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Volumn 53, Issue 11, 2008, Pages 1003-1010

Electron microscopic detection and activity of glucosyltransferase B, C, and D in the in situ formed pellicle

Author keywords

Activity; Biofilm; Enzymes; Fructose; Glucosyltranferases; Immunolabelling; Isoform; Pellicle

Indexed keywords

1,3 ALPHA GLUCAN SYNTHASE; 1,3-ALPHA-D-GLUCAN SYNTHASE; GLUCOSYLTRANSFERASE; GLUCOSYLTRANSFERASE C; GLUCOSYLTRANSFERASE D;

EID: 51549097128     PISSN: 00039969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.archoralbio.2008.04.005     Document Type: Article
Times cited : (32)

References (33)
  • 2
    • 33644820983 scopus 로고    scopus 로고
    • The structure, function and properties of the acquired pellicle
    • Hannig M., and Joiner A. The structure, function and properties of the acquired pellicle. Monogr Oral Sci 19 (2006) 29-64
    • (2006) Monogr Oral Sci , vol.19 , pp. 29-64
    • Hannig, M.1    Joiner, A.2
  • 3
    • 14644439885 scopus 로고    scopus 로고
    • Enzymes in the acquired enamel pellicle
    • Hannig C., Hannig M., and Attin T. Enzymes in the acquired enamel pellicle. Eur J Oral Sci 113 (2005) 2-13
    • (2005) Eur J Oral Sci , vol.113 , pp. 2-13
    • Hannig, C.1    Hannig, M.2    Attin, T.3
  • 4
    • 0028478301 scopus 로고
    • Bacterial-protein interactions in the oral cavity
    • Douglas C.W. Bacterial-protein interactions in the oral cavity. Adv Dent Res 8 (1994) 254-262
    • (1994) Adv Dent Res , vol.8 , pp. 254-262
    • Douglas, C.W.1
  • 5
    • 0034111261 scopus 로고    scopus 로고
    • In situ studies of pellicle formation on hydroxyapatite discs
    • Vacca-Smith A.M., and Bowen W.H. In situ studies of pellicle formation on hydroxyapatite discs. Arch Oral Biol 45 (2000) 277-291
    • (2000) Arch Oral Biol , vol.45 , pp. 277-291
    • Vacca-Smith, A.M.1    Bowen, W.H.2
  • 6
    • 84989555017 scopus 로고
    • Glucosyltransferase activity in human in vivo formed enamel pellicle and in whole saliva
    • Scheie A.A., Eggen K.H., and Rolla G. Glucosyltransferase activity in human in vivo formed enamel pellicle and in whole saliva. Scand J Dent Res 95 (1987) 212-215
    • (1987) Scand J Dent Res , vol.95 , pp. 212-215
    • Scheie, A.A.1    Eggen, K.H.2    Rolla, G.3
  • 7
    • 0030332898 scopus 로고    scopus 로고
    • Characterization of glucosyltransferase of human saliva adsorbed onto hydroxyapatite surfaces
    • Vacca-Smith A.M., Venkitaraman A.R., Schilling K.M., and Bowen W.H. Characterization of glucosyltransferase of human saliva adsorbed onto hydroxyapatite surfaces. Caries Res 30 (1996) 354-360
    • (1996) Caries Res , vol.30 , pp. 354-360
    • Vacca-Smith, A.M.1    Venkitaraman, A.R.2    Schilling, K.M.3    Bowen, W.H.4
  • 8
    • 0024352390 scopus 로고
    • Isolation and characterization of the Streptococcus mutans gtfD gene, coding for primer-dependent soluble glucan synthesis
    • Hanada N., and Kuramitsu H.K. Isolation and characterization of the Streptococcus mutans gtfD gene, coding for primer-dependent soluble glucan synthesis. Infect Immun 57 (1989) 2079-2085
    • (1989) Infect Immun , vol.57 , pp. 2079-2085
    • Hanada, N.1    Kuramitsu, H.K.2
  • 9
    • 0022993292 scopus 로고
    • Role of Streptococcus mutans in human dental decay
    • Loesche W.J. Role of Streptococcus mutans in human dental decay. Microbiol Rev 50 (1986) 353-380
    • (1986) Microbiol Rev , vol.50 , pp. 353-380
    • Loesche, W.J.1
  • 10
    • 0019255349 scopus 로고
    • Biology, immunology, and cariogenicity of Streptococcus mutans
    • Hamada S., and Slade H.D. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol Rev 44 (1980) 331-384
    • (1980) Microbiol Rev , vol.44 , pp. 331-384
    • Hamada, S.1    Slade, H.D.2
  • 11
    • 0034221147 scopus 로고    scopus 로고
    • Studies concerning the glucosyltransferase of Streptococcus sanguis
    • Vacca Smith A.M., Ng-Evans L., Wunder D., and Bowen W.H. Studies concerning the glucosyltransferase of Streptococcus sanguis. Caries Res 34 (2000) 295-302
    • (2000) Caries Res , vol.34 , pp. 295-302
    • Vacca Smith, A.M.1    Ng-Evans, L.2    Wunder, D.3    Bowen, W.H.4
  • 12
    • 0030099910 scopus 로고    scopus 로고
    • Interactions of streptococcal glucosyltransferases with alpha-amylase and starch on the surface of saliva-coated hydroxyapatite
    • Vacca-Smith A.M., Venkitaraman A.R., Quivey Jr. R.G., and Bowen W.H. Interactions of streptococcal glucosyltransferases with alpha-amylase and starch on the surface of saliva-coated hydroxyapatite. Arch Oral Biol 41 (1996) 291-298
    • (1996) Arch Oral Biol , vol.41 , pp. 291-298
    • Vacca-Smith, A.M.1    Venkitaraman, A.R.2    Quivey Jr., R.G.3    Bowen, W.H.4
  • 13
    • 0028186760 scopus 로고
    • The application of molecular genetics to the microbiology of dental caries
    • Russell R.R. The application of molecular genetics to the microbiology of dental caries. Caries Res 28 (1994) 69-82
    • (1994) Caries Res , vol.28 , pp. 69-82
    • Russell, R.R.1
  • 14
    • 0023253002 scopus 로고
    • Sequence analysis of the gtfB gene from Streptococcus mutans
    • Shiroza T., Ueda S., and Kuramitsu H.K. Sequence analysis of the gtfB gene from Streptococcus mutans. J Bacteriol 169 (1987) 4263-4270
    • (1987) J Bacteriol , vol.169 , pp. 4263-4270
    • Shiroza, T.1    Ueda, S.2    Kuramitsu, H.K.3
  • 15
    • 0025013877 scopus 로고
    • Nucleotide sequence of the Streptococcus mutans gtfD gene encoding the glucosyltransferase-S enzyme
    • Honda O., Kato C., and Kuramitsu H.K. Nucleotide sequence of the Streptococcus mutans gtfD gene encoding the glucosyltransferase-S enzyme. J Gen Microbiol 136 (1990) 2099-2105
    • (1990) J Gen Microbiol , vol.136 , pp. 2099-2105
    • Honda, O.1    Kato, C.2    Kuramitsu, H.K.3
  • 16
    • 0023678631 scopus 로고
    • Sequence analysis of the gtfC gene from Streptococcus mutans GS-5
    • Ueda S., Shiroza T., and Kuramitsu H.K. Sequence analysis of the gtfC gene from Streptococcus mutans GS-5. Gene 69 (1988) 101-109
    • (1988) Gene , vol.69 , pp. 101-109
    • Ueda, S.1    Shiroza, T.2    Kuramitsu, H.K.3
  • 19
    • 15844401945 scopus 로고    scopus 로고
    • Transmission electron microscopy comparison of methods for collecting in situ formed enamel pellicle
    • Hannig M., Khanafer A.K., Hoth-Hannig W., Al-Marrawi F., and Acil Y. Transmission electron microscopy comparison of methods for collecting in situ formed enamel pellicle. Clin Oral Investig 9 (2005) 30-37
    • (2005) Clin Oral Investig , vol.9 , pp. 30-37
    • Hannig, M.1    Khanafer, A.K.2    Hoth-Hannig, W.3    Al-Marrawi, F.4    Acil, Y.5
  • 20
    • 34948841994 scopus 로고    scopus 로고
    • Fluorescence microscopic visualization and quantification of initial bacterial colonization on enamel in situ
    • Hannig C., Hannig M., Rehmer O., Braun G., Hellwig E., and Al-Ahmad A. Fluorescence microscopic visualization and quantification of initial bacterial colonization on enamel in situ. Arch Oral Biol 52 (2007) 1048-1056
    • (2007) Arch Oral Biol , vol.52 , pp. 1048-1056
    • Hannig, C.1    Hannig, M.2    Rehmer, O.3    Braun, G.4    Hellwig, E.5    Al-Ahmad, A.6
  • 22
    • 0000440206 scopus 로고
    • Determination of d-fructose and d-glucose
    • Bermeyer H.U. (Ed), Verlag Chemie, Basel
    • Kunst A., Draeger B., and Ziegenhorn J. Determination of d-fructose and d-glucose. In: Bermeyer H.U. (Ed). Methods of enzymatic analysis (1984), Verlag Chemie, Basel 163-172
    • (1984) Methods of enzymatic analysis , pp. 163-172
    • Kunst, A.1    Draeger, B.2    Ziegenhorn, J.3
  • 23
    • 10344249113 scopus 로고    scopus 로고
    • Immobilisation and activity of human alpha-amylase in the acquired enamel pellicle
    • Hannig C., Attin T., Hannig M., Henze E., Brinkmann K., and Zech R. Immobilisation and activity of human alpha-amylase in the acquired enamel pellicle. Arch Oral Biol 49 (2004) 469-475
    • (2004) Arch Oral Biol , vol.49 , pp. 469-475
    • Hannig, C.1    Attin, T.2    Hannig, M.3    Henze, E.4    Brinkmann, K.5    Zech, R.6
  • 24
    • 41149147032 scopus 로고    scopus 로고
    • Intrinsic enzymatic crosslinking and maturation of the in situ pellicle
    • Hannig C., Spitzmüller B., Miller M.B., and Hannig M. Intrinsic enzymatic crosslinking and maturation of the in situ pellicle. Arch Oral Biol 53 (2008) 416-422
    • (2008) Arch Oral Biol , vol.53 , pp. 416-422
    • Hannig, C.1    Spitzmüller, B.2    Miller, M.B.3    Hannig, M.4
  • 25
    • 23844506852 scopus 로고    scopus 로고
    • Development of a rapid, quantitative glucosyltransferase assay based on a screen-printed fructose enzyme electrode and application to optimization studies on gtfD expression in recombinant Escherichia coli
    • Kadow S., Betiku E., Rinas U., and Bilitewski U. Development of a rapid, quantitative glucosyltransferase assay based on a screen-printed fructose enzyme electrode and application to optimization studies on gtfD expression in recombinant Escherichia coli. Biotechnol Bioeng 91 (2005) 154-161
    • (2005) Biotechnol Bioeng , vol.91 , pp. 154-161
    • Kadow, S.1    Betiku, E.2    Rinas, U.3    Bilitewski, U.4
  • 27
    • 20444476766 scopus 로고    scopus 로고
    • Lysozyme activity in the initially formed in situ pellicle
    • Hannig C., Hoch J., Becker K., Hannig M., and Attin T. Lysozyme activity in the initially formed in situ pellicle. Arch Oral Biol 50 (2005) 821-828
    • (2005) Arch Oral Biol , vol.50 , pp. 821-828
    • Hannig, C.1    Hoch, J.2    Becker, K.3    Hannig, M.4    Attin, T.5
  • 28
    • 0344110195 scopus 로고    scopus 로고
    • Binding properties of streptococcal glucosyltransferases for hydroxyapatite, saliva-coated hydroxyapatite, and bacterial surfaces
    • Vacca-Smith A.M., and Bowen W.H. Binding properties of streptococcal glucosyltransferases for hydroxyapatite, saliva-coated hydroxyapatite, and bacterial surfaces. Arch Oral Biol 43 (1998) 103-110
    • (1998) Arch Oral Biol , vol.43 , pp. 103-110
    • Vacca-Smith, A.M.1    Bowen, W.H.2
  • 29
    • 0033139583 scopus 로고    scopus 로고
    • Ultrastructural investigation of pellicle morphogenesis at two different intraoral sites during a 24-h period
    • Hannig M. Ultrastructural investigation of pellicle morphogenesis at two different intraoral sites during a 24-h period. Clin Oral Investig 3 (1999) 88-95
    • (1999) Clin Oral Investig , vol.3 , pp. 88-95
    • Hannig, M.1
  • 30
    • 0014515631 scopus 로고
    • Dextran-induced agglutination of Streptococcus mutans, and its potential role in the formation of microbial dental plaques
    • Gibbons R.J., and Fitzgerald R.J. Dextran-induced agglutination of Streptococcus mutans, and its potential role in the formation of microbial dental plaques. J Bacteriol 98 (1969) 341-346
    • (1969) J Bacteriol , vol.98 , pp. 341-346
    • Gibbons, R.J.1    Fitzgerald, R.J.2
  • 31
    • 0026592688 scopus 로고
    • Glucans synthesized in situ in experimental salivary pellicle function as specific binding sites for Streptococcus mutans
    • Schilling K.M., and Bowen W.H. Glucans synthesized in situ in experimental salivary pellicle function as specific binding sites for Streptococcus mutans. Infect Immun 60 (1992) 284-295
    • (1992) Infect Immun , vol.60 , pp. 284-295
    • Schilling, K.M.1    Bowen, W.H.2
  • 32
    • 0024160452 scopus 로고
    • Infections from biomaterials and implants: a race for the surface
    • Gristina A.G., Naylor P., and Myrvik Q. Infections from biomaterials and implants: a race for the surface. Med Prog Technol 14 (1988) 205-224
    • (1988) Med Prog Technol , vol.14 , pp. 205-224
    • Gristina, A.G.1    Naylor, P.2    Myrvik, Q.3
  • 33
    • 0028866787 scopus 로고
    • Dental plaque as a biofilm
    • Marsh P., and Bradshaw D.J. Dental plaque as a biofilm. J Induct Micro 15 (1995) 169-175
    • (1995) J Induct Micro , vol.15 , pp. 169-175
    • Marsh, P.1    Bradshaw, D.J.2


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