphosphatidylglycerol
    • Tocanne, J. F., Ververgaert, P. H., Verkleij, A. J., and van Deenen, L. L. (1974) A monolayer and freeze-etching study of charged phospholipids. II. Ionic properties of mixtures of phosphatidylglycerol and lysylphosphatidylglycerol. Chem. Phys. Lipids 12, 220-231.
    • (1974) Chem. Phys. Lipids , vol.12 , pp. 220-231
    • Tocanne, J.F.1    Ververgaert, P.H.2    Verkleij, A.J.3    Van Deenen, L.L.4
  • 62
    • 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
    • Jones, T., Yeaman, M. R., Sakoulas, G., Yang, S. J., Proctor, R. A., Sahl, H. G., Schrenzel, J., Xiong, Y. Q., and Bayer, A. S. (2008) 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, 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
  • 63
    • 0041706282 scopus 로고    scopus 로고
    • Inhibitory effects of basic or neutral phospholipid on acidic phospholipid-mediated dissociation of adenine nucleotide bound to DnaA protein, the initiator of chromosomal DNA replication
    • Ichihashi, N., Kurokawa, K., Matsuo, M., Kaito, C., and Sekimizu, K. (2003) Inhibitory effects of basic or neutral phospholipid on acidic phospholipid-mediated dissociation of adenine nucleotide bound to DnaA protein, the initiator of chromosomal DNA replication. J. Biol. Chem. 278, 28778-28786.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28778-28786
    • Ichihashi, N.1    Kurokawa, K.2    Matsuo, M.3    Kaito, C.4    Sekimizu, K.5
  • 64
    • 0015465015 scopus 로고
    • Action of phospholipase a 2 and phospholipase C on Bacillus subtilis protoplasts
    • Op den Kamp, J. A., Kauerz, M. T., and van Deenen, L. L. (1972) Action of phospholipase A 2 and phospholipase C on Bacillus subtilis protoplasts. J. Bacteriol. 112, 1090-1098.
    • (1972) J. Bacteriol. , vol.112 , pp. 1090-1098
    • Op Den Kamp, J.A.1    Kauerz, M.T.2    Van Deenen, L.L.3
  • 65
    • 0347298784 scopus 로고    scopus 로고
    • Role of charge properties of bacterial envelope in bactericidal action of human group IIA phospholipase A2 against Staphylococcus aureus
    • Koprivnjak, T., Peschel, A., Gelb, M. H., Liang, N. S., and Weiss, J. P. (2002) Role of charge properties of bacterial envelope in bactericidal action of human group IIA phospholipase A2 against Staphylococcus aureus. J. Biol. Chem. 277, 47636-47644.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47636-47644
    • Koprivnjak, T.1    Peschel, A.2    Gelb, M.H.3    Liang, N.S.4    Weiss, J.P.5
  • 66
    • 9644266728 scopus 로고    scopus 로고
    • Reduced content of lysyl-phosphatidylglycerol in the cytoplasmic membrane affects susceptibility to moenomycin, as well as vancomycin, gentamicin, and antimicrobial peptides, in Staphylococcus aureus
    • Nishi, H., Komatsuzawa, H., Fujiwara, T., McCallum, N., and Sugai, M. (2004) Reduced content of lysyl-phosphatidylglycerol in the cytoplasmic membrane affects susceptibility to moenomycin, as well as vancomycin, gentamicin, and antimicrobial peptides, in Staphylococcus aureus. Antimicrob. Agents Chemother. 48, 4800-4807.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4800-4807
    • Nishi, H.1    Komatsuzawa, H.2    Fujiwara, T.3    McCallum, N.4    Sugai, M.5
  • 67
    • 0035845595 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene, fmtC, which affects oxacillin resistance in methicillin-resistant Staphylococcus aureus
    • Komatsuzawa, H., Ohta, K., Fujiwara, T., Choi, G. H., Labischinski, H., and Sugai, M. (2001) Cloning and sequencing of the gene, fmtC, which affects oxacillin resistance in methicillin-resistant Staphylococcus aureus. FEMS Microbiol. Lett. 203, 49-54.
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 49-54
    • Komatsuzawa, H.1    Ohta, K.2    Fujiwara, T.3    Choi, G.H.4    Labischinski, H.5    Sugai, M.6
  • 68
    • 33644655658 scopus 로고    scopus 로고
    • Correlation between reduced daptomycin susceptibility and vancomycin resistance in vancomycin-intermediate Staphylococcus aureus
    • Cui, L., Tominaga, E., Neoh, H. M., and Hiramatsu, K. (2006) Correlation between reduced daptomycin susceptibility and vancomycin resistance in vancomycin-intermediate Staphylococcus aureus. Antimicrob. Agents Chemother. 50, 1079-1082.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1079-1082
    • Cui, L.1    Tominaga, E.2    Neoh, H.M.3    Hiramatsu, K.4
  • 69
    • 33646741453 scopus 로고    scopus 로고
    • An association between reduced susceptibility to daptomycin and reduced susceptibility to vancomycin in Staphylococcus aureus
    • Patel, J. B., Jevitt, L. A., Hageman, J., McDonald, L. C., and Tenover, F. C. (2006) An association between reduced susceptibility to daptomycin and reduced susceptibility to vancomycin in Staphylococcus aureus. Clin. Infect. Dis. 42, 1652-1653.
    • (2006) Clin. Infect. Dis. , vol.42 , pp. 1652-1653
    • Patel, J.B.1    Jevitt, L.A.2    Hageman, J.3    McDonald, L.C.4    Tenover, F.C.5
  • 71
    • 23044457737 scopus 로고    scopus 로고
    • Functional interrelationships between cell membrane and cell wall in antimicrobial peptide-mediated killing of Staphylococcus aureus
    • Xiong, Y. Q., Mukhopadhyay, K., Yeaman, M. R., Adler-Moore, J., and Bayer, A. S. (2005) Functional interrelationships between cell membrane and cell wall in antimicrobial peptide-mediated killing of Staphylococcus aureus. Antimicrob. Agents Chemother. 49, 3114-3121.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3114-3121
    • Xiong, Y.Q.1    Mukhopadhyay, K.2    Yeaman, M.R.3    Adler-Moore, J.4    Bayer, A.S.5
  • 72
    • 28444471602 scopus 로고    scopus 로고
    • DltABCD- And MprF-mediated cell envelope modifications of Staphylococcus aureus confer resistance to platelet microbicidal proteins and contribute to virulence in a rabbit endocarditis model
    • Weidenmaier, C., Peschel, A., Kempf, V. A., Lucindo, N., Yeaman, M. R., and Bayer, A. S. (2005) DltABCD- and MprF-mediated cell envelope modifications of Staphylococcus aureus confer resistance to platelet microbicidal proteins and contribute to virulence in a rabbit endocarditis model. Infect. Immun. 73, 8033-8038.
    • (2005) Infect. Immun. , vol.73 , pp. 8033-8038
    • Weidenmaier, C.1    Peschel, A.2    Kempf, V.A.3    Lucindo, N.4    Yeaman, M.R.5    Bayer, A.S.6
  • 73
    • 65649154706 scopus 로고    scopus 로고
    • Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin
    • Hachmann, A. B., Angert, E. R., and Helmann, J. D. (2009) Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin. Antimicrob. Agents Chemother. 53, 1598-1609
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1598-1609
    • Hachmann, A.B.1    Angert, E.R.2    Helmann, J.D.3
  • 75
    • 27944489962 scopus 로고    scopus 로고
    • Expression of tcaA and mprF and glycopeptide resistance in clinical glycopeptideintermediate Staphylococcus aureus (GISA) and heteroGISA strains
    • Wootton, M., Macgowan, A. P., and Walsh, T. R. (2005) Expression of tcaA and mprF and glycopeptide resistance in clinical glycopeptideintermediate Staphylococcus aureus (GISA) and heteroGISA strains. Biochim. Biophys. Acta 1726, 326-327.
    • (2005) Biochim. Biophys. Acta , vol.1726 , pp. 326-327
    • Wootton, M.1    Macgowan, A.P.2    Walsh, T.R.3
  • 76
    • 33744485823 scopus 로고    scopus 로고
    • Genetic changes that correlate with reduced susceptibility to daptomycin in Staphylococcus aureus
    • Friedman, L., Alder, J. D., and Silverman, J. A. (2006) Genetic changes that correlate with reduced susceptibility to daptomycin in Staphylococcus aureus. Antimicrob. Agents Chemother. 50, 2137-2145.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 2137-2145
    • Friedman, L.1    Alder, J.D.2    Silverman, J.A.3
  • 78
    • 34250189880 scopus 로고    scopus 로고
    • Daptomycin nonsusceptibility in Staphylococcus aureus with reduced vancomycin susceptibility is independent of alterations in MprF
    • Pillai, S. K., Gold, H. S., Sakoulas, G., Wennersten, C., Moellering, R. C. Jr., and Eliopoulos, G. M. (2007) Daptomycin nonsusceptibility in Staphylococcus aureus with reduced vancomycin susceptibility is independent of alterations in MprF. Antimicrob. Agents Chemother. 51, 2223-2225.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2223-2225
    • Pillai, S.K.1    Gold, H.S.2    Sakoulas, G.3    Wennersten, C.4    Moellering Jr., R.C.5    Eliopoulos, G.M.6
  • 79
    • 50249138332 scopus 로고    scopus 로고
    • Daptomycin non-susceptible meticillin-resistant Staphylococcus aureus USA 300 isolate
    • Murthy, M. H., Olson, M. E., Wickert, R. W., Fey, P. D., and Jalali, Z. (2008) Daptomycin non-susceptible meticillin-resistant Staphylococcus aureus USA 300 isolate. J. Med. Microbiol. 57, 1036-1038.
    • (2008) J. Med. Microbiol. , vol.57 , pp. 1036-1038
    • Murthy, M.H.1    Olson, M.E.2    Wickert, R.W.3    Fey, P.D.4    Jalali, Z.5
  • 80
    • 77951126947 scopus 로고    scopus 로고
    • Evaluation of daptomycin activity against Staphylococcus aureus following vancomycin exposure in an in vitro pharmacodynamic model with simulated endocardial vegetations
    • Rose, W. E., Leonard, S. N., Sakoulas, G., Kaatz, G. W., Zervos, M. M., Sheth, A., Carpenter, C. F., and Rybak, M. J. (2007) Evaluation of daptomycin activity against Staphylococcus aureus following vancomycin exposure in an in vitro pharmacodynamic model with simulated endocardial vegetations. Antimicrob. Agents Chemother.
    • (2007) Antimicrob. Agents Chemother.
    • Rose, W.E.1    Leonard, S.N.2    Sakoulas, G.3    Kaatz, G.W.4    Zervos, M.M.5    Sheth, A.6    Carpenter, C.F.7    Rybak, M.J.8
  • 81
    • 34548204872 scopus 로고    scopus 로고
    • Perspectives on daptomycin resistance, with emphasis on resistance in Staphylococcus aureus
    • Boucher, H. W. and Sakoulas, G. (2007) Perspectives on daptomycin resistance, with emphasis on resistance in Staphylococcus aureus. Clin. Infect. Dis. 45, 601-608.
    • (2007) Clin. Infect. Dis. , vol.45 , pp. 601-608
    • Boucher, H.W.1    Sakoulas, G.2
  • 82
    • 57049134826 scopus 로고    scopus 로고
    • Serial daptomycin selection generates daptomycin-nonsusceptible Staphylococcus aureus strains with a heterogeneous vancomycin-intermediate phenotype
    • Camargo, I. L., Neoh, H. M., Cui, L., and Hiramatsu, K. (2008) Serial daptomycin selection generates daptomycin-nonsusceptible Staphylococcus aureus strains with a heterogeneous vancomycin-intermediate phenotype. Antimicrob. Agents Chemother. 52, 4289-4299.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 4289-4299
    • Camargo, I.L.1    Neoh, H.M.2    Cui, L.3    Hiramatsu, K.4
  • 83
    • 40549101845 scopus 로고    scopus 로고
    • Daptomycin activity against Staphylococcus aureus following vancomycin exposure in an in vitro pharmacodynamic model with simulated endocardial vegetations
    • Rose, W. E., Leonard, S. N., Sakoulas, G., Kaatz, G. W., Zervos, M. J., Sheth, A., Carpenter, C. F., and Rybak, M. J. (2008) Daptomycin activity against Staphylococcus aureus following vancomycin exposure in an in vitro pharmacodynamic model with simulated endocardial vegetations. Antimicrob. Agents Chemother. 52, 831-836.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 831-836
    • Rose, W.E.1    Leonard, S.N.2    Sakoulas, G.3    Kaatz, G.W.4    Zervos, M.J.5    Sheth, A.6    Carpenter, C.F.7    Rybak, M.J.8
  • 84
    • 0015666462 scopus 로고
    • Regulation of the bacterial cell wall: Effect of antibiotics on lipid biosynthesis
    • Hebeler, B. H., Chatterjee, A. N., and Young, F. E. (1973) Regulation of the bacterial cell wall: effect of antibiotics on lipid biosynthesis. Antimicrob. Agents Chemother. 4, 346-353.
    • (1973) Antimicrob. Agents Chemother. , vol.4 , pp. 346-353
    • Hebeler, B.H.1    Chatterjee, A.N.2    Young, F.E.3
  • 85
    • 0019475302 scopus 로고
    • Effect of methicillin on the fatty acid composition of phospholipids in methicillin sensitive Staphylococcus aureus
    • Rozgonyi, F., Biacs, P., Szitha, K., and Kiss, J. (1981) Effect of methicillin on the fatty acid composition of phospholipids in methicillin sensitive Staphylococcus aureus. Acta Microbiol. Acad. Sci. Hung. 28, 97-110.
    • (1981) Acta Microbiol. Acad. Sci. Hung. , vol.28 , pp. 97-110
    • Rozgonyi, F.1    Biacs, P.2    Szitha, K.3    Kiss, J.4
  • 86
    • 25144512582 scopus 로고    scopus 로고
    • Beta-lactam antibiotic resistance: A current structural perspective
    • Wilke, M. S., Lovering, A. L., and Strynadka, N. C. (2005) Beta-lactam antibiotic resistance: a current structural perspective. Curr. Opin. Microbiol. 8, 525-533.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 525-533
    • Wilke, M.S.1    Lovering, A.L.2    Strynadka, N.C.3
  • 87
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: Multiple enzymes with multiple functions
    • Smith, T. J., Blackman, S. A., and Foster, S. J. (2000) Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology 146 (Part 2), 249-262.
    • (2000) Microbiology , vol.146 , Issue.PART 2 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 89
    • 0037306656 scopus 로고    scopus 로고
    • Genetic analysis of a pHregulated operon from Rhizobium tropici CIAT899 involved in acid tolerance and nodulation competitiveness
    • Vinuesa, P., Neumann-Silkow, F., Pacios-Bras, C., Spaink, H. P., Martinez-Romero, E., and Werner, D. (2003) Genetic analysis of a pHregulated operon from Rhizobium tropici CIAT899 involved in acid tolerance and nodulation competitiveness. Mol. Plant Microbe Interact. 16, 159-168.
    • (2003) Mol. Plant Microbe Interact. , vol.16 , pp. 159-168
    • Vinuesa, P.1    Neumann-Silkow, F.2    Pacios-Bras, C.3    Spaink, H.P.4    Martinez-Romero, E.5    Werner, D.6
  • 90
    • 33749589117 scopus 로고    scopus 로고
    • The Sinorhizobium medicae WSM419 lpiA gene is transcriptionally activated by FsrR and required to enhance survival in lethal acid conditions
    • Reeve, W. G., Brau, L., Castelli, J., Garau, G., Sohlenkamp, C., Geiger, O., Dilworth, M. J., Glenn, A. R., Howieson, J. G., and Tiwari, R. P. (2006) The Sinorhizobium medicae WSM419 lpiA gene is transcriptionally activated by FsrR and required to enhance survival in lethal acid conditions. Microbiology 152, 3049-3059.
    • (2006) Microbiology , vol.152 , pp. 3049-3059
    • Reeve, W.G.1    Brau, L.2    Castelli, J.3    Garau, G.4    Sohlenkamp, C.5    Geiger, O.6    Dilworth, M.J.7    Glenn, A.R.8    Howieson, J.G.9    Tiwari, R.P.10
  • 91
    • 0043017532 scopus 로고
    • Metabolism of phosphatidylglycerol and lysyl phosphatidylglycerol in Staphylococcus aureus
    • Gould, R. M. and Lennarz, W. J. (1970) Metabolism of phosphatidylglycerol and lysyl phosphatidylglycerol in Staphylococcus aureus. J. Bacteriol. 104, 1135-1144.
    • (1970) J. Bacteriol. , vol.104 , pp. 1135-1144
    • Gould, R.M.1    Lennarz, W.J.2
  • 92
    • 0020093420 scopus 로고
    • Lactate acid inhibition of Salmonella typhimurium in yogurt
    • Rubin, H. E., Nerad, T., and Vaughan, F. (1982) Lactate acid inhibition of Salmonella typhimurium in yogurt. J. Dairy Sci. 65, 197-203.
    • (1982) J. Dairy Sci. , vol.65 , pp. 197-203
    • Rubin, H.E.1    Nerad, T.2    Vaughan, F.3
  • 93
    • 0037218495 scopus 로고    scopus 로고
    • MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing
    • Kristian, S. A., Durr, M., Van Strijp, J. A., Neumeister, B., and Peschel, A. (2003) MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing. Infect. Immun. 71, 546-549.
    • (2003) Infect. Immun. , vol.71 , pp. 546-549
    • Kristian, S.A.1    Durr, M.2    Van Strijp, J.A.3    Neumeister, B.4    Peschel, A.5
  • 94
    • 33646851752 scopus 로고    scopus 로고
    • Pushing the envelope: Extracytoplasmic stress responses in bacterial pathogens
    • Rowley, G., Spector, M., Kormanec, J., and Roberts, M. (2006) Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens. Nat. Rev. Microbiol. 4, 383-394.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 383-394
    • Rowley, G.1    Spector, M.2    Kormanec, J.3    Roberts, M.4
  • 95
    • 37349034233 scopus 로고    scopus 로고
    • Cell envelope stress response in gram-positive bacteria
    • Jordan, S., Hutchings, M. I., and Mascher, T. (2008) Cell envelope stress response in gram-positive bacteria. FEMS Microbiol. Rev. 32, 107-146.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 107-146
    • Jordan, S.1    Hutchings, M.I.2    Mascher, T.3
  • 96
    • 0014545399 scopus 로고
    • Bacteria-shaped gymnoplasts (protoplasts) of Bacillus subtilis
    • van Iterson, W. and den Kamp, J. A. (1969) Bacteria-shaped gymnoplasts (protoplasts) of Bacillus subtilis. J. Bacteriol. 99, 304-315.
    • (1969) J. Bacteriol. , vol.99 , pp. 304-315
    • Van Iterson, W.1    Den Kamp, J.A.2
  • 98
    • 0018881860 scopus 로고
    • Effect of methicillin on the phospholipid content of methicillin sensitive Staphylococcus aureus
    • Rozgonyi, F., Kiss, J., Jekel, P., and Vaczi, L. (1980) Effect of methicillin on the phospholipid content of methicillin sensitive Staphylococcus aureus. Acta Microbiol. Acad. Sci. Hung. 27, 31-40.
    • (1980) Acta Microbiol. Acad. Sci. Hung. , vol.27 , pp. 31-40
    • Rozgonyi, F.1    Kiss, J.2    Jekel, P.3    Vaczi, L.4
  • 99
    • 36148999436 scopus 로고    scopus 로고
    • The antimicrobial peptide-sensing system aps of Staphylococcus aureus
    • Li, M., Cha, D. J., Lai, Y., Villaruz, A. E., Sturdevant, D. E., and Otto, M. (2007) The antimicrobial peptide-sensing system aps of Staphylococcus aureus. Mol. Microbiol. 66, 1136-1147.
    • (2007) Mol. Microbiol. , vol.66 , pp. 1136-1147
    • Li, M.1    Cha, D.J.2    Lai, Y.3    Villaruz, A.E.4    Sturdevant, D.E.5    Otto, M.6
  • 101
    • 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
    • Meehl, M., Herbert, S., Gotz, F., and Cheung, A. (2007) Interaction of the GraRS two-component system with the VraFG ABC transporter to support vancomycin-intermediate resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 51, 2679-2689.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2679-2689
    • Meehl, M.1    Herbert, S.2    Gotz, F.3    Cheung, A.4
  • 102
    • 67349119801 scopus 로고    scopus 로고
    • Native graS mutation supports the susceptibility of Staphylococcus aureus strain SG511 to antimicrobial peptides
    • Sass, P. and Bierbaum, G. (2009) Native graS mutation supports the susceptibility of Staphylococcus aureus strain SG511 to antimicrobial peptides. Int. J. Med. Microbiol. 299, 313-322.
    • (2009) Int. J. Med. Microbiol. , vol.299 , pp. 313-322
    • Sass, P.1    Bierbaum, G.2
  • 103
    • 34547629994 scopus 로고    scopus 로고
    • Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci
    • Herbert, S., Bera, A., Nerz, C., Kraus, D., Peschel, A., Goerke, C., Meehl, M., Cheung, A., and Gotz, F. (2007) Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci. PLoS Pathog. 3, 981-994.
    • (2007) PLoS Pathog. , vol.3 , pp. 981-994
    • Herbert, S.1    Bera, A.2    Nerz, C.3    Kraus, D.4    Peschel, A.5    Goerke, C.6    Meehl, M.7    Cheung, A.8    Gotz, F.9
  • 104
    • 46249116492 scopus 로고    scopus 로고
    • The GraRS regulatory system controls Staphylococcus aureus susceptibility to antimicrobial host defenses
    • Kraus, D., Herbert, S., Kristian, S. A., Khosravi, A., Nizet, V., Gotz, F., and Peschel, A. (2008) The GraRS regulatory system controls Staphylococcus aureus susceptibility to antimicrobial host defenses. BMC Microbiol. 8, 85-89.
    • (2008) BMC Microbiol. , vol.8 , pp. 85-89
    • Kraus, D.1    Herbert, S.2    Kristian, S.A.3    Khosravi, A.4    Nizet, V.5    Gotz, F.6    Peschel, A.7
  • 105
    • 0037031594 scopus 로고    scopus 로고
    • An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes
    • Johansson, J., Mandin, P., Renzoni, A., Chiaruttini, C., Springer, M., and Cossart, P. (2002) An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes. Cell 110, 551-561.
    • (2002) Cell , vol.110 , pp. 551-561
    • Johansson, J.1    Mandin, P.2    Renzoni, A.3    Chiaruttini, C.4    Springer, M.5    Cossart, P.6
  • 107
    • 0028870094 scopus 로고
    • The vanZ gene of Tn1546 from Enterococcus faecium BM4147 confers resistance to teicoplanin
    • Arthur, M., Depardieu, F., Molinas, C., Reynolds, P., and Courvalin, P. (1995) The vanZ gene of Tn1546 from Enterococcus faecium BM4147 confers resistance to teicoplanin. Gene 154, 87-92.
    • (1995) Gene , vol.154 , pp. 87-92
    • Arthur, M.1    Depardieu, F.2    Molinas, C.3    Reynolds, P.4    Courvalin, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.