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Volumn 15, Issue 2, 2013, Pages 502-516

Insight into the composition of the intercellular matrix of Streptococcus pneumoniae biofilms

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL POLYSACCHARIDE; BACTERIAL PROTEIN; LYTC PROTEIN, STREPTOCOCCUS; N ACETYLMURAMOYLALANINE AMIDASE;

EID: 84873142364     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/j.1462-2920.2012.02853.x     Document Type: Article
Times cited : (49)

References (66)
  • 1
    • 0001610838 scopus 로고
    • Complete acid hydrolysis
    • Adams, G.A. (1965) Complete acid hydrolysis. Methods Carbohydr Chem 5: 269-276.
    • (1965) Methods Carbohydr Chem , vol.5 , pp. 269-276
    • Adams, G.A.1
  • 2
    • 33645052196 scopus 로고    scopus 로고
    • A characterization of DNA release in Pseudomonas aeruginosa cultures and biofilms
    • Allesen-Holm, M., Barken, K.B., Yang, L., Klausen, M., Webb, J.S., Kjelleberg, S., etal. (2006) A characterization of DNA release in Pseudomonas aeruginosa cultures and biofilms. Mol Microbiol 59: 1114-1128.
    • (2006) Mol Microbiol , vol.59 , pp. 1114-1128
    • Allesen-Holm, M.1    Barken, K.B.2    Yang, L.3    Klausen, M.4    Webb, J.S.5    Kjelleberg, S.6
  • 3
    • 67650634980 scopus 로고    scopus 로고
    • Characterization of structures in biofilms formed by a Pseudomonas fluorescens isolated from soil
    • Baum, M., Kainovic, A., O'Keeffe, T., Pandita, R., McDonald, K., Wu, S., and Webster, P. (2009) Characterization of structures in biofilms formed by a Pseudomonas fluorescens isolated from soil. BMC Microbiol 9: 103.
    • (2009) BMC Microbiol , vol.9 , pp. 103
    • Baum, M.1    Kainovic, A.2    O'Keeffe, T.3    Pandita, R.4    McDonald, K.5    Wu, S.6    Webster, P.7
  • 5
    • 64349095283 scopus 로고
    • Influence of lipoteichoic acid and choline on the autolytic enzyme activity of Streptococcus pneumoniae
    • Nombela, C. (ed.). Amsterdam, the Netherland: Elsevier Science Publishers B.V.
    • Briese, T., and Hakenbeck, R. (1984) Influence of lipoteichoic acid and choline on the autolytic enzyme activity of Streptococcus pneumoniae. In Microbial Cell Wall Synthesis and Autolysis. Nombela, C. (ed.). Amsterdam, the Netherland: Elsevier Science Publishers B.V., pp. 201-206.
    • (1984) Microbial Cell Wall Synthesis and Autolysis , pp. 201-206
    • Briese, T.1    Hakenbeck, R.2
  • 7
    • 78650883397 scopus 로고    scopus 로고
    • Prophage spontaneous activation promotes DNA release enhancing biofilm formation in Streptococcus pneumoniae
    • Carrolo, M., Frias, M.J., Pinto, F.R., Melo-Cristino, J., and Ramirez, M. (2010) Prophage spontaneous activation promotes DNA release enhancing biofilm formation in Streptococcus pneumoniae. PLoS ONE 5: e15678.
    • (2010) PLoS ONE , vol.5
    • Carrolo, M.1    Frias, M.J.2    Pinto, F.R.3    Melo-Cristino, J.4    Ramirez, M.5
  • 8
    • 79958171834 scopus 로고    scopus 로고
    • Unexpected and widespread connections between bacterial glycogen and trehalose metabolism
    • Chandra, G., Chater, K.F., and Bornemann, S. (2011) Unexpected and widespread connections between bacterial glycogen and trehalose metabolism. Microbiology 157: 1565-1572.
    • (2011) Microbiology , vol.157 , pp. 1565-1572
    • Chandra, G.1    Chater, K.F.2    Bornemann, S.3
  • 9
    • 33847129667 scopus 로고    scopus 로고
    • Cannibalism and fratricide: mechanisms and raisons d'être
    • Claverys, J.-P., and Håvarstein, L.S. (2007) Cannibalism and fratricide: mechanisms and raisons d'être. Nat Rev Microbiol 5: 219-229.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 219-229
    • Claverys, J.-P.1    Håvarstein, L.S.2
  • 11
    • 0036724742 scopus 로고    scopus 로고
    • Purification and polar localization of pneumococcal LytB, a putative endo-β-N-acetylglucosaminidase: the chain-dispersing murein hydrolase
    • De las Rivas, B., García, J.L., López, R., and García, P. (2002) Purification and polar localization of pneumococcal LytB, a putative endo-β-N-acetylglucosaminidase: the chain-dispersing murein hydrolase. J Bacteriol 184: 4988-5000.
    • (2002) J Bacteriol , vol.184 , pp. 4988-5000
    • De las Rivas, B.1    García, J.L.2    López, R.3    García, P.4
  • 12
    • 84873107993 scopus 로고    scopus 로고
    • Biofilm de Streptococcus pneumoniae: genética, composición y terapia. PhD Thesis. Madrid, Spain: Universidad Complutense de Madrid.
    • Domenech, M. (2012) Biofilm de Streptococcus pneumoniae: genética, composición y terapia. PhD Thesis. Madrid, Spain: Universidad Complutense de Madrid.
    • (2012)
    • Domenech, M.1
  • 13
    • 80051828499 scopus 로고    scopus 로고
    • In vitro destruction of Streptococcus pneumoniae biofilms with bacterial and phage peptidoglycan hydrolases
    • Domenech, M., García, E., and Moscoso, M. (2011) In vitro destruction of Streptococcus pneumoniae biofilms with bacterial and phage peptidoglycan hydrolases. Antimicrob Agents Chemother 55: 4144-4148.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 4144-4148
    • Domenech, M.1    García, E.2    Moscoso, M.3
  • 14
    • 84862018527 scopus 로고    scopus 로고
    • Biofilm formation in Streptococcus pneumoniae
    • Domenech, M., García, E., and Moscoso, M. (2012) Biofilm formation in Streptococcus pneumoniae. Microb Biotechnol 5: 455-465.
    • (2012) Microb Biotechnol , vol.5 , pp. 455-465
    • Domenech, M.1    García, E.2    Moscoso, M.3
  • 15
    • 79952085066 scopus 로고    scopus 로고
    • Extracellular DNA is abundant and important for microcolony strength in mixed microbial biofilms
    • Dominiak, D.M., Nielsen, J.L., and Nielsen, P.H. (2011) Extracellular DNA is abundant and important for microcolony strength in mixed microbial biofilms. Environ Microbiol 13: 710-721.
    • (2011) Environ Microbiol , vol.13 , pp. 710-721
    • Dominiak, D.M.1    Nielsen, J.L.2    Nielsen, P.H.3
  • 16
    • 4143132359 scopus 로고    scopus 로고
    • Model system for growing and quantifying Streptococcus pneumoniae biofilms in situ and in real time
    • Donlan, R.M., Piede, J.A., Heyes, C.D., Sanii, L., Murga, R., Edmonds, P., etal. (2004) Model system for growing and quantifying Streptococcus pneumoniae biofilms in situ and in real time. Appl Environ Microbiol 70: 4980-4988.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 4980-4988
    • Donlan, R.M.1    Piede, J.A.2    Heyes, C.D.3    Sanii, L.4    Murga, R.5    Edmonds, P.6
  • 17
    • 0011025527 scopus 로고
    • Interaction of pneumococcal S-14 polysaccharide with lectins from Ricinus communis, Triticum vulgaris, and bandeiraea simplicifolia
    • Ebisu, S., Lonngren, J., and Goldstein, I.J. (1977) Interaction of pneumococcal S-14 polysaccharide with lectins from Ricinus communis, Triticum vulgaris, and bandeiraea simplicifolia. Carbohydr Res 58: 187-191.
    • (1977) Carbohydr Res , vol.58 , pp. 187-191
    • Ebisu, S.1    Lonngren, J.2    Goldstein, I.J.3
  • 18
    • 69949170096 scopus 로고    scopus 로고
    • Fratricide in Streptococcus pneumoniae: contributions and role of the cell wall hydrolases CbpD, LytA and LytC
    • Eldholm, V., Johnsborg, O., Haugen, K., Ohnstad, H.S., and Håvarstein, L.S. (2009) Fratricide in Streptococcus pneumoniae: contributions and role of the cell wall hydrolases CbpD, LytA and LytC. Microbiology 155: 2223-2234.
    • (2009) Microbiology , vol.155 , pp. 2223-2234
    • Eldholm, V.1    Johnsborg, O.2    Haugen, K.3    Ohnstad, H.S.4    Håvarstein, L.S.5
  • 19
    • 77952163865 scopus 로고    scopus 로고
    • Pneumococcal CbpD is a murein hydrolase that requires a dual cell envelope binding specificity to kill target cells during fratricide
    • Eldholm, V., Johnsborg, O., Straume, D., Ohnstad, H.S., Berg, K.H., Hermoso, J.A., and Håvarstein, L.S. (2010) Pneumococcal CbpD is a murein hydrolase that requires a dual cell envelope binding specificity to kill target cells during fratricide. Mol Microbiol 76: 905-917.
    • (2010) Mol Microbiol , vol.76 , pp. 905-917
    • Eldholm, V.1    Johnsborg, O.2    Straume, D.3    Ohnstad, H.S.4    Berg, K.H.5    Hermoso, J.A.6    Håvarstein, L.S.7
  • 20
    • 84864416657 scopus 로고    scopus 로고
    • Multi-species biofilms: living with friendly neighbors
    • doi: 10.1111/j.1574-6976.2012.00325.x [Epub ahead of print].
    • Elias, S., and Banin, E. (2012) Multi-species biofilms: living with friendly neighbors. FEMS Microbiol Rev. doi: 10.1111/j.1574-6976.2012.00325.x [Epub ahead of print].
    • (2012) FEMS Microbiol Rev
    • Elias, S.1    Banin, E.2
  • 22
    • 77953381240 scopus 로고    scopus 로고
    • Extracellular DNA: a major proinflammatory component of Pseudomonas aeruginosa biofilms
    • Fuxman Bass, J.I., Russo, D.M., Gabelloni, M.L., Geffner, J.R., Giordano, M., Catalano, M., etal. (2011) Extracellular DNA: a major proinflammatory component of Pseudomonas aeruginosa biofilms. J Immunol 184: 6386-6395.
    • (2011) J Immunol , vol.184 , pp. 6386-6395
    • Fuxman Bass, J.I.1    Russo, D.M.2    Gabelloni, M.L.3    Geffner, J.R.4    Giordano, M.5    Catalano, M.6
  • 23
    • 0025037846 scopus 로고
    • Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
    • García, P., García, J.L., García, E., Sánchez-Puelles, J.M., and López, R. (1990) Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Gene 86: 81-88.
    • (1990) Gene , vol.86 , pp. 81-88
    • García, P.1    García, J.L.2    García, E.3    Sánchez-Puelles, J.M.4    López, R.5
  • 24
    • 17444442315 scopus 로고    scopus 로고
    • The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains
    • García, P., González, M.P., García, E., García, J.L., and López, R. (1999) The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains. Mol Microbiol 33: 128-138.
    • (1999) Mol Microbiol , vol.33 , pp. 128-138
    • García, P.1    González, M.P.2    García, E.3    García, J.L.4    López, R.5
  • 25
    • 64349102718 scopus 로고    scopus 로고
    • Versatility of choline metabolism and choline-binding proteins in Streptococcus pneumoniae and commensal streptococci
    • Hakenbeck, R., Madhour, A., Denapaite, D., and Brückner, R. (2009) Versatility of choline metabolism and choline-binding proteins in Streptococcus pneumoniae and commensal streptococci. FEMS Microbiol Rev 33: 572-586.
    • (2009) FEMS Microbiol Rev , vol.33 , pp. 572-586
    • Hakenbeck, R.1    Madhour, A.2    Denapaite, D.3    Brückner, R.4
  • 26
    • 57649129086 scopus 로고    scopus 로고
    • Characterization of biofilm matrix, degradation by DNase treatment and evidence of capsule downregulation in Streptococcus pneumoniae clinical isolates
    • Hall-Stoodley, L., Nistico, L., Sambanthamoorthy, K., Dice, B., Nguyen, D., Mershon, W.J., etal. (2008) Characterization of biofilm matrix, degradation by DNase treatment and evidence of capsule downregulation in Streptococcus pneumoniae clinical isolates. BMC Microbiol 8: 173.
    • (2008) BMC Microbiol , vol.8 , pp. 173
    • Hall-Stoodley, L.1    Nistico, L.2    Sambanthamoorthy, K.3    Dice, B.4    Nguyen, D.5    Mershon, W.J.6
  • 27
    • 0037408156 scopus 로고    scopus 로고
    • Calcofluor white: a review of its uses and applications in clinical mycology and parasitology
    • Harrington, B.J., and Hageage, G.J. (2003) Calcofluor white: a review of its uses and applications in clinical mycology and parasitology. Lab Med 34: 361-367.
    • (2003) Lab Med , vol.34 , pp. 361-367
    • Harrington, B.J.1    Hageage, G.J.2
  • 28
    • 33645081479 scopus 로고    scopus 로고
    • New insights into the pneumococcal fratricide: relationship to clumping and identification of a novel immunity factor
    • Håvarstein, L.S., Martin, B., Johnsborg, O., Granadel, C., and Claverys, J. (2006) New insights into the pneumococcal fratricide: relationship to clumping and identification of a novel immunity factor. Mol Microbiol 59: 1297-1037.
    • (2006) Mol Microbiol , vol.59 , pp. 1297-1037
    • Håvarstein, L.S.1    Martin, B.2    Johnsborg, O.3    Granadel, C.4    Claverys, J.5
  • 29
    • 59649117156 scopus 로고    scopus 로고
    • Staphylococcus aureus beta-toxin induces lung injury through syndecan-1
    • Hayashida, A., Bartlett, A.H., Foster, T.J., and Park, P.W. (2009) Staphylococcus aureus beta-toxin induces lung injury through syndecan-1. Am J Pathol 174: 509-518.
    • (2009) Am J Pathol , vol.174 , pp. 509-518
    • Hayashida, A.1    Bartlett, A.H.2    Foster, T.J.3    Park, P.W.4
  • 30
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • Henderson, B., and Martin, A. (2011) Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease. Infect Immun 79: 3476-3491.
    • (2011) Infect Immun , vol.79 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 31
    • 0038943721 scopus 로고
    • Lipoteichoic acid: a specific inhibitor of autolysin activity in pneumococcus
    • Höltje, J.V., and Tomasz, A. (1975) Lipoteichoic acid: a specific inhibitor of autolysin activity in pneumococcus. Proc Natl Acad Sci USA 72: 1690-1694.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 1690-1694
    • Höltje, J.V.1    Tomasz, A.2
  • 32
    • 77956276034 scopus 로고    scopus 로고
    • Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms
    • Huseby, M.J., Kruse, A.C., Digre, J., Kohler, P.L., Vocke, J.A., Mann, E.E., etal. (2010) Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms. Proc Natl Acad Sci USA 107: 14407-14412.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14407-14412
    • Huseby, M.J.1    Kruse, A.C.2    Digre, J.3    Kohler, P.L.4    Vocke, J.A.5    Mann, E.E.6
  • 33
    • 11144330206 scopus 로고    scopus 로고
    • Depolymerization of β-1,6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms
    • Itoh, Y., Wang, X., Hinnebusch, B.J., Preston, J.F., and Romeo, T. (2005) Depolymerization of β-1, 6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms. J Bacteriol 187: 382-387.
    • (2005) J Bacteriol , vol.187 , pp. 382-387
    • Itoh, Y.1    Wang, X.2    Hinnebusch, B.J.3    Preston, J.F.4    Romeo, T.5
  • 34
    • 38349097592 scopus 로고    scopus 로고
    • Differential roles of poly-N-acetylglucosamine surface polysaccharide and extracellular DNA in Staphylococcus aureus and Staphylococcus epidermidis biofilms
    • Izano, E.A., Amarante, M.A., Kher, W.B., and Kaplan, J.B. (2008) Differential roles of poly-N-acetylglucosamine surface polysaccharide and extracellular DNA in Staphylococcus aureus and Staphylococcus epidermidis biofilms. Appl Environ Microbiol 74: 470-476.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 470-476
    • Izano, E.A.1    Amarante, M.A.2    Kher, W.B.3    Kaplan, J.B.4
  • 35
    • 0014759913 scopus 로고
    • Cell wall glucans of the yeast and mycelial forms of Paracoccidioides brasiliensis
    • Kanetsuna, F., and Carbonell, L.M. (1970) Cell wall glucans of the yeast and mycelial forms of Paracoccidioides brasiliensis. J Bacteriol 101: 675-680.
    • (1970) J Bacteriol , vol.101 , pp. 675-680
    • Kanetsuna, F.1    Carbonell, L.M.2
  • 36
  • 37
    • 79958165964 scopus 로고    scopus 로고
    • The expanding horizons of asparagine-linked glycosylation
    • Larkin, A., and Imperiali, B. (2011) The expanding horizons of asparagine-linked glycosylation. Biochemistry 50: 4411-4426.
    • (2011) Biochemistry , vol.50 , pp. 4411-4426
    • Larkin, A.1    Imperiali, B.2
  • 38
    • 78651457518 scopus 로고    scopus 로고
    • Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homologues
    • Löfling, J., Vimberg, V., Battig, P., and Henriques-Normark, B. (2011) Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homologues. Cell Microbiol 13: 186-197.
    • (2011) Cell Microbiol , vol.13 , pp. 186-197
    • Löfling, J.1    Vimberg, V.2    Battig, P.3    Henriques-Normark, B.4
  • 39
    • 7944231131 scopus 로고    scopus 로고
    • Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage
    • López, R., and García, E. (2004) Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage. FEMS Microbiol Rev 28: 553-580.
    • (2004) FEMS Microbiol Rev , vol.28 , pp. 553-580
    • López, R.1    García, E.2
  • 41
    • 35748984396 scopus 로고    scopus 로고
    • Role of active-site residues of dispersin B, a biofilm-releasing β-hexosaminidase from a periodontal pathogen, in substrate hydrolysis
    • Manuel, S.G.A., Ragunath, C., Sait, H.B.R., Izano, E.A., Kaplan, J.B., and Ramasubbu, N. (2007) Role of active-site residues of dispersin B, a biofilm-releasing β-hexosaminidase from a periodontal pathogen, in substrate hydrolysis. FEBS J 274: 5987-5999.
    • (2007) FEBS J , vol.274 , pp. 5987-5999
    • Manuel, S.G.A.1    Ragunath, C.2    Sait, H.B.R.3    Izano, E.A.4    Kaplan, J.B.5    Ramasubbu, N.6
  • 42
    • 61849105426 scopus 로고    scopus 로고
    • Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae
    • Molina, R., González, A., Stelter, M., Pérez-Dorado, I., Kahn, R., Morales, M., etal. (2009) Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae. EMBO Rep 10: 246-251.
    • (2009) EMBO Rep , vol.10 , pp. 246-251
    • Molina, R.1    González, A.2    Stelter, M.3    Pérez-Dorado, I.4    Kahn, R.5    Morales, M.6
  • 43
    • 58149316359 scopus 로고    scopus 로고
    • Eutectic phase in water-ice: a self-assembled environment conducive to metal-catalyzed non-enzymatic RNA polymerization
    • Monnard, P.-A., and Ziock, H. (2008) Eutectic phase in water-ice: a self-assembled environment conducive to metal-catalyzed non-enzymatic RNA polymerization. Chem Biodivers 5: 1521-1539.
    • (2008) Chem Biodivers , vol.5 , pp. 1521-1539
    • Monnard, P.-A.1    Ziock, H.2
  • 45
    • 8444246041 scopus 로고    scopus 로고
    • DNA condensation by high-affinity interaction with avidin
    • Morpurgo, M., Radu, A., Bayer, E.A., and Wilchek, M. (2004) DNA condensation by high-affinity interaction with avidin. J Mol Recognit 17: 558-566.
    • (2004) J Mol Recognit , vol.17 , pp. 558-566
    • Morpurgo, M.1    Radu, A.2    Bayer, E.A.3    Wilchek, M.4
  • 46
    • 7644243116 scopus 로고    scopus 로고
    • Release of DNA into the medium by competent Streptococcus pneumoniae: kinetics, mechanism and stability of the liberated DNA
    • Moscoso, M., and Claverys, J.P. (2004) Release of DNA into the medium by competent Streptococcus pneumoniae: kinetics, mechanism and stability of the liberated DNA. Mol Microbiol 54: 783-794.
    • (2004) Mol Microbiol , vol.54 , pp. 783-794
    • Moscoso, M.1    Claverys, J.P.2
  • 47
    • 33751119902 scopus 로고    scopus 로고
    • Biofilm formation by Streptococcus pneumoniae: role of choline, extracellular DNA, and capsular polysaccharide in microbial accretion
    • Moscoso, M., García, E., and López, R. (2006) Biofilm formation by Streptococcus pneumoniae: role of choline, extracellular DNA, and capsular polysaccharide in microbial accretion. J Bacteriol 188: 7785-7795.
    • (2006) J Bacteriol , vol.188 , pp. 7785-7795
    • Moscoso, M.1    García, E.2    López, R.3
  • 48
    • 55849105558 scopus 로고    scopus 로고
    • Isolation of Streptococcus pneumoniae biofilm mutants and their characterization during nasopharyngeal colonization
    • Muñoz-Elías, E.J., Marcano, J., and Camilli, A. (2008) Isolation of Streptococcus pneumoniae biofilm mutants and their characterization during nasopharyngeal colonization. Infect Immun 76: 5049-5061.
    • (2008) Infect Immun , vol.76 , pp. 5049-5061
    • Muñoz-Elías, E.J.1    Marcano, J.2    Camilli, A.3
  • 49
    • 0027607995 scopus 로고
    • Avoiding oxidative degradation during sodium hydroxide/methyl iodide-mediated carbohydrate methylation in dimethyl sulfoxide
    • Needs, P.W., and Selvendran, R.R. (1993) Avoiding oxidative degradation during sodium hydroxide/methyl iodide-mediated carbohydrate methylation in dimethyl sulfoxide. Carbohydr Res 245: 1-10.
    • (1993) Carbohydr Res , vol.245 , pp. 1-10
    • Needs, P.W.1    Selvendran, R.R.2
  • 50
    • 0000612766 scopus 로고
    • Release of genetic transforming agent from pneumococcal cultures during growth and disintegration
    • Ottolenghi, E., and Hotchkiss, R.D. (1962) Release of genetic transforming agent from pneumococcal cultures during growth and disintegration. J Exp Med 116: 491-519.
    • (1962) J Exp Med , vol.116 , pp. 491-519
    • Ottolenghi, E.1    Hotchkiss, R.D.2
  • 51
    • 33846603188 scopus 로고    scopus 로고
    • Role of a putative polysaccharide locus in Bordetella biofilm development
    • Parise, G., Mishra, M., Itoh, Y., Romeo, T., and Deora, R. (2007) Role of a putative polysaccharide locus in Bordetella biofilm development. J Bacteriol 189: 750-760.
    • (2007) J Bacteriol , vol.189 , pp. 750-760
    • Parise, G.1    Mishra, M.2    Itoh, Y.3    Romeo, T.4    Deora, R.5
  • 52
    • 77951978074 scopus 로고    scopus 로고
    • Insights into pneumococcal fratricide from the crystal structures of the modular killing factor LytC
    • Pérez-Dorado, I., González, A., Morales, M., Sanles, R., Striker, W., Vollmer, W., etal. (2010) Insights into pneumococcal fratricide from the crystal structures of the modular killing factor LytC. Nat Struct Mol Biol 17: 576-581.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 576-581
    • Pérez-Dorado, I.1    González, A.2    Morales, M.3    Sanles, R.4    Striker, W.5    Vollmer, W.6
  • 54
    • 77958137426 scopus 로고    scopus 로고
    • The pneumococcal serine-rich repeat protein is an intra-species bacterial adhesin that promotes bacterial aggregation in vivo and in biofilms
    • Sanchez, C.J., Shivshankar, P., Stol, K., Trakhtenbroit, S., Sullam, P.M., Sauer, K., etal. (2010) The pneumococcal serine-rich repeat protein is an intra-species bacterial adhesin that promotes bacterial aggregation in vivo and in biofilms. PLoS Pathog 6: e1001044.
    • (2010) PLoS Pathog , vol.6
    • Sanchez, C.J.1    Shivshankar, P.2    Stol, K.3    Trakhtenbroit, S.4    Sullam, P.M.5    Sauer, K.6
  • 55
    • 34047255890 scopus 로고    scopus 로고
    • Lectins: carbohydrate-specific reagents and biological recognition molecules
    • Sharon, N. (2007) Lectins: carbohydrate-specific reagents and biological recognition molecules. J Biol Chem 282: 2753-2764.
    • (2007) J Biol Chem , vol.282 , pp. 2753-2764
    • Sharon, N.1
  • 56
    • 57849133629 scopus 로고    scopus 로고
    • Nonspecific activity of Bacillus acidopullulyticus pullulanase on debranching of guar galactomannan
    • Shobha, M.S., and Tharanathan, R.N. (2008) Nonspecific activity of Bacillus acidopullulyticus pullulanase on debranching of guar galactomannan. J Agric Food Chem 56: 10858-10864.
    • (2008) J Agric Food Chem , vol.56 , pp. 10858-10864
    • Shobha, M.S.1    Tharanathan, R.N.2
  • 57
    • 67650133220 scopus 로고    scopus 로고
    • Biofilm characteristics of Staphylococcus epidermidis isolates associated with device-related meningitis
    • Stevens, N.T., Greene, C.M., O'Gara, J.P., and Humphreys, H. (2009) Biofilm characteristics of Staphylococcus epidermidis isolates associated with device-related meningitis. J Med Microbiol 58: 855-862.
    • (2009) J Med Microbiol , vol.58 , pp. 855-862
    • Stevens, N.T.1    Greene, C.M.2    O'Gara, J.P.3    Humphreys, H.4
  • 58
    • 0028298367 scopus 로고
    • A comparison of conventional SEM techniques, low temperature SEM and the electroscan wet scanning electron microscope to study the structure of a biofilm of Streptococcus crista CR3
    • Sutton, N.A., Hughes, N., and Handley, P.S. (1994) A comparison of conventional SEM techniques, low temperature SEM and the electroscan wet scanning electron microscope to study the structure of a biofilm of Streptococcus crista CR3. J Appl Bacteriol 76: 448-454.
    • (1994) J Appl Bacteriol , vol.76 , pp. 448-454
    • Sutton, N.A.1    Hughes, N.2    Handley, P.S.3
  • 59
    • 0035919670 scopus 로고    scopus 로고
    • Complete genome sequence of a virulent isolate of Streptococcus pneumoniae
    • Tettelin, H., Nelson, K.E., Paulsen, I.T., Eisen, J.A., Read, T.D., Peterson, S., etal. (2001) Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science 293: 498-506.
    • (2001) Science , vol.293 , pp. 498-506
    • Tettelin, H.1    Nelson, K.E.2    Paulsen, I.T.3    Eisen, J.A.4    Read, T.D.5    Peterson, S.6
  • 60
    • 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
  • 61
    • 80855157164 scopus 로고    scopus 로고
    • LuxS mediates iron-dependent biofilm formation, competence and fratricide in Streptococcus pneumoniae
    • Trappetti, C., Potter, A.J., Paton, A.W., Oggioni, M.R., and Paton, J.C. (2011) LuxS mediates iron-dependent biofilm formation, competence and fratricide in Streptococcus pneumoniae. Infect Immun 79: 4550-4558.
    • (2011) Infect Immun , vol.79 , pp. 4550-4558
    • Trappetti, C.1    Potter, A.J.2    Paton, A.W.3    Oggioni, M.R.4    Paton, J.C.5
  • 62
    • 84866166944 scopus 로고    scopus 로고
    • Fratricide is essential for efficient gene transfer between pneumococci in biofilms
    • Wei, H., and Håvarstein, L.S. (2012) Fratricide is essential for efficient gene transfer between pneumococci in biofilms. Appl Environ Microbiol 78: 5897-5905.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 5897-5905
    • Wei, H.1    Håvarstein, L.S.2
  • 63
    • 77951207196 scopus 로고    scopus 로고
    • The pneumococcus: why a commensal misbehaves
    • Weiser, J.N. (2010) The pneumococcus: why a commensal misbehaves. J Mol Med 88: 97-102.
    • (2010) J Mol Med , vol.88 , pp. 97-102
    • Weiser, J.N.1
  • 64
    • 44949093604 scopus 로고    scopus 로고
    • Biofilms and chronic infections
    • Wolcott, R.D., and Ehrlich, G.D. (2008) Biofilms and chronic infections. JAMA 299: 2682-2684.
    • (2008) JAMA , vol.299 , pp. 2682-2684
    • Wolcott, R.D.1    Ehrlich, G.D.2
  • 65
    • 78650413684 scopus 로고    scopus 로고
    • Purification and characterization of an active N-acetylglucosaminyltransferase enzyme complex from streptococci
    • Wu, R., Zhou, M., and Wu, H. (2010) Purification and characterization of an active N-acetylglucosaminyltransferase enzyme complex from streptococci. Appl Environ Microbiol 76: 7966-7971.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 7966-7971
    • Wu, R.1    Zhou, M.2    Wu, H.3
  • 66
    • 77951246027 scopus 로고    scopus 로고
    • A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis
    • Zhou, M., Zhu, F., Dong, S., Pritchard, D.G., and Wu, H. (2010) A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis. J Biol Chem 285: 12140-12148.
    • (2010) J Biol Chem , vol.285 , pp. 12140-12148
    • Zhou, M.1    Zhu, F.2    Dong, S.3    Pritchard, D.G.4    Wu, H.5


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