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Volumn 8, Issue 10, 2013, Pages

Critical Role of a Ferritin-Like Protein in the Control of Listeria monocytogenes Cell Envelope Structure and Stability under β-lactam Pressure

Author keywords

[No Author keywords available]

Indexed keywords

AUTOLYSIN; BETA LACTAM ANTIBIOTIC; FERRITIN; PENICILLIN G; TEICHOIC ACID;

EID: 84886246869     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0077808     Document Type: Article
Times cited : (8)

References (81)
  • 1
    • 0031037124 scopus 로고    scopus 로고
    • The pathogenicity of Listeria monocytogenes: a public health perspective
    • McLaughlin J, (1997) The pathogenicity of Listeria monocytogenes: a public health perspective. Rev Med Bacteriol 8: 1-14.
    • (1997) Rev Med Bacteriol , vol.8 , pp. 1-14
    • McLaughlin, J.1
  • 4
    • 0037376145 scopus 로고    scopus 로고
    • Listeriosis: therapeutic options
    • Hof H, (2003) Listeriosis: therapeutic options. FEMS Immunol Med Microbiol 35: 203-205.
    • (2003) FEMS Immunol Med Microbiol , vol.35 , pp. 203-205
    • Hof, H.1
  • 5
    • 0031963480 scopus 로고    scopus 로고
    • The role of autolysins during vegetative growth of Bacillus subtilis 168
    • Blackman SA, Smith TJ, Foster SJ, (1998) The role of autolysins during vegetative growth of Bacillus subtilis 168. Microbiology 144: 73-82.
    • (1998) Microbiology , vol.144 , pp. 73-82
    • Blackman, S.A.1    Smith, T.J.2    Foster, S.J.3
  • 6
    • 0000544892 scopus 로고
    • Microbial murein (peptidoglycan) hydrolases
    • In: Ghuysen J-M, Hakenbeck R (eds)
    • Shockman GD, Höltje J-V (1994) Microbial murein (peptidoglycan) hydrolases. In: Ghuysen J-M, Hakenbeck R (eds) Bacterial Cell Wall pp. 131-144.
    • (1994) Bacterial Cell Wall , pp. 131-144
    • Shockman, G.D.1    Höltje, J.-V.2
  • 7
    • 0014941489 scopus 로고
    • Multiple antibiotic resistance in a bacterium with suppressed autolytic system
    • Tomasz A, Albino A, Zanati E, (1970) Multiple antibiotic resistance in a bacterium with suppressed autolytic system. Nature 227: 138-140.
    • (1970) Nature , vol.227 , pp. 138-140
    • Tomasz, A.1    Albino, A.2    Zanati, E.3
  • 8
    • 0018338932 scopus 로고
    • The mechanism of the irreversible antimicrobial effects of penicillins: how the beta-lactam antibiotics kill and lyse bacteria
    • Tomasz A, (1979) The mechanism of the irreversible antimicrobial effects of penicillins: how the beta-lactam antibiotics kill and lyse bacteria. Annu Rev Microbiol 33: 113-137.
    • (1979) Annu Rev Microbiol , vol.33 , pp. 113-137
    • Tomasz, A.1
  • 9
    • 0034812451 scopus 로고    scopus 로고
    • Autolysis control hypotheses for tolerance to wall antibiotics
    • Koch AL, (2001) Autolysis control hypotheses for tolerance to wall antibiotics. Antimicrob Agents Chemother 45: 2671-2675.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 2671-2675
    • Koch, A.L.1
  • 10
    • 0026690127 scopus 로고
    • Structural and functional properties of the p60 proteins from different Listeria species
    • Bubert A, Kuhn M, Goebel W, Kohler S, (1992) Structural and functional properties of the p60 proteins from different Listeria species. J Bacteriol 174: 8166-8171.
    • (1992) J Bacteriol , vol.174 , pp. 8166-8171
    • Bubert, A.1    Kuhn, M.2    Goebel, W.3    Kohler, S.4
  • 11
    • 0031782074 scopus 로고    scopus 로고
    • Molecular characterization of an autolytic amidase of Listeria monocytogenes EGD
    • McLaughlan AM, Foster SJ, (1998) Molecular characterization of an autolytic amidase of Listeria monocytogenes EGD. Microbiol 144: 1359-1367.
    • (1998) Microbiol , vol.144 , pp. 1359-1367
    • McLaughlan, A.M.1    Foster, S.J.2
  • 12
    • 0033966330 scopus 로고    scopus 로고
    • P45, an extracellular 45 kDa protein of Listeria monocytogenes with similarity to protein p60 and exhibiting murein lytic activity
    • Schubert K, Bichlmaier AM, Mager E, Wolff K, Ruhland G, et al. (2000) P45, an extracellular 45 kDa protein of Listeria monocytogenes with similarity to protein p60 and exhibiting murein lytic activity. Arch Microbiol 173: 21-28.
    • (2000) Arch Microbiol , vol.173 , pp. 21-28
    • Schubert, K.1    Bichlmaier, A.M.2    Mager, E.3    Wolff, K.4    Ruhland, G.5
  • 13
    • 0344393481 scopus 로고    scopus 로고
    • Identification and characterization of a murein hydrolase, MurA, of Listeria monocytogenes, a muramidase needed for cell separation
    • Carroll SA, Hain T, Technow U, Darji A, Pashalidis P, et al. (2003) Identification and characterization of a murein hydrolase, MurA, of Listeria monocytogenes, a muramidase needed for cell separation. J Bacteriol 185: 6801-6808.
    • (2003) J Bacteriol , vol.185 , pp. 6801-6808
    • Carroll, S.A.1    Hain, T.2    Technow, U.3    Darji, A.4    Pashalidis, P.5
  • 14
    • 1642442774 scopus 로고    scopus 로고
    • Auto, a surface associated autolysin of Listeria monocytogenes required for entry into eukaryotic cells and virulence
    • Cabanes D, Dehoux P, Dussurget O, Frangeul L, Cossar P, (2004) Auto, a surface associated autolysin of Listeria monocytogenes required for entry into eukaryotic cells and virulence. Mol Microbiol 51: 1601-1614.
    • (2004) Mol Microbiol , vol.51 , pp. 1601-1614
    • Cabanes, D.1    Dehoux, P.2    Dussurget, O.3    Frangeul, L.4    Cossar, P.5
  • 15
    • 0038104676 scopus 로고    scopus 로고
    • Deletion of the gene encoding p60 in Listeria monocytogenes leads to abnormal cell division and loss of actin-based motility
    • Pilgrim V, Kolb-Maurer A, Gentschev L, Goebel W, Kuhn M, (2003) Deletion of the gene encoding p60 in Listeria monocytogenes leads to abnormal cell division and loss of actin-based motility. Infect Immun 71: 3473-3484.
    • (2003) Infect Immun , vol.71 , pp. 3473-3484
    • Pilgrim, V.1    Kolb-Maurer, A.2    Gentschev, L.3    Goebel, W.4    Kuhn, M.5
  • 16
    • 40849104947 scopus 로고    scopus 로고
    • Molecular control of bacterial death and lysis
    • Rice KC, Bayles KW, (2008) Molecular control of bacterial death and lysis. Microbiol Mol Biol Rev 72: 85-109.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 85-109
    • Rice, K.C.1    Bayles, K.W.2
  • 17
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria
    • Neuhaus FC, Baddiley J, (2003) A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. Microbiol Mol Biol Rev 67: 686-723.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 18
    • 40949089662 scopus 로고    scopus 로고
    • Teichoic acids and related cell wall glycopolymers in Gram-positive physiology and host interactions
    • Weidenmaier C, Peschel A, (2008) Teichoic acids and related cell wall glycopolymers in Gram-positive physiology and host interactions. Nat Rev Microbiol 6: 276-287.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 276-287
    • Weidenmaier, C.1    Peschel, A.2
  • 19
    • 0036192372 scopus 로고    scopus 로고
    • Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes
    • Abachin E, Poyart C, Pellegrini E, Milohanic E, Fiedler F, et al. (2002) Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes. Mol Microbiol 43: 1-14.
    • (2002) Mol Microbiol , vol.43 , pp. 1-14
    • Abachin, E.1    Poyart, C.2    Pellegrini, E.3    Milohanic, E.4    Fiedler, F.5
  • 20
    • 84869861799 scopus 로고    scopus 로고
    • Identification of a ferritin-like protein of Listeria monocytogenes as a mediator of β-lactam tolerance and innate resistance to cephalosporins
    • Krawczyk-Balska A, Marchlewicz J, Dudek D, Wasiak K, Samluk A, (2012) Identification of a ferritin-like protein of Listeria monocytogenes as a mediator of β-lactam tolerance and innate resistance to cephalosporins. BMC Microbiol 12: 278.
    • (2012) BMC Microbiol , vol.12 , pp. 278
    • Krawczyk-Balska, A.1    Marchlewicz, J.2    Dudek, D.3    Wasiak, K.4    Samluk, A.5
  • 21
    • 75849150278 scopus 로고    scopus 로고
    • Dps-like proteins: structural and functional insights into a versatile protein family
    • Haikarainen T, Papageorgiou AC, (2010) Dps-like proteins: structural and functional insights into a versatile protein family. Cell Mol Life Sci 67: 341-351.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 341-351
    • Haikarainen, T.1    Papageorgiou, A.C.2
  • 22
    • 17144402211 scopus 로고    scopus 로고
    • The socalled Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties
    • Su M, Cavallo S, Stefanini S, Chiancone E, Chasteen ND, (2005) The socalled Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties. Biochemistry 44: 5572-5578.
    • (2005) Biochemistry , vol.44 , pp. 5572-5578
    • Su, M.1    Cavallo, S.2    Stefanini, S.3    Chiancone, E.4    Chasteen, N.D.5
  • 23
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells: A ferritin-like DNA-binding protein of Escherichia coli
    • Zhao G, Ceci P, Ilari A, Giangiacomo L, Laue TM, et al. (2002) Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells: A ferritin-like DNA-binding protein of Escherichia coli. J Biol Chemistry 277: 27689-27696.
    • (2002) J Biol Chemistry , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5
  • 24
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P, (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275: 161-203.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 25
    • 0031763106 scopus 로고    scopus 로고
    • Iron storage in bacteria
    • Andrews SC, (1998) Iron storage in bacteria. Adv Microb Physiol 40: 281-351.
    • (1998) Adv Microb Physiol , vol.40 , pp. 281-351
    • Andrews, S.C.1
  • 26
    • 33846972315 scopus 로고    scopus 로고
    • The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence
    • Velayudhan J, Castor M, Richardson A, Main-Hester KL, Fang FC, (2007) The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence. Mol Microbiol 63: 1495-1507.
    • (2007) Mol Microbiol , vol.63 , pp. 1495-1507
    • Velayudhan, J.1    Castor, M.2    Richardson, A.3    Main-Hester, K.L.4    Fang, F.C.5
  • 27
    • 0037309086 scopus 로고    scopus 로고
    • The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni
    • Ishikawa T, Mizunoe Y, Kawabata S, Takade A, Harada M, et al. (2003) The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. J Bacteriol 185: 1010-1017.
    • (2003) J Bacteriol , vol.185 , pp. 1010-1017
    • Ishikawa, T.1    Mizunoe, Y.2    Kawabata, S.3    Takade, A.4    Harada, M.5
  • 28
    • 0037371197 scopus 로고    scopus 로고
    • Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis
    • Ueshima J, Shoji M, Ratnayake DB, Abe K, Yoshida S, et al. (2003) Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis. Infect Immun 71: 1170-1178.
    • (2003) Infect Immun , vol.71 , pp. 1170-1178
    • Ueshima, J.1    Shoji, M.2    Ratnayake, D.B.3    Abe, K.4    Yoshida, S.5
  • 29
    • 0027218065 scopus 로고
    • Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions
    • Chen L, James LP, Helmann JD, (1993) Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions. J Bacteriol 175: 5428-5437.
    • (1993) J Bacteriol , vol.175 , pp. 5428-5437
    • Chen, L.1    James, L.P.2    Helmann, J.D.3
  • 30
    • 33748878031 scopus 로고    scopus 로고
    • Paired Bacillus anthracis Dps (Mini-ferritin) have different reactivities with peroxide
    • Liu X, Kim K, Leighton T, Theil EC, (2006) Paired Bacillus anthracis Dps (Mini-ferritin) have different reactivities with peroxide. J Biol Chem 281: 27827-27835.
    • (2006) J Biol Chem , vol.281 , pp. 27827-27835
    • Liu, X.1    Kim, K.2    Leighton, T.3    Theil, E.C.4
  • 32
    • 15844374760 scopus 로고    scopus 로고
    • The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells
    • Olsen KN, Larsen MH, Gahan CG, Kallipolitis B, Wolf XA, et al. (2005) The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells. Microbiology 151: 925-933.
    • (2005) Microbiology , vol.151 , pp. 925-933
    • Olsen, K.N.1    Larsen, M.H.2    Gahan, C.G.3    Kallipolitis, B.4    Wolf, X.A.5
  • 33
    • 40649086144 scopus 로고    scopus 로고
    • Transcription of the Listeria monocytogenes fri gene is growth-phase dependent and is repressed directly by Fur, the ferric uptake regulator
    • Fiorini F, Stefanini S, Valenti P, Chiancone E, De Biase D, (2008) Transcription of the Listeria monocytogenes fri gene is growth-phase dependent and is repressed directly by Fur, the ferric uptake regulator. Gene 410: 113-121.
    • (2008) Gene , vol.410 , pp. 113-121
    • Fiorini, F.1    Stefanini, S.2    Valenti, P.3    Chiancone, E.4    De Biase, D.5
  • 34
    • 29144438143 scopus 로고    scopus 로고
    • Listeria monocytogenes PerR mutants display a small-colony phenotype, increased sensitivity to hydrogen peroxide, and significantly reduced murine virulence
    • Rea RB, Hill C, Gahan CGM, (2005) Listeria monocytogenes PerR mutants display a small-colony phenotype, increased sensitivity to hydrogen peroxide, and significantly reduced murine virulence. Appl Environ Microbiol 71: 8314-8322.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8314-8322
    • Rea, R.B.1    Hill, C.2    Gahan, C.G.M.3
  • 35
    • 0034284246 scopus 로고    scopus 로고
    • The main cold shock protein of Listeria monocytogenes belongs to the family of ferritin-like proteins
    • Hebraud M, Guzzo J, (2000) The main cold shock protein of Listeria monocytogenes belongs to the family of ferritin-like proteins. FEMS Microbiol Lett 190: 29-34.
    • (2000) FEMS Microbiol Lett , vol.190 , pp. 29-34
    • Hebraud, M.1    Guzzo, J.2
  • 36
    • 0037151781 scopus 로고    scopus 로고
    • The expression of the dodecameric ferritin in Listeria spp. is induced by iron limitation and stationary growth phase
    • Polidoro M, De Biase D, Montagnini B, Guarrera L, Cavallo S, et al. (2002) The expression of the dodecameric ferritin in Listeria spp. is induced by iron limitation and stationary growth phase. Gene 296: 121-128.
    • (2002) Gene , vol.296 , pp. 121-128
    • Polidoro, M.1    De Biase, D.2    Montagnini, B.3    Guarrera, L.4    Cavallo, S.5
  • 37
    • 23944523843 scopus 로고    scopus 로고
    • Listeria monocytogenes ferritin protects against multiple stresses and is required for virulence
    • Dussurget O, Dumas E, Archambaud C, Chafsey I, Chambon C, et al. (2005) Listeria monocytogenes ferritin protects against multiple stresses and is required for virulence. FEMS Microbiology Letters 250: 253-261.
    • (2005) FEMS Microbiology Letters , vol.250 , pp. 253-261
    • Dussurget, O.1    Dumas, E.2    Archambaud, C.3    Chafsey, I.4    Chambon, C.5
  • 38
    • 33645820010 scopus 로고    scopus 로고
    • The ferritin-like protein Frm is a target for the humoral immune response to Listeria monocytogenes genes and is required for efficient bacterial survival
    • Mohamed W, Darji A, Domann A, Chiancone E, Chakraborty T, (2006) The ferritin-like protein Frm is a target for the humoral immune response to Listeria monocytogenes genes and is required for efficient bacterial survival. Mol Genet Genomics 275: 344-353.
    • (2006) Mol Genet Genomics , vol.275 , pp. 344-353
    • Mohamed, W.1    Darji, A.2    Domann, A.3    Chiancone, E.4    Chakraborty, T.5
  • 41
    • 33748783782 scopus 로고    scopus 로고
    • Identification of an essential gene of Listeria monocytogenes involved in teichoic acid biogenesis
    • Dubail I, Bigot A, Lazarevic V, Soldo B, Euphrasie D, et al. (2006) Identification of an essential gene of Listeria monocytogenes involved in teichoic acid biogenesis. J Bacteriol 188: 6580-6591.
    • (2006) J Bacteriol , vol.188 , pp. 6580-6591
    • Dubail, I.1    Bigot, A.2    Lazarevic, V.3    Soldo, B.4    Euphrasie, D.5
  • 42
    • 84862732488 scopus 로고    scopus 로고
    • N-acetylglucosamine-6-phosphate deacetylase (NagA) of Listeria monocytogenes EGD, an essential enzyme for the metabolism and recycling of amino sugars
    • Popowska M, Osińska M, Rzeczkowska M, (2012) N-acetylglucosamine-6-phosphate deacetylase (NagA) of Listeria monocytogenes EGD, an essential enzyme for the metabolism and recycling of amino sugars. Arch Microbiol 194: 255-268.
    • (2012) Arch Microbiol , vol.194 , pp. 255-268
    • Popowska, M.1    Osińska, M.2    Rzeczkowska, M.3
  • 43
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner B, (1988) Separation and quantification of muropeptides with high-performance liquid chromatography. Anal Biochem 172: 451-464.
    • (1988) Anal Biochem , vol.172 , pp. 451-464
    • Glauner, B.1
  • 44
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • Chen PS, (1956) Microdetermination of phosphorus. Anal Chem 18: 1756-1758.
    • (1956) Anal Chem , vol.18 , pp. 1756-1758
    • Chen, P.S.1
  • 45
    • 0031573015 scopus 로고    scopus 로고
    • A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to β-galactosidase in Gram-positive bacteria
    • Poyart C, Trieu-Cuot P, (1997) A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to β-galactosidase in Gram-positive bacteria. FEMS Microbiol Lett 156: 193-198.
    • (1997) FEMS Microbiol Lett , vol.156 , pp. 193-198
    • Poyart, C.1    Trieu-Cuot, P.2
  • 46
    • 0025146736 scopus 로고
    • High efficiency transformation of Listeria monocytogenes by electroporation of penicillin-treated cells
    • Park SF, Stewart GS, (1990) High efficiency transformation of Listeria monocytogenes by electroporation of penicillin-treated cells. Gene 94: 129-132.
    • (1990) Gene , vol.94 , pp. 129-132
    • Park, S.F.1    Stewart, G.S.2
  • 47
    • 0242385535 scopus 로고    scopus 로고
    • CesRK, a two-component signal transduction system in Listeria monocytogenes, responds to the presence of cell wall-acting antibiotics and affects β-lactam resistance
    • Kallipolitis BH, Ingmer H, Gahan CG, Hill C, Søgaard-Andersen L, (2003) CesRK, a two-component signal transduction system in Listeria monocytogenes, responds to the presence of cell wall-acting antibiotics and affects β-lactam resistance. Antimicrob Agents Chemother 47: 3421-3429.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3421-3429
    • Kallipolitis, B.H.1    Ingmer, H.2    Gahan, C.G.3    Hill, C.4    Søgaard-Andersen, L.5
  • 48
    • 0003785155 scopus 로고
    • Cold Spring HarborN.Y.: Cold Spring Harbor Laboratory Press
    • Miller JH (1972) Experiments in molecular genetics. Cold Spring HarborN.Y.: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 49
    • 13444278970 scopus 로고    scopus 로고
    • The svpA-srtB locus of Listeria monocytogenes: fur-mediated iron regulation and effect on virulence
    • Newton SM, Klebba PE, Raynaud C, Shao Y, Jiang X, et al. (2005) The svpA-srtB locus of Listeria monocytogenes: fur-mediated iron regulation and effect on virulence. Mol Microbiol 55: 927-940.
    • (2005) Mol Microbiol , vol.55 , pp. 927-940
    • Newton, S.M.1    Klebba, P.E.2    Raynaud, C.3    Shao, Y.4    Jiang, X.5
  • 50
    • 33645053499 scopus 로고    scopus 로고
    • Associated roles of hemolysin and p60 protein for the intracellular growth of Bacillus subtilis
    • Wiśniewski J, Krawczyk-Balska A, Bielecki J, (2006) Associated roles of hemolysin and p60 protein for the intracellular growth of Bacillus subtilis. FEMS Immunol Med Microbiol 46: 330-339.
    • (2006) FEMS Immunol Med Microbiol , vol.46 , pp. 330-339
    • Wiśniewski, J.1    Krawczyk-Balska, A.2    Bielecki, J.3
  • 51
    • 34250773925 scopus 로고    scopus 로고
    • Listeria monocytogenes surface proteins: From genome predictions to function
    • Bierne H, Cossart P, (2007) Listeria monocytogenes surface proteins: From genome predictions to function. Microbiol Mol Biol Rev 71: 377-397.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 377-397
    • Bierne, H.1    Cossart, P.2
  • 52
    • 0026512822 scopus 로고
    • Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis
    • Foster SJ, (1992) Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis. J Bacteriol 174: 464-470.
    • (1992) J Bacteriol , vol.174 , pp. 464-470
    • Foster, S.J.1
  • 53
    • 84859788603 scopus 로고    scopus 로고
    • Re-evaluation of the significance of penicillin binding protein 3 in the susceptibility of Listeria monocytogenes to β-lactam antibiotics
    • Krawczyk-Balska A, Popowska M, Markiewicz Z, (2012) Re-evaluation of the significance of penicillin binding protein 3 in the susceptibility of Listeria monocytogenes to β-lactam antibiotics. BMC Microbiol 12: 57.
    • (2012) BMC Microbiol , vol.12 , pp. 57
    • Krawczyk-Balska, A.1    Popowska, M.2    Markiewicz, Z.3
  • 54
    • 25644433668 scopus 로고    scopus 로고
    • Listeria monocytogenes EGD lacking penicillin-binding protein 5 (PBP5) produces a thicker cell wall
    • Korsak D, Vollmer W, Markiewicz Z, (2005) Listeria monocytogenes EGD lacking penicillin-binding protein 5 (PBP5) produces a thicker cell wall. FEMS Microbiol Lett 251: 281-288.
    • (2005) FEMS Microbiol Lett , vol.251 , pp. 281-288
    • Korsak, D.1    Vollmer, W.2    Markiewicz, Z.3
  • 55
    • 33846526208 scopus 로고    scopus 로고
    • A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system
    • Boneca IG, Dussurget O, Cabanes D, Nahori MA, Sousa S, et al. (2007) A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system. Proc Natl Acad Sci USA 104: 997-1002.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 997-1002
    • Boneca, I.G.1    Dussurget, O.2    Cabanes, D.3    Nahori, M.A.4    Sousa, S.5
  • 56
    • 70849090947 scopus 로고    scopus 로고
    • Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis
    • Popowska M, Kusio M, Szymanska P, Markiewicz Z, (2009) Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis. J Microbiol Biotechnol 19: 932-945.
    • (2009) J Microbiol Biotechnol , vol.19 , pp. 932-945
    • Popowska, M.1    Kusio, M.2    Szymanska, P.3    Markiewicz, Z.4
  • 57
    • 33845941753 scopus 로고    scopus 로고
    • Influence of wall teichoic acid on lysozyme resistance in Staphylococcus aureus
    • Bera A, Biswas R, Herbert S, Kulauzovic E, Weidenmaier C, et al. (2007) Influence of wall teichoic acid on lysozyme resistance in Staphylococcus aureus. J Bacteriol 189: 280-283.
    • (2007) J Bacteriol , vol.189 , pp. 280-283
    • Bera, A.1    Biswas, R.2    Herbert, S.3    Kulauzovic, E.4    Weidenmaier, C.5
  • 58
    • 84879047022 scopus 로고    scopus 로고
    • Increased cell wall teichoic acid production and D-alanylation are common phenotypes among daptomycin-resistant methicillin-resistant Staphylococcus aureus (MRSA) clinical isolates
    • Bertsche U, Yang S, Kuehner D, Wanner S, Mishra NN, et al. (2013) Increased cell wall teichoic acid production and D-alanylation are common phenotypes among daptomycin-resistant methicillin-resistant Staphylococcus aureus (MRSA) clinical isolates. PLoS ONE 8(6): e67398.
    • (2013) PLoS ONE , vol.8 , Issue.6
    • Bertsche, U.1    Yang, S.2    Kuehner, D.3    Wanner, S.4    Mishra, N.N.5
  • 59
    • 28844489096 scopus 로고    scopus 로고
    • Simultaneous deficiency of both MurA and p60 proteins generates a rough phenotype in Listeria monocytogenes
    • Machata S, Hain T, Rohde M, Chakraborty T, (2005) Simultaneous deficiency of both MurA and p60 proteins generates a rough phenotype in Listeria monocytogenes. J Bacteriol 187: 8385-8394.
    • (2005) J Bacteriol , vol.187 , pp. 8385-8394
    • Machata, S.1    Hain, T.2    Rohde, M.3    Chakraborty, T.4
  • 60
    • 0036040839 scopus 로고    scopus 로고
    • Identification of a second Listeria secA gene associated with protein secretion and the rough phenotype
    • Lenz LL, Portnoy DA, (2002) Identification of a second Listeria secA gene associated with protein secretion and the rough phenotype. Mol Microbiol 45: 1043-1056.
    • (2002) Mol Microbiol , vol.45 , pp. 1043-1056
    • Lenz, L.L.1    Portnoy, D.A.2
  • 61
    • 0142091351 scopus 로고    scopus 로고
    • SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis
    • Lenz LL, Mohammadi S, Geissler A, Portnoy DA, (2003) SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis. Proc Natl Acad Sci USA 100: 12432-12437.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12432-12437
    • Lenz, L.L.1    Mohammadi, S.2    Geissler, A.3    Portnoy, D.A.4
  • 62
    • 84874580124 scopus 로고    scopus 로고
    • Exoproteomic analysis of the SecA2-dependent secretion in Listeria monocytogenes EGD-e
    • Renier S, Chambon C, Viala D, Chagnot C, Hébraud M, et al. (2013) Exoproteomic analysis of the SecA2-dependent secretion in Listeria monocytogenes EGD-e. J Proteomics 80: 183-195.
    • (2013) J Proteomics , vol.80 , pp. 183-195
    • Renier, S.1    Chambon, C.2    Viala, D.3    Chagnot, C.4    Hébraud, M.5
  • 63
    • 0030819057 scopus 로고    scopus 로고
    • The absence of D-alanine from lipoteichoic acid and wall teichoic acid alters surface charge, enhances autolysis and increases susceptibility to methicillin in Bacillus subtilis
    • Wecke J, Madela K, Fischer W, (1997) The absence of D-alanine from lipoteichoic acid and wall teichoic acid alters surface charge, enhances autolysis and increases susceptibility to methicillin in Bacillus subtilis. Microbiology 143: 2953-2960.
    • (1997) Microbiology , vol.143 , pp. 2953-2960
    • Wecke, J.1    Madela, K.2    Fischer, W.3
  • 64
    • 11144322172 scopus 로고    scopus 로고
    • Autolysis of Lactococcus lactis is increased upon D-alanine depletion of peptidoglycan and lipoteichoic acids
    • Steen A, Palumbo E, Deghorain M, Cocconcelli PS, Delcour J, et al. (2005) Autolysis of Lactococcus lactis is increased upon D-alanine depletion of peptidoglycan and lipoteichoic acids. J Bacteriol 187: 114-124.
    • (2005) J Bacteriol , vol.187 , pp. 114-124
    • Steen, A.1    Palumbo, E.2    Deghorain, M.3    Cocconcelli, P.S.4    Delcour, J.5
  • 65
    • 33646574610 scopus 로고    scopus 로고
    • D-Alanyl ester depletion of teichoic acids in Lactobacillus plantarum results in a major modification of lipoteichoic acid composition and cell wall perforations at the septum mediated by the Acm2 autolysin
    • Hartung T, Morath S, Hols P, (2006) D-Alanyl ester depletion of teichoic acids in Lactobacillus plantarum results in a major modification of lipoteichoic acid composition and cell wall perforations at the septum mediated by the Acm2 autolysin. J Bacteriol 188: 3709-3715.
    • (2006) J Bacteriol , vol.188 , pp. 3709-3715
    • Hartung, T.1    Morath, S.2    Hols, P.3
  • 66
    • 67649268395 scopus 로고    scopus 로고
    • The Listeria transcriptional landscape from saprophytism to virulence
    • Toledo-Arana A, Dussurget O, Nikitas G, Sesto N, Guet-Revillet H, et al. (2009) The Listeria transcriptional landscape from saprophytism to virulence. Nature 459: 950-956.
    • (2009) Nature , vol.459 , pp. 950-956
    • Toledo-Arana, A.1    Dussurget, O.2    Nikitas, G.3    Sesto, N.4    Guet-Revillet, H.5
  • 67
    • 84865035715 scopus 로고    scopus 로고
    • Subcellular localization of extracytoplasmic proteins in monoderm bacteria: rational secretomics-based strategy for genomic and proteomic analyses
    • Renier S, Micheau P, Talon R, Hébraud M, Desvaux M, (2012) Subcellular localization of extracytoplasmic proteins in monoderm bacteria: rational secretomics-based strategy for genomic and proteomic analyses. PLoS One 7: e42982.
    • (2012) PLoS One , vol.7
    • Renier, S.1    Micheau, P.2    Talon, R.3    Hébraud, M.4    Desvaux, M.5
  • 68
    • 77957352841 scopus 로고    scopus 로고
    • Comprehensive appraisal of the extracellular proteins from a monoderm bacterium: theoretical and empirical exoproteomes of Listeria monocytogenes EGD-e by secretomics
    • Desvaux M, Dumas E, Chafsey I, Chambon C, Hebraud M, (2010) Comprehensive appraisal of the extracellular proteins from a monoderm bacterium: theoretical and empirical exoproteomes of Listeria monocytogenes EGD-e by secretomics. J Proteome Res 9: 5076-5092.
    • (2010) J Proteome Res , vol.9 , pp. 5076-5092
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Chambon, C.4    Hebraud, M.5
  • 69
    • 21644461938 scopus 로고    scopus 로고
    • LaneSpector. a tool for membrane proteome profiling based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis/liquid chromatography-tandem mass spectrometry analysis: application to Listeria monocytogenes membrane proteins
    • Wehmhoner D, Dieterich G, Fischer E, Baumgartner M, Wehland J, et al. (2005) LaneSpector. a tool for membrane proteome profiling based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis/liquid chromatography-tandem mass spectrometry analysis: application to Listeria monocytogenes membrane proteins. Electrophoresis 26: 2450-2460.
    • (2005) Electrophoresis , vol.26 , pp. 2450-2460
    • Wehmhoner, D.1    Dieterich, G.2    Fischer, E.3    Baumgartner, M.4    Wehland, J.5
  • 70
    • 0024581874 scopus 로고
    • Identification of an extracellular protein of Listeria monocytogenes possibly involved in intracellular uptake by mammalian cells
    • Kuhn M, Goebel W, (1989) Identification of an extracellular protein of Listeria monocytogenes possibly involved in intracellular uptake by mammalian cells. Infect Immun 57: 55-61.
    • (1989) Infect Immun , vol.57 , pp. 55-61
    • Kuhn, M.1    Goebel, W.2
  • 71
    • 0021233596 scopus 로고
    • Attachment of pneumococcal autolysin to wall teichoic acids, an essential step in enzymatic wall degradation
    • Giudicelli S, Tomasz A, (1984) Attachment of pneumococcal autolysin to wall teichoic acids, an essential step in enzymatic wall degradation. J Bacteriol 158: 1188-1190.
    • (1984) J Bacteriol , vol.158 , pp. 1188-1190
    • Giudicelli, S.1    Tomasz, A.2
  • 72
    • 0023547233 scopus 로고
    • Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-l-alanine amidase
    • Bierbaum G, Sahl HG, (1987) Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-l-alanine amidase. J Bacteriol 169: 5452-5458.
    • (1987) J Bacteriol , vol.169 , pp. 5452-5458
    • Bierbaum, G.1    Sahl, H.G.2
  • 73
    • 0014935603 scopus 로고
    • Teichoic acids and membrane function in bacteria
    • Heptinstall S, Archibald AR, Baddiley J, (1970) Teichoic acids and membrane function in bacteria. Nature 225: 519-52.
    • (1970) Nature , vol.225 , pp. 519-552
    • Heptinstall, S.1    Archibald, A.R.2    Baddiley, J.3
  • 74
    • 84864267124 scopus 로고    scopus 로고
    • Proton-binding capacity of Staphylococcus aureus wall teichoic acid and its role in controlling autolysin activity
    • Biswas R, Martinez RE, Göhring N, Schlag M, Josten M, et al. (2012) Proton-binding capacity of Staphylococcus aureus wall teichoic acid and its role in controlling autolysin activity. PLoS ONE 7: e41415.
    • (2012) PLoS ONE , vol.7
    • Biswas, R.1    Martinez, R.E.2    Göhring, N.3    Schlag, M.4    Josten, M.5
  • 75
    • 0029775205 scopus 로고    scopus 로고
    • D-Alanine deprivation of Bacillus subtilis teichoic acids is without effect on cell growth and morphology but affects the autolytic activity
    • Wecke J, Perego M, Fischer W, (1996) D-Alanine deprivation of Bacillus subtilis teichoic acids is without effect on cell growth and morphology but affects the autolytic activity. Microb Drug Resist 2: 123-129.
    • (1996) Microb Drug Resist , vol.2 , pp. 123-129
    • Wecke, J.1    Perego, M.2    Fischer, W.3
  • 76
    • 0034282698 scopus 로고    scopus 로고
    • D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis
    • Hyyrylainen HL, Vitikainen M, Thwaite J, Wu H, Sarvas M, et al. (2000) D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis. J Biol Chem 275: 26696-26703.
    • (2000) J Biol Chem , vol.275 , pp. 26696-26703
    • Hyyrylainen, H.L.1    Vitikainen, M.2    Thwaite, J.3    Wu, H.4    Sarvas, M.5
  • 77
    • 84859939178 scopus 로고    scopus 로고
    • Protein transport across the cell wall of monoderm Gram-positive bacteria
    • Forster BM, Marquis H, (2012) Protein transport across the cell wall of monoderm Gram-positive bacteria. Mol Microbiol 84: 405-413.
    • (2012) Mol Microbiol , vol.84 , pp. 405-413
    • Forster, B.M.1    Marquis, H.2
  • 78
    • 33644944649 scopus 로고    scopus 로고
    • Tolerance of Listeria monocytogenes to cell envelope-acting antimicrobial agents is dependent on SigB
    • Begley M, Hill C, Ross RP, (2006) Tolerance of Listeria monocytogenes to cell envelope-acting antimicrobial agents is dependent on SigB. Appl Environ Microbiol 72: 2231-2234.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 2231-2234
    • Begley, M.1    Hill, C.2    Ross, R.P.3
  • 79
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski MA, Dwyer DJ, Hayete B, Lawrence CA, Collins JJ, (2007) A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130: 797-810.
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 80
    • 79951948791 scopus 로고    scopus 로고
    • The ferritin-like protein Dps protects Salmonella enterica serotype Enteritidis from the Fenton-mediated killing mechanism of bactericidal antibiotics
    • Calhoun LN, Kwon YM, (2011) The ferritin-like protein Dps protects Salmonella enterica serotype Enteritidis from the Fenton-mediated killing mechanism of bactericidal antibiotics. Int J Antimicrob Agents 37: 261-265.
    • (2011) Int J Antimicrob Agents , vol.37 , pp. 261-265
    • Calhoun, L.N.1    Kwon, Y.M.2
  • 81
    • 84867584201 scopus 로고    scopus 로고
    • A ferritin mutant of Mycobacterium tuberculosis is highly susceptible to killing by antibiotics and is unable to establish a chronic infection in mice
    • Pandey R, Rodriguez GM, (2012) A ferritin mutant of Mycobacterium tuberculosis is highly susceptible to killing by antibiotics and is unable to establish a chronic infection in mice. Infect Immun 80: 3650-3659.
    • (2012) Infect Immun , vol.80 , pp. 3650-3659
    • Pandey, R.1    Rodriguez, G.M.2


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