메뉴 건너뛰기




Volumn 14, Issue 2, 2003, Pages 89-99

Glucan-binding proteins of the oral streptococci

Author keywords

GBP; Glucan; Glucosyltransferase; Plaque; Streptococci

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; GLUCAN; GLUCAN BINDING PROTEINS; GLUCAN-BINDING PROTEINS; GLUCOSYLTRANSFERASE; LECTIN; VIRULENCE FACTOR;

EID: 0038010630     PISSN: 10454411     EISSN: None     Source Type: Journal    
DOI: 10.1177/154411130301400203     Document Type: Review
Times cited : (273)

References (147)
  • 1
    • 0026024402 scopus 로고
    • Peptide sequences for sucrose splitting and glucan binding within Streptococcus sobrinus glucosyltransferase (waterinsoluble glucan synthetase)
    • Abo H, Matsumura T, Kodama T, Ohta H, Fukui K, Kato K, et al. (1991). Peptide sequences for sucrose splitting and glucan binding within Streptococcus sobrinus glucosyltransferase (waterinsoluble glucan synthetase). J Bacteriol 173:989-996.
    • (1991) J Bacteriol , vol.173 , pp. 989-996
    • Abo, H.1    Matsumura, T.2    Kodama, T.3    Ohta, H.4    Fukui, K.5    Kato, K.6
  • 3
    • 0032774759 scopus 로고    scopus 로고
    • Stress-induced membrane association of the streptococcus mutans GTP-binding protein, an essential g protein, and investigation of its physiological role by utilizing an antisense RNA strategy
    • Baev D, England R, Kuramitsu HK (1999). Stress-induced membrane association of the Streptococcus mutans GTP-binding protein, an essential G protein, and investigation of its physiological role by utilizing an antisense RNA strategy. Infect Immun 67:4510-4516.
    • (1999) Infect Immun , vol.67 , pp. 4510-4516
    • Baev, D.1    England, R.2    Kuramitsu, H.K.3
  • 4
    • 0025095420 scopus 로고
    • Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt
    • Banas JA, Russell RRB, Ferretti JJ (1990). Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt. Infect Immun 58:667-673.
    • (1990) Infect Immun , vol.58 , pp. 667-673
    • Banas, J.A.1    Russell, R.R.B.2    Ferretti, J.J.3
  • 5
    • 0030800548 scopus 로고    scopus 로고
    • The regulation of Streptococcus mutans glucan-binding protein-A expression
    • Banas JA, Potvin HC, Singh RN (1997). The regulation of Streptococcus mutans glucan-binding protein-A expression. FEMS Microbiol Lett 154:289-292.
    • (1997) FEMS Microbiol Lett , vol.154 , pp. 289-292
    • Banas, J.A.1    Potvin, H.C.2    Singh, R.N.3
  • 6
    • 0034920446 scopus 로고    scopus 로고
    • An in vitro model for studying the contributions of the Streptococcus mutans glucan-binding protein-A to biofilm structure
    • Banas JA, Hazlett KRO, Mazurkiewicz JE (2001). An in vitro model for studying the contributions of the Streptococcus mutans glucan-binding protein-A to biofilm structure. Meth Enzymol 337:425-433.
    • (2001) Meth Enzymol , vol.337 , pp. 425-433
    • Banas, J.A.1    Kro, H.2    Mazurkiewicz, J.E.3
  • 7
    • 0034192848 scopus 로고    scopus 로고
    • Osmoregulated periplasmic glucans in Proteobacteria
    • Bohin J-P (2000). Osmoregulated periplasmic glucans in Proteobacteria. FEMS Microbiol Lett 186:11-19.
    • (2000) FEMS Microbiol Lett , vol.186 , pp. 11-19
    • Bohin, J.-P.1
  • 8
    • 0035077507 scopus 로고    scopus 로고
    • Identification of stress-responsive genes in Streptococcus mutans by differential display reverse transcription PCR
    • Chia J-S, Lee Y-Y, Huang P-T, Chen J-Y (2001a). Identification of stress-responsive genes in Streptococcus mutans by differential display reverse transcription PCR. Infect Immun 69:2493-2501.
    • (2001) Infect Immun , vol.69 , pp. 2493-2501
    • Chia, J.-S.1    Lee, Y.-Y.2    Huang, P.-T.3    Chen, J.-Y.4
  • 9
    • 0034777402 scopus 로고    scopus 로고
    • A 60-kilodalton immunodominant glycoprotein is essential for cell wall integrity and the maintenance of cell shape in Streptococcus mutans
    • Chia J-S, Chang LY, Shun C-T, Chang Y-Y, Chen J-Y (2001b). A 60-kilodalton immunodominant glycoprotein is essential for cell wall integrity and the maintenance of cell shape in Streptococcus mutans. Infect Immun 69:6987-6998.
    • (2001) Infect Immun , vol.69 , pp. 6987-6998
    • Chia, J.-S.1    Chang, L.Y.2    Shun, C.-T.3    Chang, Y.-Y.4    Chen, J.-Y.5
  • 10
    • 0033978703 scopus 로고    scopus 로고
    • Adaptation to the environment: Streptococcus pneumoniae, a paradigm for recombination-mediated genetic plasticity?
    • Claverys JP, Prudhomme M, Mortier-Barriere I, Martin B (2000). Adaptation to the environment: Streptococcus pneumoniae, a paradigm for recombination-mediated genetic plasticity? Molec Microbiol 35:251-259.
    • (2000) Molec Microbiol , vol.35 , pp. 251-259
    • Claverys, J.P.1    Prudhomme, M.2    Mortier-Barriere, I.3    Martin, B.4
  • 12
    • 0022651648 scopus 로고
    • Comparative adhesion of seven species of streptococci isolated from the blood of patients with subacute bacterial endocarditis to platelet-fibrin clots in vitro
    • Crawford I, Russell C (1986). Comparative adhesion of seven species of streptococci isolated from the blood of patients with subacute bacterial endocarditis to platelet-fibrin clots in vitro. J Appl Bacteriol 60:127-133.
    • (1986) J Appl Bacteriol , vol.60 , pp. 127-133
    • Crawford, I.1    Russell, C.2
  • 13
    • 0021775650 scopus 로고
    • Genetic analysis of Streptococcus mutans virulence
    • Goebel W, editor. New York: Springer-Verlag
    • Curtiss R III (1985). Genetic analysis of Streptococcus mutans virulence. In: Current topics in microbial immunity. Goebel W, editor. New York: Springer-Verlag, pp. 253-277.
    • (1985) Current Topics in Microbial Immunity , pp. 253-277
    • Curtiss III, R.1
  • 14
    • 0025350016 scopus 로고
    • Association of cell-adherent glycocalyx and endocarditis production by viridans group streptococci
    • Dall LH, Herndon BL (1990). Association of cell-adherent glycocalyx and endocarditis production by viridans group streptococci. J Clin Microbiol 28:1698-1700.
    • (1990) J Clin Microbiol , vol.28 , pp. 1698-1700
    • Dall, L.H.1    Herndon, B.L.2
  • 15
    • 0031454064 scopus 로고    scopus 로고
    • Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutans streptococci
    • Devulapalle KS, Goodman SD, Gao Q, Hemsley A, Mooser G (1997). Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutans streptococci. Protein Sci 6:2489-2493.
    • (1997) Protein Sci , vol.6 , pp. 2489-2493
    • Devulapalle, K.S.1    Goodman, S.D.2    Gao, Q.3    Hemsley, A.4    Mooser, G.5
  • 16
    • 0024027006 scopus 로고
    • Physical and biochemical studies of Streptococcus mutans sediments suggest new factors linking the cariogenicity of plaque with its extracellular polysaccharide content
    • Dibdin GH, Shellis RP (1988). Physical and biochemical studies of Streptococcus mutans sediments suggest new factors linking the cariogenicity of plaque with its extracellular polysaccharide content. J Dent Res 67:890-895.
    • (1988) J Dent Res , vol.67 , pp. 890-895
    • Dibdin, G.H.1    Shellis, R.P.2
  • 17
    • 0020400707 scopus 로고
    • Effect of specific antisera on adherence properties of the oral bacterium Streptococcus mutans
    • Douglas CWI, Russell RRB (1982). Effect of specific antisera on adherence properties of the oral bacterium Streptococcus mutans. Arch Oral Biol 27:1039-1045.
    • (1982) Arch Oral Biol , vol.27 , pp. 1039-1045
    • Douglas, C.W.I.1    Russell, R.R.B.2
  • 18
    • 0023706671 scopus 로고
    • Specificity of the glucan-binding lectin of Streptococcus cricetus
    • Drake D, Taylor KG, Bleiweis AS, Doyle RJ (1988). Specificity of the glucan-binding lectin of Streptococcus cricetus. Infect Immun 56:1864-1872.
    • (1988) Infect Immun , vol.56 , pp. 1864-1872
    • Drake, D.1    Taylor, K.G.2    Bleiweis, A.S.3    Doyle, R.J.4
  • 19
    • 0023203218 scopus 로고
    • Nucleotide sequence of a glucosyltransferase gene from Streptococcus sobrinus MFe28
    • Ferretti JJ, Gilpin ML, Russell RRB (1987). Nucleotide sequence of a glucosyltransferase gene from Streptococcus sobrinus MFe28. J Bacteriol 169:4271-4278.
    • (1987) J Bacteriol , vol.169 , pp. 4271-4278
    • Ferretti, J.J.1    Gilpin, M.L.2    Russell, R.R.B.3
  • 20
    • 0034059449 scopus 로고    scopus 로고
    • Purification, characterization, and molecular analysis of the gene encoding glucosyltransferase from Streptococcus oralis
    • Fujiwara T, Hoshino T, Ooshima T, Sobue S, Hamada S (2000). Purification, characterization, and molecular analysis of the gene encoding glucosyltransferase from Streptococcus oralis. Infect Immun 68:2475-2483.
    • (2000) Infect Immun , vol.68 , pp. 2475-2483
    • Fujiwara, T.1    Hoshino, T.2    Ooshima, T.3    Sobue, S.4    Hamada, S.5
  • 21
    • 0036484444 scopus 로고    scopus 로고
    • Differential and quantitative analyses of mRNA expression of glucosyltransferases from Streptococcus mutans MT8148
    • Fujiwara T, Hoshino T, Ooshima T, Hamada S (2002). Differential and quantitative analyses of mRNA expression of glucosyltransferases from Streptococcus mutans MT8148. J Dent Res 81:109-113.
    • (2002) J Dent Res , vol.81 , pp. 109-113
    • Fujiwara, T.1    Hoshino, T.2    Ooshima, T.3    Hamada, S.4
  • 22
    • 0027728992 scopus 로고
    • An active-site peptide containing the second essential carboxyl group of dextransucrase from Leuconostoc mesenteroides by chemical modifications
    • Funane K, Shiraiwa M, Hashimoto K, Ichishima E, Kobayashi M (1993). An active-site peptide containing the second essential carboxyl group of dextransucrase from Leuconostoc mesenteroides by chemical modifications. Biochemistry 32:13696-13702.
    • (1993) Biochemistry , vol.32 , pp. 13696-13702
    • Funane, K.1    Shiraiwa, M.2    Hashimoto, K.3    Ichishima, E.4    Kobayashi, M.5
  • 23
    • 0031602383 scopus 로고    scopus 로고
    • Glucan binding regions of dextransucrase from Leuconostoc mesenteroides NRRL B-512F
    • Funane K, Ookura T, Kobayashi M (1998). Glucan binding regions of dextransucrase from Leuconostoc mesenteroides NRRL B-512F. Biosci Biotechnol Biochem 62:123-127.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 123-127
    • Funane, K.1    Ookura, T.2    Kobayashi, M.3
  • 24
    • 0025037846 scopus 로고
    • Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
    • Garcia P, Garcia JL, Garcia E, Sanchez-Puelles JM, Lopez 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
    • Garcia, P.1    Garcia, J.L.2    Garcia, E.3    Sanchez-Puelles, J.M.4    Lopez, R.5
  • 25
    • 17444442315 scopus 로고    scopus 로고
    • The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains
    • Garcia P, Paz Gonzalez M, Garcia E, Garcia JL, Lopez R (1999). The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains. Molec Microbiol 33:128-138.
    • (1999) Molec Microbiol , vol.33 , pp. 128-138
    • Garcia, P.1    Paz Gonzalez, M.2    Garcia, E.3    Garcia, J.L.4    Lopez, R.5
  • 26
    • 0342577705 scopus 로고
    • Importance of glucosyltransferases in the colonization of oral bacteria
    • Glucosyltransferases, glucans, sucrose and dental caries. Doyle RJ, Ciardi JE, editors, Washington, DC: IRL Press
    • Gibbons RJ (1983). Importance of glucosyltransferases in the colonization of oral bacteria. In: Glucosyltransferases, glucans, sucrose and dental caries. Doyle RJ, Ciardi JE, editors. Chemical Synthesis. Washington, DC: IRL Press, pp. 11-19.
    • (1983) Chemical Synthesis , pp. 11-19
    • Gibbons, R.J.1
  • 27
    • 0014515631 scopus 로고
    • Dextran-induced agglutination of Streptococcus mutans, and its potential role in the formation of microbial dental plaques
    • Gibbons RJ, Fitzgerald RJ (1969). Dextran-induced agglutination of Streptococcus mutans, and its potential role in the formation of microbial dental plaques. J Bacteriol 98:341-346.
    • (1969) J Bacteriol , vol.98 , pp. 341-346
    • Gibbons, R.J.1    Fitzgerald, R.J.2
  • 28
    • 0015876869 scopus 로고
    • On the formation of dental plaques
    • Gibbons RJ, van Houte J (1973). On the formation of dental plaques. J Periodontol 6:347-360.
    • (1973) J Periodontol , vol.6 , pp. 347-360
    • Gibbons, R.J.1    Van Houte, J.2
  • 29
    • 0028453501 scopus 로고
    • Definition of a fundamental repeating unit in streptococcal glucosyltransferase glucan-binding regions and related sequences
    • Giffard PM, Jacques NA (1994). Definition of a fundamental repeating unit in streptococcal glucosyltransferase glucan-binding regions and related sequences. J Dent Res 73:1133-1141.
    • (1994) J Dent Res , vol.73 , pp. 1133-1141
    • Giffard, P.M.1    Jacques, N.A.2
  • 30
    • 0025936694 scopus 로고
    • Molecular characterization of a cluster of at least two glucosyltransferase genes in Streptococcus salivarius ATCC 25975
    • Giffard PM, Simpson CL, Milward CP, Jacques NA (1991). Molecular characterization of a cluster of at least two glucosyltransferase genes in Streptococcus salivarius ATCC 25975. J Gen Microbiol 137:2577-2593.
    • (1991) J Gen Microbiol , vol.137 , pp. 2577-2593
    • Giffard, P.M.1    Simpson, C.L.2    Milward, C.P.3    Jacques, N.A.4
  • 31
    • 0033955056 scopus 로고    scopus 로고
    • Characterization of the gtfB and gtfC promoters from Streptococcus mutans GS-5
    • Goodman SD, Gao Q (2000). Characterization of the gtfB and gtfC promoters from Streptococcus mutans GS-5. Plasmid 43:85-98.
    • (2000) Plasmid , vol.43 , pp. 85-98
    • Goodman, S.D.1    Gao, Q.2
  • 33
    • 0014144281 scopus 로고
    • Biochemical and morphological aspects of extracellular polysaccharides produced by cariogenic streptococci
    • Guggenheim B, Schroeder HE (1967). Biochemical and morphological aspects of extracellular polysaccharides produced by cariogenic streptococci. Helv Odontol Acta 11:131-152.
    • (1967) Helv Odontol Acta , vol.11 , pp. 131-152
    • Guggenheim, B.1    Schroeder, H.E.2
  • 34
    • 0033984037 scopus 로고    scopus 로고
    • Ligand-binding properties of the carboxyl terminal repeat domain of the Streptococcus mutans glucanbinding protein-A
    • Haas W, Banas JA (2000). Ligand-binding properties of the carboxyl terminal repeat domain of the Streptococcus mutans glucanbinding protein-A. J Bacteriol 182:728-733.
    • (2000) J Bacteriol , vol.182 , pp. 728-733
    • Haas, W.1    Banas, J.A.2
  • 35
    • 0032559987 scopus 로고    scopus 로고
    • Circular dichroism analysis of the glucan binding domain of Streptococcus mutans glucan binding protein-A
    • Haas W, MacColl R, Banas JA (1998). Circular dichroism analysis of the glucan binding domain of Streptococcus mutans glucan binding protein-A. Biochim Biophys Acta 1384:112-120.
    • (1998) Biochim Biophys Acta , vol.1384 , pp. 112-120
    • Haas, W.1    Maccoll, R.2    Banas, J.A.3
  • 36
    • 0025963832 scopus 로고
    • Mutants of Streptococcus gordonii Challis over-producing glucosyltransferase
    • Haisman RJ, Jenkinson HF (1991). Mutants of Streptococcus gordonii Challis over-producing glucosyltransferase. J Gen Microbiol 137:483-489.
    • (1991) J Gen Microbiol , vol.137 , pp. 483-489
    • Haisman, R.J.1    Jenkinson, H.F.2
  • 37
    • 0019255349 scopus 로고
    • Biology, immunology, and cariogenicity of Streptococcus mutans
    • Hamada S, Slade HD (1980). Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol Rev 44:331-384.
    • (1980) Microbiol Rev , vol.44 , pp. 331-384
    • Hamada, S.1    Slade, H.D.2
  • 38
    • 0037084998 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence analysis of the Streptococcus sobrinus gtfU gene that produces a highly branched water-soluble glucan
    • Hanada N, Fukushima K, Nomura Y, Senpuku H, Hayakawa M, Mukasa H, et al. (2002). Cloning and nucleotide sequence analysis of the Streptococcus sobrinus gtfU gene that produces a highly branched water-soluble glucan. Biochim Biophys Acta 1570:75-79.
    • (2002) Biochim Biophys Acta , vol.1570 , pp. 75-79
    • Hanada, N.1    Fukushima, K.2    Nomura, Y.3    Senpuku, H.4    Hayakawa, M.5    Mukasa, H.6
  • 39
    • 0031946839 scopus 로고    scopus 로고
    • Inactivation of the gbpA gene of Streptococcus mutans increases virulence and promotes in vivo accumulation of recombinations between the glucosyltransferase B and C genes
    • Hazlett KRO, Michalek SM, Banas JA (1998). Inactivation of the gbpA gene of Streptococcus mutans increases virulence and promotes in vivo accumulation of recombinations between the glucosyltransferase B and C genes. Infect Immun 66:2180-2185.
    • (1998) Infect Immun , vol.66 , pp. 2180-2185
    • Hazlett, K.R.O.1    Michalek, S.M.2    Banas, J.A.3
  • 40
    • 0032791045 scopus 로고    scopus 로고
    • Inactivation of the gbpA gene of Streptococcus mutans alters structural and functional aspects of plaque biofilm which are compensated by recombination of the gtfB and gtfC genes
    • Hazlett KRO, Mazurkiewicz JE, Banas JA (1999). Inactivation of the gbpA gene of Streptococcus mutans alters structural and functional aspects of plaque biofilm which are compensated by recombination of the gtfB and gtfC genes. Infect Immun 67:3909-3914.
    • (1999) Infect Immun , vol.67 , pp. 3909-3914
    • Kro, H.1    Mazurkiewicz, J.E.2    Banas, J.A.3
  • 41
    • 0020684201 scopus 로고
    • Aggregation of human platelets and adhesion of Streptococcus sanguis
    • Herzberg MC, Brintzenhofe KL, Clawson CC (1983). Aggregation of human platelets and adhesion of Streptococcus sanguis. Infect Immun 39:1457-1469.
    • (1983) Infect Immun , vol.39 , pp. 1457-1469
    • Herzberg, M.C.1    Brintzenhofe, K.L.2    Clawson, C.C.3
  • 42
    • 0025128843 scopus 로고
    • Phenotype characterization of Streptococcus sanguis virulence factors associated with bacterial endocarditis
    • Herzberg MC, Gong K, MacFarlane GD, Erickson PR, Soberaly AH, Krebsbach PH, et al. (1990). Phenotype characterization of Streptococcus sanguis virulence factors associated with bacterial endocarditis. Infect Immun 58:515-522.
    • (1990) Infect Immun , vol.58 , pp. 515-522
    • Herzberg, M.C.1    Gong, K.2    Macfarlane, G.D.3    Erickson, P.R.4    Soberaly, A.H.5    Krebsbach, P.H.6
  • 43
    • 0033814084 scopus 로고    scopus 로고
    • Nucleotide sequencing and transcriptional analysis of two tandem genes encoding glucosyltransferase (water-soluble-glucan synthetase) in Streptococccus cricetus HS-6
    • Inoue M, Inoue T, Miyagi A, Tanimoto I, Shingaki R, Ohta H, et al. (2000). Nucleotide sequencing and transcriptional analysis of two tandem genes encoding glucosyltransferase (water-soluble-glucan synthetase) in Streptococccus cricetus HS-6. Microbiol Immunol 44:755-764.
    • (2000) Microbiol Immunol , vol.44 , pp. 755-764
    • Inoue, M.1    Inoue, T.2    Miyagi, A.3    Tanimoto, I.4    Shingaki, R.5    Ohta, H.6
  • 45
    • 0032721526 scopus 로고    scopus 로고
    • Protective immunity against Streptococcus mutans infection in mice after intranasal immunization with the glucan-binding region of S. Mutans glucosyltransferase
    • Jespersgaard C, Hajishengallis G, Huang Y, Russell MW, Smith DJ, Michalek SM (1999b). Protective immunity against Streptococcus mutans infection in mice after intranasal immunization with the glucan-binding region of S. mutans glucosyltransferase. Infect Immun 67:6543-6549.
    • (1999) Infect Immun , vol.67 , pp. 6543-6549
    • Jespersgaard, C.1    Hajishengallis, G.2    Huang, Y.3    Russell, M.W.4    Smith, D.J.5    Michalek, S.M.6
  • 46
    • 0033959684 scopus 로고    scopus 로고
    • Single-molecule imaging of interaction between dextran and glucosyltransferase from Streptococcus sobrinus
    • Kaseda K, Yokota H, Ishii Y, Yanagida T, Inoue T, Fukui K, Kodama T (2000). Single-molecule imaging of interaction between dextran and glucosyltransferase from Streptococcus sobrinus. J Bacteriol 182:1162-1166.
    • (2000) J Bacteriol , vol.182 , pp. 1162-1166
    • Kaseda, K.1    Yokota, H.2    Ishii, Y.3    Yanagida, T.4    Inoue, T.5    Fukui, K.6    Kodama, T.7
  • 47
    • 0035816441 scopus 로고    scopus 로고
    • A novel approach for purification of recombinant proteins using the dextranbinding domain
    • Kaseda K, Kodama T, Fukui K, Hirose K (2001). A novel approach for purification of recombinant proteins using the dextranbinding domain. FEBS Lett 500:141-144.
    • (2001) FEBS Lett , vol.500 , pp. 141-144
    • Kaseda, K.1    Kodama, T.2    Fukui, K.3    Hirose, K.4
  • 48
    • 0025119148 scopus 로고
    • Carboxyl-terminal deletion analysis of the Streptococcus mutans glucosyltransferase-I enzyme
    • Kato C, Kuramitsu HK (1990). Carboxyl-terminal deletion analysis of the Streptococcus mutans glucosyltransferase-I enzyme. FEMS Microbiol Lett 72:299-302.
    • (1990) FEMS Microbiol Lett , vol.72 , pp. 299-302
    • Kato, C.1    Kuramitsu, H.K.2
  • 49
    • 0025911210 scopus 로고
    • Molecular basis for the association of glucosyltransferases with the cell surface of oral streptococci
    • Kato C, Kuramitsu HK (1991). Molecular basis for the association of glucosyltransferases with the cell surface of oral streptococci. FEMS Microbiol Lett 79:153-158.
    • (1991) FEMS Microbiol Lett , vol.79 , pp. 153-158
    • Kato, C.1    Kuramitsu, H.K.2
  • 50
    • 0016153607 scopus 로고
    • Adhesion of dextran to Streptococcus mutans
    • Kelstrup J, Funder-Neilsen TD (1974). Adhesion of dextran to Streptococcus mutans. J Gen Microbiol 81:485-489.
    • (1974) J Gen Microbiol , vol.81 , pp. 485-489
    • Kelstrup, J.1    Funder-Neilsen, T.D.2
  • 51
    • 0001223159 scopus 로고    scopus 로고
    • Escherichia coli and Salmonella. Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, et al., editors. Washington, DC: ASM Press
    • Kennedy EP (1996). Membrane-derived oligosaccharides (periplasmic beta-D-glucans) of Escherichia coli. In: Escherichia coli and Salmonella. Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, et al., editors. Washington, DC: ASM Press, pp. 1064-1071.
    • (1996) Membrane-derived Oligosaccharides (Periplasmic Beta-D-glucans) of Escherichia Col , pp. 1064-1071
    • Kennedy, E.P.1
  • 52
    • 0036181645 scopus 로고    scopus 로고
    • Role of the C-terminal YG repeats of the primer-dependent streptococcal glucosyltransferase, GtfJ, in binding to dextran and mutan
    • Kingston KB, Allen DM, Jacques NA (2002). Role of the C-terminal YG repeats of the primer-dependent streptococcal glucosyltransferase, GtfJ, in binding to dextran and mutan. Microbiology 148:549-558.
    • (2002) Microbiology , vol.148 , pp. 549-558
    • Kingston, K.B.1    Allen, D.M.2    Jacques, N.A.3
  • 53
    • 0037093598 scopus 로고    scopus 로고
    • Immunization against dental caries
    • Koga T, Oho T, Shimazaki Y, Nakano Y (2002). Immunization against dental caries. Vaccine 20:2027-2044.
    • (2002) Vaccine , vol.20 , pp. 2027-2044
    • Koga, T.1    Oho, T.2    Shimazaki, Y.3    Nakano, Y.4
  • 54
    • 0035219757 scopus 로고    scopus 로고
    • Properties of Streptococcus sanguinis glucans formed under various conditions
    • Kopec LK, Vacca-Smith AM, Wunder D, Ng-Evans L, Bowen WH (2001). Properties of Streptococcus sanguinis glucans formed under various conditions. Caries Res 35:67-74.
    • (2001) Caries Res , vol.35 , pp. 67-74
    • Kopec, L.K.1    Vacca-Smith, A.M.2    Wunder, D.3    Ng-Evans, L.4    Bowen, W.H.5
  • 55
    • 0036731751 scopus 로고    scopus 로고
    • Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1,4) and alpha-(1,6) glucosidic bonds
    • Kralj S, Van Geel-Schutten GH, Rahaoui H, Leer RJ, Faber EJ, Van Der Maarel MJ, et al. (2002). Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1,4) and alpha-(1,6) glucosidic bonds. Appl Env Microbiol 68:4283-4291.
    • (2002) Appl Env Microbiol , vol.68 , pp. 4283-4291
    • Kralj, S.1    Van Geel-Schutten, G.H.2    Rahaoui, H.3    Leer, R.J.4    Faber, E.J.5    Van Der Maarel, M.J.6
  • 56
    • 0001023448 scopus 로고
    • The effect of caries-inducing streptococci in hamsters fed diets with sucrose or glucose
    • Krasse B (1965). The effect of caries-inducing streptococci in hamsters fed diets with sucrose or glucose. Arch Oral Biol 10:223-226.
    • (1965) Arch Oral Biol , vol.10 , pp. 223-226
    • Krasse, B.1
  • 57
    • 0016185492 scopus 로고
    • Adherence of Streptococcus mutans to dextran synthesized in the presence of extracellular dextransucrase
    • Kuramitsu HK (1974). Adherence of Streptococcus mutans to dextran synthesized in the presence of extracellular dextransucrase. Infect Immun 9:764-765.
    • (1974) Infect Immun , vol.9 , pp. 764-765
    • Kuramitsu, H.K.1
  • 58
    • 0027530878 scopus 로고
    • Virulence factors of mutans streptococci: Role of molecular genetics
    • Kuramitsu HK (1993). Virulence factors of mutans streptococci: role of molecular genetics. Crit Rev Oral Biol Med 4:159-176.
    • (1993) Crit Rev Oral Biol Med , vol.4 , pp. 159-176
    • Kuramitsu, H.K.1
  • 59
    • 0017902877 scopus 로고
    • Interaction of glucosyltransferase with the cell surface of Streptococcus mutans
    • Kuramitsu HK, Ingersoll L (1978). Interaction of glucosyltransferase with the cell surface of Streptococcus mutans. Infect Immun 20:652-659.
    • (1978) Infect Immun , vol.20 , pp. 652-659
    • Kuramitsu, H.K.1    Ingersoll, L.2
  • 60
    • 0023515531 scopus 로고
    • Characterization by affinity electrophoresis of an alpha-1,6-glucan- binding protein from Streptococcus sobrinus
    • Landale EC, McCabe MM (1987). Characterization by affinity electrophoresis of an alpha-1,6-glucan-binding protein from Streptococcus sobrinus. Infect Immun 55:3011-3016.
    • (1987) Infect Immun , vol.55 , pp. 3011-3016
    • Landale, E.C.1    McCabe, M.M.2
  • 61
    • 0034779082 scopus 로고    scopus 로고
    • Regulation of the gtfBC and ftf genes of Streptococcus mutans in biofilms in response to pH and carbohydrate
    • Li Y, Burne RA (2001). Regulation of the gtfBC and ftf genes of Streptococcus mutans in biofilms in response to pH and carbohydrate. Microbiology 147:2841-2848.
    • (2001) Microbiology , vol.147 , pp. 2841-2848
    • Li, Y.1    Burne, R.A.2
  • 62
    • 0028989758 scopus 로고
    • Role of C-terminal direct repeating units of the Streptococcus mutans glucosyltransferase-S in glucan binding
    • Lis M, Shiroza T, Kuramitsu HK (1995). Role of C-terminal direct repeating units of the Streptococcus mutans glucosyltransferase-S in glucan binding. Appl Env Microbiol 61:2040-2042.
    • (1995) Appl Env Microbiol , vol.61 , pp. 2040-2042
    • Lis, M.1    Shiroza, T.2    Kuramitsu, H.K.3
  • 63
    • 0022993292 scopus 로고
    • Role of Streptococcus mutans in human dental decay
    • Loesche WJ (1986). Role of Streptococcus mutans in human dental decay. Microbiol Rev 50:353-380.
    • (1986) Microbiol Rev , vol.50 , pp. 353-380
    • Loesche, W.J.1
  • 64
    • 0026737727 scopus 로고
    • Chelating agents inhibit activity and prevent expression of streptococcal glucan-binding lectins
    • Lu L, Singh JS, Galperin MY, Drake D, Taylor KG, Doyle RJ (1992). Chelating agents inhibit activity and prevent expression of streptococcal glucan-binding lectins. Infect Immun 60:3807-3813.
    • (1992) Infect Immun , vol.60 , pp. 3807-3813
    • Lu, L.1    Singh, J.S.2    Galperin, M.Y.3    Drake, D.4    Taylor, K.G.5    Doyle, R.J.6
  • 66
    • 0029671161 scopus 로고    scopus 로고
    • A circularly permuted alpha-amylase-type alpha/beta-barrel structure in glucan-synthesizing glucosyltransferases
    • MacGregor EA, Jespersen HM, Svensson B (1996). A circularly permuted alpha-amylase-type alpha/beta-barrel structure in glucan-synthesizing glucosyltransferases. FEBS Lett 378:263-266.
    • (1996) FEBS Lett , vol.378 , pp. 263-266
    • Macgregor, E.A.1    Jespersen, H.M.2    Svensson, B.3
  • 67
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes
    • MacGregor EA, Janecek S, Svensson B (2001). Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim Biophys Acta 1546:1-20.
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 1-20
    • Macgregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 68
    • 0034441153 scopus 로고    scopus 로고
    • Waterinsoluble glucan synthesis by mutans streptococcal strains correlates with caries incidence in 12- to 30-month-old children
    • Mattos-Graner RO, Smith DJ, King WF, Mayer MPA (2000). Waterinsoluble glucan synthesis by mutans streptococcal strains correlates with caries incidence in 12- to 30-month-old children. J Dent Res 79:1372-1377.
    • (2000) J Dent Res , vol.79 , pp. 1372-1377
    • Mattos-Graner, R.O.1    Smith, D.J.2    King, W.F.3    Mayer, M.P.A.4
  • 69
    • 0034772911 scopus 로고    scopus 로고
    • Cloning of the Streptococcus mutans gene encoding glucan binding protein B and analysis of genetic diversity and protein production in clinical isolates
    • Mattos-Graner RO, Jin S, King WF, Chen T, Smith DJ, Duncan MJ (2001). Cloning of the Streptococcus mutans gene encoding glucan binding protein B and analysis of genetic diversity and protein production in clinical isolates. Infect Immun 69:6931-6941.
    • (2001) Infect Immun , vol.69 , pp. 6931-6941
    • Mattos-Graner, R.O.1    Jin, S.2    King, W.F.3    Chen, T.4    Smith, D.J.5    Duncan, M.J.6
  • 70
    • 4244125380 scopus 로고    scopus 로고
    • Mutant analysis of the gene encoding glucan binding protein B indicates an essential role in Streptococcus mutans (abstract)
    • Mattos-Graner RO, Zucchi P, Smith DJ, Duncan MJ (2002). Mutant analysis of the gene encoding glucan binding protein B indicates an essential role in Streptococcus mutans (abstract). J Dent Res 81(Spec Iss A):40.
    • (2002) J Dent Res , vol.81 , Issue.SPEC. ISS A , pp. 40
    • Mattos-Graner, R.O.1    Zucchi, P.2    Smith, D.J.3    Duncan, M.J.4
  • 71
    • 0017080587 scopus 로고
    • Comments on adherence of Streptococcus mutans
    • McCabe MM (1976). Comments on adherence of Streptococcus mutans. J Dent Res 55:C226-C228.
    • (1976) J Dent Res , vol.55
    • McCabe, M.M.1
  • 72
    • 0018157061 scopus 로고
    • Multiple forms of dextran-binding proteins from Streptococcus mutans
    • McCabe MM, Hamelik RM (1978). Multiple forms of dextran-binding proteins from Streptococcus mutans. Adv Exp Biol Med 107:749-759.
    • (1978) Adv Exp Biol Med , vol.107 , pp. 749-759
    • McCabe, M.M.1    Hamelik, R.M.2
  • 73
    • 0016836298 scopus 로고
    • Relationship between cell-bound dextransucrase and the agglutination of Streptococcus mutans
    • McCabe MM, Smith EE (1975). Relationship between cell-bound dextransucrase and the agglutination of Streptococcus mutans. Infect Immun 12:512-520.
    • (1975) Infect Immun , vol.12 , pp. 512-520
    • McCabe, M.M.1    Smith, E.E.2
  • 74
    • 84885191633 scopus 로고
    • Carbohydrate receptors of oral streptococci
    • Bowen WH, Genco RJ, O'Brien TC, editors. Washington, DC: Information Retrieval, Inc.
    • McCabe MM, Smith EE (1976). Carbohydrate receptors of oral streptococci. In: Immunologic aspects of dental caries. Bowen WH, Genco RJ, O'Brien TC, editors. Washington, DC: Information Retrieval, Inc., pp. 111-119.
    • (1976) Immunologic Aspects of Dental Caries , pp. 111-119
    • McCabe, M.M.1    Smith, E.E.2
  • 75
    • 0017755063 scopus 로고
    • Specific method for the purification of Streptococcus mutans dextransucrase
    • McCabe MM, Smith EE (1977). Specific method for the purification of Streptococcus mutans dextransucrase. Infect Immun 16:760-765.
    • (1977) Infect Immun , vol.16 , pp. 760-765
    • McCabe, M.M.1    Smith, E.E.2
  • 76
    • 0017707254 scopus 로고
    • Purification of dextran-binding protein from cariogenic Streptococcus mutans
    • McCabe MM, Hamelik RM, Smith EE (1977). Purification of dextran-binding protein from cariogenic Streptococcus mutans. Biochem Biophys Res Commun 78:273-278.
    • (1977) Biochem Biophys Res Commun , vol.78 , pp. 273-278
    • McCabe, M.M.1    Hamelik, R.M.2    Smith, E.E.3
  • 78
    • 0020455805 scopus 로고
    • Effect of extracellular polysaccharides on diffusion of NaF and [14C]-sucrose in human dental plaque and in sediments of the bacterium Streptococcus sanguis 804 (NCTC 10904
    • McNee SG, Geddes DA, Weetman DA, Sweeney D, Beeley JA (1982). Effect of extracellular polysaccharides on diffusion of NaF and [14C]-sucrose in human dental plaque and in sediments of the bacterium Streptococcus sanguis 804 (NCTC 10904). Arch Oral Biol 27:981-986.
    • (1982) Arch Oral Biol , vol.27 , pp. 981-986
    • McNee, S.G.1    Geddes, D.A.2    Weetman, D.A.3    Sweeney, D.4    Beeley, J.A.5
  • 79
    • 0021269728 scopus 로고
    • Role of granulocytes in the induction of an experimental endocarditis with a dextran-producing Streptococcus sanguis and its dextrannegative mutant
    • Meddens MJ, Thompson J, Leijh PC, Van Furth R (1984). Role of granulocytes in the induction of an experimental endocarditis with a dextran-producing Streptococcus sanguis and its dextrannegative mutant. Br J Exp Pathol 65:257-265.
    • (1984) Br J Exp Pathol , vol.65 , pp. 257-265
    • Meddens, M.J.1    Thompson, J.2    Leijh, P.C.3    Van Furth, R.4
  • 80
    • 0017399191 scopus 로고
    • Low sucrose levels promote extensive Streptococcus mutans-induced dental caries
    • Michalek SM, McGhee JR, Shiota T, Devenyns D (1977). Low sucrose levels promote extensive Streptococcus mutans-induced dental caries. Infect Immun 16:712-714.
    • (1977) Infect Immun , vol.16 , pp. 712-714
    • Michalek, S.M.1    McGhee, J.R.2    Shiota, T.3    Devenyns, D.4
  • 81
    • 0034786060 scopus 로고    scopus 로고
    • A vaccine against dental caries: An overview
    • Michalek SM, Katz J, Childers NK (2001). A vaccine against dental caries: an overview. BioDrugs 15:501-508.
    • (2001) BioDrugs , vol.15 , pp. 501-508
    • Michalek, S.M.1    Katz, J.2    Childers, N.K.3
  • 82
    • 0032781308 scopus 로고    scopus 로고
    • Secondary structure of Streptococcus downei GTF-I glucansucrase
    • Monchois V, Lakey JH, Russell RRB (1999a). Secondary structure of Streptococcus downei GTF-I glucansucrase. FEMS Microbiol Lett 177:243-248.
    • (1999) FEMS Microbiol Lett , vol.177 , pp. 243-248
    • Monchois, V.1    Lakey, J.H.2    Russell, R.R.B.3
  • 83
    • 0032896501 scopus 로고    scopus 로고
    • Glucansucrases: Mechanism of action and structure-function relationships
    • Monchois V, Willemot RM, Monsan P (1999b). Glucansucrases: mechanism of action and structure-function relationships. FEMS Microbiol Rev 23:131-151.
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 131-151
    • Monchois, V.1    Willemot, R.M.2    Monsan, P.3
  • 85
    • 0023907043 scopus 로고
    • Isolation of a glucan-binding domain of glucosyltransferase (1,6-alpha-glucan synthase) from Streptococcus sobrinus
    • Mooser G, Wong C (1988). Isolation of a glucan-binding domain of glucosyltransferase (1,6-alpha-glucan synthase) from Streptococcus sobrinus. Infect Immun 56:880-884.
    • (1988) Infect Immun , vol.56 , pp. 880-884
    • Mooser, G.1    Wong, C.2
  • 86
    • 0025827032 scopus 로고
    • Isolation and sequence of an active site peptide containing a catalytic aspartic acid from two Streptococcus sobrinus glucosyltransferases
    • Mooser G, Hefta SA, Paxton RJ, Shively JE, Lee TD (1991). Isolation and sequence of an active site peptide containing a catalytic aspartic acid from two Streptococcus sobrinus glucosyltransferases. J Biol Chem 266:8916-8922.
    • (1991) J Biol Chem , vol.266 , pp. 8916-8922
    • Mooser, G.1    Hefta, S.A.2    Paxton, R.J.3    Shively, J.E.4    Lee, T.D.5
  • 87
    • 0015947472 scopus 로고
    • Mechanism of adherence of Streptococcus mutans to smooth surfaces. II. Nature of the binding site and the adsorption of dextran-levan synthetase enzymes on the cell-wall surface of the streptococcus
    • Mukasa H, Slade HD (1974). Mechanism of adherence of Streptococcus mutans to smooth surfaces. II. Nature of the binding site and the adsorption of dextran-levan synthetase enzymes on the cell-wall surface of the streptococcus. Infect Immun 9:419-429.
    • (1974) Infect Immun , vol.9 , pp. 419-429
    • Mukasa, H.1    Slade, H.D.2
  • 88
    • 0027453283 scopus 로고
    • Sucrose-derived exopolysaccharides of Streptococcus mutans V403 contribute to infectivity in endocarditis
    • Munro C, Macrina FL (1993). Sucrose-derived exopolysaccharides of Streptococcus mutans V403 contribute to infectivity in endocarditis. Molec Microbiol 8:133-142.
    • (1993) Molec Microbiol , vol.8 , pp. 133-142
    • Munro, C.1    Macrina, F.L.2
  • 89
    • 0025741198 scopus 로고
    • Cariogenicity of Streptococcus mutans V403 glucosyltransferase and fructosyltransferase mutants constructed by allelic exchange
    • Munro C, Michalek SM, Macrina FL (1991). Cariogenicity of Streptococcus mutans V403 glucosyltransferase and fructosyltransferase mutants constructed by allelic exchange. Infect Immun 59:2316-2323.
    • (1991) Infect Immun , vol.59 , pp. 2316-2323
    • Munro, C.1    Michalek, S.M.2    Macrina, F.L.3
  • 90
    • 0029016526 scopus 로고
    • Sucrose-derived exopolymers have site-dependent roles in Streptococcus mutanspromoted dental decay
    • Munro CL, Michalek SM, Macrina FL (1995). Sucrose-derived exopolymers have site-dependent roles in Streptococcus mutanspromoted dental decay. FEMS Microbiol Lett 128:327-332.
    • (1995) FEMS Microbiol Lett , vol.128 , pp. 327-332
    • Munro, C.L.1    Michalek, S.M.2    Macrina, F.L.3
  • 91
    • 0035983372 scopus 로고    scopus 로고
    • Attenuation of glucan-binding protein C reduces the cariogencity of Streptococcus mutans: Analysis of strains isolated from human blood
    • Nakano K, Matsumura M, Kawaguchi M, Fujiwara T, Sobue S, Nakagawa I, et al. (2002). Attenuation of glucan-binding protein C reduces the cariogencity of Streptococcus mutans: analysis of strains isolated from human blood. J Dent Res 81:376-379.
    • (2002) J Dent Res , vol.81 , pp. 376-379
    • Nakano, K.1    Matsumura, M.2    Kawaguchi, M.3    Fujiwara, T.4    Sobue, S.5    Nakagawa, I.6
  • 92
    • 0026787839 scopus 로고
    • Mechanism of Streptococcus mutans glucosyltransferases: Hybrid-enzyme analysis
    • Nakano YJ, Kuramitsu HK (1992). Mechanism of Streptococcus mutans glucosyltransferases: hybrid-enzyme analysis. J Bacteriol 174:5639-5646.
    • (1992) J Bacteriol , vol.174 , pp. 5639-5646
    • Nakano, Y.J.1    Kuramitsu, H.K.2
  • 93
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of Gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre WW, Schneewind O (1999). Surface proteins of Gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol Mol Biol Rev 63:174-229.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 94
    • 0018067467 scopus 로고
    • Dextran receptors as immunogens in caries prophylaxis
    • McGhee J.R, editor. New York: Plenum Press
    • Olson GA (1978). Dextran receptors as immunogens in caries prophylaxis. In: Secretory immunity and infection. McGhee JR, editor. New York: Plenum Press, pp. 771-781.
    • (1978) Secretory Immunity and Infection , pp. 771-781
    • Olson, G.A.1
  • 95
    • 0015964844 scopus 로고
    • Antibody-mediated inhibition of dextran-sucrose-induced agglutination of Streptococcus mutans
    • Olson GA, Guggenheim B, Small PAJ (1974). Antibody-mediated inhibition of dextran-sucrose-induced agglutination of Streptococcus mutans. Infect Immun 9:273-278.
    • (1974) Infect Immun , vol.9 , pp. 273-278
    • Olson, G.A.1    Guggenheim, B.2    Paj, S.3
  • 96
    • 0018169824 scopus 로고
    • Dextran production as a possible virulence factor in streptococcal endocarditis
    • Pelletier LL, Coyle M, Petersdorf RG (1978). Dextran production as a possible virulence factor in streptococcal endocarditis. Proc Soc Exp Biol Med 158:415-420.
    • (1978) Proc Soc Exp Biol Med , vol.158 , pp. 415-420
    • Pelletier, L.L.1    Coyle, M.2    Petersdorf, R.G.3
  • 97
    • 0020577661 scopus 로고
    • Genetic transformation of putative cariogenic properties in Streptococcus mutans
    • Perry D, Wondrack LM, Kuramitsu HK (1983). Genetic transformation of putative cariogenic properties in Streptococcus mutans. Infect Immun 41:722-727.
    • (1983) Infect Immun , vol.41 , pp. 722-727
    • Perry, D.1    Wondrack, L.M.2    Kuramitsu, H.K.3
  • 98
    • 0024834054 scopus 로고
    • Physiology, biochemistry and genetics of bacterial glycogen synthesis
    • Preiss J, Romeo T (1989). Physiology, biochemistry and genetics of bacterial glycogen synthesis. Adv Microb Physiol 30:183-238.
    • (1989) Adv Microb Physiol , vol.30 , pp. 183-238
    • Preiss, J.1    Romeo, T.2
  • 99
    • 0018079899 scopus 로고
    • Adherence of glucan-positive and glucan-negative streptococcal strains to normal and damaged heart valves
    • Ramiriz-Ronda CH (1978). Adherence of glucan-positive and glucan-negative streptococcal strains to normal and damaged heart valves. J Clin Invest 62:805-814.
    • (1978) J Clin Invest , vol.62 , pp. 805-814
    • Ramiriz-Ronda, C.H.1
  • 100
    • 0018902811 scopus 로고
    • Effects of molecular weight of dextran on the adherence of Streptococcus sanguis to damaged heart valves
    • Ramiriz-Ronda CH (1980). Effects of molecular weight of dextran on the adherence of Streptococcus sanguis to damaged heart valves. Infect Immun 29:1-7.
    • (1980) Infect Immun , vol.29 , pp. 1-7
    • Ramiriz-Ronda, C.H.1
  • 101
    • 0018379163 scopus 로고
    • Glucan-binding proteins of Streptococcus mutans serotype c
    • Russell RRB (1979). Glucan-binding proteins of Streptococcus mutans serotype c. J Gen Microbiol 112:197-201.
    • (1979) J Gen Microbiol , vol.112 , pp. 197-201
    • Russell, R.R.B.1
  • 102
    • 0025619626 scopus 로고
    • Molecular genetics of glucan metabolism in oral streptococci
    • Russell RRB (1990). Molecular genetics of glucan metabolism in oral streptococci. Arch Oral Biol 35:53S-58S.
    • (1990) Arch Oral Biol , vol.35
    • Russell, R.R.B.1
  • 103
    • 0021933503 scopus 로고
    • Expression of a gene for glucan-binding protein from Streptococcus mutans in Escherichia coli
    • Russell RRB, Coleman D, Dougan G (1985). Expression of a gene for glucan-binding protein from Streptococcus mutans in Escherichia coli. J Gen Microbiol 131:295-299.
    • (1985) J Gen Microbiol , vol.131 , pp. 295-299
    • Russell, R.R.B.1    Coleman, D.2    Dougan, G.3
  • 104
    • 0031036878 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the gbpC gene encoding a novel glucan-binding protein of Streptococcus mutans
    • Sato Y, Yamamoto Y, Kizaki H (1997). Cloning and sequence analysis of the gbpC gene encoding a novel glucan-binding protein of Streptococcus mutans. Infect Immun 65:668-675.
    • (1997) Infect Immun , vol.65 , pp. 668-675
    • Sato, Y.1    Yamamoto, Y.2    Kizaki, H.3
  • 105
    • 0034607978 scopus 로고    scopus 로고
    • Construction of regionspecific partial duplication mutants (merodiploid mutants) to identify the regulatory gene for the glucan-binding protein C gene in vivo in Streptococcus mutans
    • Sato Y, Yamamoto Y, Harutoshi K (2000). Construction of regionspecific partial duplication mutants (merodiploid mutants) to identify the regulatory gene for the glucan-binding protein C gene in vivo in Streptococcus mutans. FEMS Microbiol Lett 186:187-191.
    • (2000) FEMS Microbiol Lett , vol.186 , pp. 187-191
    • Sato, Y.1    Yamamoto, Y.2    Harutoshi, K.3
  • 106
    • 0034897764 scopus 로고    scopus 로고
    • The LuxS family of bacterial autoinducers: Biosynthesis of a novel quorum-sensing signal molecule
    • Schauder S, Shokat K, Surette MG, Bassler BL (2001). The LuxS family of bacterial autoinducers: biosynthesis of a novel quorum-sensing signal molecule. Molec Microbiol 41:463-476.
    • (2001) Molec Microbiol , vol.41 , pp. 463-476
    • Schauder, S.1    Shokat, K.2    Surette, M.G.3    Bassler, B.L.4
  • 107
    • 0018144003 scopus 로고
    • Bacterial adhesion in the pathogenesis of endocarditis: Interactions of bacterial dextran, platelets, and fibrin
    • Scheld WM, Valone JA, Sande MA (1978). Bacterial adhesion in the pathogenesis of endocarditis: interactions of bacterial dextran, platelets, and fibrin. J Clin Invest 61:1394-1404.
    • (1978) J Clin Invest , vol.61 , pp. 1394-1404
    • Scheld, W.M.1    Valone, J.A.2    Sande, M.A.3
  • 108
    • 0015238731 scopus 로고
    • Dental caries: Prospects for prevention
    • Scherp HW (1971). Dental caries: prospects for prevention. Science 173:1199-1205.
    • (1971) Science , vol.173 , pp. 1199-1205
    • Scherp, H.W.1
  • 109
    • 4043123760 scopus 로고    scopus 로고
    • A novel glucan-binding protein from Streptococcus mutans
    • 6th ed. Asheville, NC: American Society for Microbiology
    • Shah DS, Russell RRB (2002). A novel glucan-binding protein from Streptococcus mutans. In: Streptococcal genetics. 6th ed. Asheville, NC: American Society for Microbiology, pp. 75.
    • (2002) Streptococcal Genetics , pp. 75
    • Shah, D.S.1    Russell, R.R.B.2
  • 110
    • 0030629244 scopus 로고    scopus 로고
    • Adsorption of Streptococcus mutans dextranase inhibitor to water-insoluble alpha-D-glucans of oral streptococci
    • Shaw JM, Wellington JE, Walker GJ (1997). Adsorption of Streptococcus mutans dextranase inhibitor to water-insoluble alpha-D-glucans of oral streptococci. Caries Res 31:441-450.
    • (1997) Caries Res , vol.31 , pp. 441-450
    • Shaw, J.M.1    Wellington, J.E.2    Walker, G.J.3
  • 111
    • 0028918003 scopus 로고
    • Streptococcus salivarius ATCC 25975 possesses at least two genes coding for primerindependent glucosyltransferases
    • Simpson CL, Giffard PM, Jacques NA (1995). Streptococcus salivarius ATCC 25975 possesses at least two genes coding for primerindependent glucosyltransferases. Infect Immun 63:609-621.
    • (1995) Infect Immun , vol.63 , pp. 609-621
    • Simpson, C.L.1    Giffard, P.M.2    Jacques, N.A.3
  • 112
    • 84912295642 scopus 로고
    • Specific binding of glucosyltransferase by Streptococcus mutans and its effect on the adherence of the organism
    • Schlessinger D, editor. Washington, DC: American Society for Microbiology
    • Slade HD (1977). Specific binding of glucosyltransferase by Streptococcus mutans and its effect on the adherence of the organism. In: Microbiology-1977. Schlessinger D, editor. Washington, DC: American Society for Microbiology, pp. 411-416.
    • (1977) Microbiology-1977 , pp. 411-416
    • Slade, H.D.1
  • 113
    • 0030037294 scopus 로고    scopus 로고
    • Experimental immunization of rats with a Streptococcus mutans 59-kilodalton glucan-binding protein protects against dental caries
    • Smith DJ, Taubman MA (1996). Experimental immunization of rats with a Streptococcus mutans 59-kilodalton glucan-binding protein protects against dental caries. Infect Immun 64:3069-3073.
    • (1996) Infect Immun , vol.64 , pp. 3069-3073
    • Smith, D.J.1    Taubman, M.A.2
  • 114
    • 0018388106 scopus 로고
    • Preparation of glucosyltransferase from Streptococcus mutans by elution from watersoluble polysaccharide with a dissociating solvent
    • Smith DJ, Taubman MA, Ebersole JL (1979). Preparation of glucosyltransferase from Streptococcus mutans by elution from watersoluble polysaccharide with a dissociating solvent. Infect Immun 23:446-452.
    • (1979) Infect Immun , vol.23 , pp. 446-452
    • Smith, D.J.1    Taubman, M.A.2    Ebersole, J.L.3
  • 115
    • 0028229808 scopus 로고
    • Purification and antigenicity of a novel glucan-binding protein of Streptococcus mutans
    • Smith DJ, Akita H, King WF, Taubman MA (1994). Purification and antigenicity of a novel glucan-binding protein of Streptococcus mutans. Infect Immun 62:2545-2552.
    • (1994) Infect Immun , vol.62 , pp. 2545-2552
    • Smith, D.J.1    Akita, H.2    King, W.F.3    Taubman, M.A.4
  • 116
    • 0000201895 scopus 로고    scopus 로고
    • Streptococcus mutans glucan binding proteins as dental caries vaccines
    • Husband AJ, Beagley KW, Clancy RL, Collins AM, Cripps AW, Emery DL, editors. Sydney: University of Sydney Press
    • Smith DJ, Heschel RL, Melvin J, King WF, Pereira MBB, Taubman MA (1997). Streptococcus mutans glucan binding proteins as dental caries vaccines. In: Mucosal solutions. Husband AJ, Beagley KW, Clancy RL, Collins AM, Cripps AW, Emery DL, editors. Sydney: University of Sydney Press, pp. 367-377.
    • (1997) Mucosal Solutions , pp. 367-377
    • Smith, D.J.1    Heschel, R.L.2    Melvin, J.3    King, W.F.4    Pereira, M.B.B.5    Taubman, M.A.6
  • 117
    • 0032438167 scopus 로고    scopus 로고
    • Structural and antigenic characteristics of Streptococcus sobrinus glucan binding proteins
    • Smith DJ, King WF, Wu CD, Shen BI, Taubman MA (1998). Structural and antigenic characteristics of Streptococcus sobrinus glucan binding proteins. Infect Immun 66:5565-5569.
    • (1998) Infect Immun , vol.66 , pp. 5565-5569
    • Smith, D.J.1    King, W.F.2    Wu, C.D.3    Shen, B.I.4    Taubman, M.A.5
  • 118
    • 0035064161 scopus 로고    scopus 로고
    • Passive transfer of immunoglobulin y antibody to Streptococcus mutans glucan binding protein B can confer protection against experimental dental caries
    • Smith DJ, King WF, Godiska R (2001). Passive transfer of immunoglobulin Y antibody to Streptococcus mutans glucan binding protein B can confer protection against experimental dental caries. Infect Immun 69:3135-3142.
    • (2001) Infect Immun , vol.69 , pp. 3135-3142
    • Smith, D.J.1    King, W.F.2    Godiska, R.3
  • 119
    • 0026708281 scopus 로고
    • Identification of a gene, rgg, which regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis
    • Sulavik MC, Tardif G, Clewell DB (1992). Identification of a gene, rgg, which regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis. J Bacteriol 174:3577-3586.
    • (1992) J Bacteriol , vol.174 , pp. 3577-3586
    • Sulavik, M.C.1    Tardif, G.2    Clewell, D.B.3
  • 120
    • 0028019545 scopus 로고
    • Cloning and DNA sequencing of the dextranase inhibitor gene (dei) from Streptococcus sobrinus
    • Sun J-W, Wanda S-Y, Camilli A, Curtiss R III (1994). Cloning and DNA sequencing of the dextranase inhibitor gene (dei) from Streptococcus sobrinus. J Bacteriol 176:7213-7222.
    • (1994) J Bacteriol , vol.176 , pp. 7213-7222
    • Sun, J.-W.1    Wanda, S.-Y.2    Camilli, A.3    Curtiss III, R.4
  • 121
    • 0028940608 scopus 로고
    • Purification, characterization, and specificity of dextranase inhibitor (Dei) expressed from Streptococcus sobrinus UAB108 gene cloned in
    • Sun J-W, Wanda S-Y, Curtiss R III (1995). Purification, characterization, and specificity of dextranase inhibitor (Dei) expressed from Streptococcus sobrinus UAB108 gene cloned in Escherichia coli. J Bacteriol 177:1703-1711.
    • (1995) Escherichia Coli. J Bacteriol , vol.177 , pp. 1703-1711
    • Sun, J.-W.1    Wanda, S.-Y.2    Curtiss III, R.3
  • 122
    • 0016198220 scopus 로고
    • Diminished virulence of glucan synthesis-defective mutants of Streptococcus mutans
    • Tanzer JM, Freedman ML, Fitzgerald RJ, Larson RH (1974). Diminished virulence of glucan synthesis-defective mutants of Streptococcus mutans. Infect Immun 10:197-203.
    • (1974) Infect Immun , vol.10 , pp. 197-203
    • Tanzer, J.M.1    Freedman, M.L.2    Fitzgerald, R.J.3    Larson, R.H.4
  • 123
    • 0002977508 scopus 로고
    • Virulence of mutants defective in glucosyltransferase, dextran-mediated aggregation, or dextranase activity
    • Mergenhagen SE, Rosan B, editors. Washington, DC: American Society for Microbiology
    • Tanzer JM, Freedman ML, Fitzgerald RJ (1985). Virulence of mutants defective in glucosyltransferase, dextran-mediated aggregation, or dextranase activity. In: Molecular basis of oral microbial adhesion. Mergenhagen SE, Rosan B, editors. Washington, DC: American Society for Microbiology, pp. 204-211.
    • (1985) Molecular Basis of Oral Microbial Adhesion , pp. 204-211
    • Tanzer, J.M.1    Freedman, M.L.2    Fitzgerald, R.J.3
  • 124
    • 0024395661 scopus 로고
    • Spontaneous switching of the sucrose-promoted colony phenotype in Streptococcus sanguis
    • Tardif G, Sulavik M, Jones GW, Clewell DB (1989). Spontaneous switching of the sucrose-promoted colony phenotype in Streptococcus sanguis. Infect Immun 57:3945-3948.
    • (1989) Infect Immun , vol.57 , pp. 3945-3948
    • Tardif, G.1    Sulavik, M.2    Jones, G.W.3    Clewell, D.B.4
  • 125
    • 0034062212 scopus 로고    scopus 로고
    • Coimmunization with complementary glucosyltransferase peptides results in enhanced immunogenicity and protection against dental caries
    • Taubman MA, Smith DJ, Holmberg CJ, Eastcott JW (2000). Coimmunization with complementary glucosyltransferase peptides results in enhanced immunogenicity and protection against dental caries. Infect Immun 68:2698-2703.
    • (2000) Infect Immun , vol.68 , pp. 2698-2703
    • Taubman, M.A.1    Smith, D.J.2    Holmberg, C.J.3    Eastcott, J.W.4
  • 126
    • 0023807889 scopus 로고
    • Molecular basis for the spontaneous generation of colonization-defective mutants of Streptococcus mutans
    • Ueda S, Kuramitsu HK (1988). Molecular basis for the spontaneous generation of colonization-defective mutants of Streptococcus mutans. Molec Microbiol 2:135-140.
    • (1988) Molec Microbiol , vol.2 , pp. 135-140
    • Ueda, S.1    Kuramitsu, H.K.2
  • 127
    • 0028290561 scopus 로고
    • Glucosyltransferase mediates adhesion of Streptococcus gordonii to human endothelial cells
    • Vacca-Smith AM, Jones CA, Levine MJ, Stinson MW (1994). Glucosyltransferase mediates adhesion of Streptococcus gordonii to human endothelial cells in vitro. Infect Immun 62:2187-2194.
    • (1994) In Vitro. Infect Immun , vol.62 , pp. 2187-2194
    • Vacca-Smith, A.M.1    Jones, C.A.2    Levine, M.J.3    Stinson, M.W.4
  • 128
    • 0024636310 scopus 로고
    • Increased pH-lowering ability of Streptococcus mutans cell masses associated with extracellular glucan-rich matrix material and the mechanisms involved
    • van Houte J, Russo J, Prostak KS (1989). Increased pH-lowering ability of Streptococcus mutans cell masses associated with extracellular glucan-rich matrix material and the mechanisms involved. J Dent Res 68:451-459.
    • (1989) J Dent Res , vol.68 , pp. 451-459
    • Van Houte, J.1    Russo, J.2    Prostak, K.S.3
  • 129
    • 0029806935 scopus 로고    scopus 로고
    • Changes in the carboxyl-terminal repeat region affect extracellular activity and glucan products of Streptococcus gordonii glucosyltransferase
    • Vickerman MM, Sulavik MC, Minick PE, Clewell DB (1996). Changes in the carboxyl-terminal repeat region affect extracellular activity and glucan products of Streptococcus gordonii glucosyltransferase. Infect Immun 64:5117-5128.
    • (1996) Infect Immun , vol.64 , pp. 5117-5128
    • Vickerman, M.M.1    Sulavik, M.C.2    Minick, P.E.3    Clewell, D.B.4
  • 130
    • 0031126254 scopus 로고    scopus 로고
    • Molecular analysis of representative Streptococcus gordonii Spp phase variants reveals no differences in the glucosyltransferase structural gene, gtfG
    • Vickerman MM, Jones GW, Clewell DB (1997a). Molecular analysis of representative Streptococcus gordonii Spp phase variants reveals no differences in the glucosyltransferase structural gene, gtfG. Oral Microbiol Immunol 12:82-90.
    • (1997) Oral Microbiol Immunol , vol.12 , pp. 82-90
    • Vickerman, M.M.1    Jones, G.W.2    Clewell, D.B.3
  • 132
    • 0026702564 scopus 로고
    • Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases
    • von Eichel-Streiber C, Sauerborn M, Kuramitsu HK (1992). Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases. J Bacteriol 174:6707-6710.
    • (1992) J Bacteriol , vol.174 , pp. 6707-6710
    • Von Eichel-Streiber, C.1    Sauerborn, M.2    Kuramitsu, H.K.3
  • 133
    • 0019766445 scopus 로고
    • Metabolism of the polysaccharides of human dental plaque: Release of dextranase in batch cultures of Streptococcus mutans
    • Walker GJ, Pulkownik A, Morrey-Jones JG (1981). Metabolism of the polysaccharides of human dental plaque: release of dextranase in batch cultures of Streptococcus mutans. J Gen Microbiol 127:201-208.
    • (1981) J Gen Microbiol , vol.127 , pp. 201-208
    • Walker, G.J.1    Pulkownik, A.2    Morrey-Jones, J.G.3
  • 134
    • 0029843079 scopus 로고    scopus 로고
    • Microbial hydrolysis of polysaccharides
    • Warren RAJ (1996). Microbial hydrolysis of polysaccharides. Annu Rev Microbiol 50:183-212.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 183-212
    • Raj, W.1
  • 135
    • 0027182940 scopus 로고
    • Infectivity of a glucan synthesis-defective mutant of Streptococcus gordonii (Challis) in a rat endocarditis model
    • Wells VD, Munro C, Sulavik M, Clewell DB, Macrina FL (1993). Infectivity of a glucan synthesis-defective mutant of Streptococcus gordonii (Challis) in a rat endocarditis model. FEMS Microbiol Lett 112:301-306.
    • (1993) FEMS Microbiol Lett , vol.112 , pp. 301-306
    • Wells, V.D.1    Munro, C.2    Sulavik, M.3    Clewell, D.B.4    Macrina, F.L.5
  • 136
    • 0027512967 scopus 로고
    • Streptococcus mutans fructosyltransferase (ftf) and glucosyltransferase (gtfBC) operon fusion strains in continuous culture
    • Wexler DL, Hudson MC, Burne RA (1993). Streptococcus mutans fructosyltransferase (ftf) and glucosyltransferase (gtfBC) operon fusion strains in continuous culture. Infect Immun 61:1259-1267.
    • (1993) Infect Immun , vol.61 , pp. 1259-1267
    • Wexler, D.L.1    Hudson, M.C.2    Burne, R.A.3
  • 137
    • 0032146784 scopus 로고    scopus 로고
    • Current classification of the oral streptococci
    • Whiley RA, Beighton D (1998). Current classification of the oral streptococci. Oral Microbiol Immunol 13:195-216.
    • (1998) Oral Microbiol Immunol , vol.13 , pp. 195-216
    • Whiley, R.A.1    Beighton, D.2
  • 138
    • 0036224825 scopus 로고    scopus 로고
    • LuxS: Its role in central metabolism and the in vitro synthesis of 4-hydroxy-5-methyl-3(2H)-furanone
    • Winzer K, Hardie KR, Burgess N, Doherty N, Kirke D, Holden MT, et al. (2002). LuxS: its role in central metabolism and the in vitro synthesis of 4-hydroxy-5-methyl-3(2H)-furanone. Microbiology 148:909-922.
    • (2002) Microbiology , vol.148 , pp. 909-922
    • Winzer, K.1    Hardie, K.R.2    Burgess, N.3    Doherty, N.4    Kirke, D.5    Holden, M.T.6
  • 139
    • 0025365829 scopus 로고
    • Size and subdomain architecture of the glucan-binding domain of sucrose: 3-alpha-D-glucosyltransferase from Streptococcus sobrinus
    • Wong C, Stanley AH, Paxton RJ, Shively JE, Mooser G (1990). Size and subdomain architecture of the glucan-binding domain of sucrose: 3-alpha-D-glucosyltransferase from Streptococcus sobrinus. Infect Immun 58:2165-2170.
    • (1990) Infect Immun , vol.58 , pp. 2165-2170
    • Wong, C.1    Stanley, A.H.2    Paxton, R.J.3    Shively, J.E.4    Mooser, G.5
  • 140
    • 0025896984 scopus 로고
    • A family of clostridial and streptococcal ligandbinding proteins with conserved C-terminal repeat sequences
    • Wren BW (1991). A family of clostridial and streptococcal ligandbinding proteins with conserved C-terminal repeat sequences. Molec Microbiol 5:797-803.
    • (1991) Molec Microbiol , vol.5 , pp. 797-803
    • Wren, B.W.1
  • 141
    • 0026448826 scopus 로고
    • An 87-kilodalton glucan-binding protein of Streptococcus sobrinus B13
    • Wu-Yuan CD, Gill RE (1992). An 87-kilodalton glucan-binding protein of Streptococcus sobrinus B13. Infect Immun 60:5291-5293.
    • (1992) Infect Immun , vol.60 , pp. 5291-5293
    • Wu-Yuan, C.D.1    Gill, R.E.2
  • 142
    • 0018163379 scopus 로고
    • Dextran/glucan binding by Streptococcus mutans: The role of molecular size and binding site in agglutination
    • Wu-Yuan CD, Tai S, Slade HD (1978). Dextran/glucan binding by Streptococcus mutans: the role of molecular size and binding site in agglutination. Adv Exp Med Biol 107:737-748.
    • (1978) Adv Exp Med Biol , vol.107 , pp. 737-748
    • Wu-Yuan, C.D.1    Tai, S.2    Slade, H.D.3
  • 143
    • 0026560577 scopus 로고
    • Molecular analysis of a Streptococcus mutans strain exhibiting polymorphism in the tandem gtfB and gtfC genes
    • Yamashita Y, Bowen WH, Kuramitsu HK (1992). Molecular analysis of a Streptococcus mutans strain exhibiting polymorphism in the tandem gtfB and gtfC genes. Infect Immun 60:1618-1624.
    • (1992) Infect Immun , vol.60 , pp. 1618-1624
    • Yamashita, Y.1    Bowen, W.H.2    Kuramitsu, H.K.3
  • 144
    • 0027323903 scopus 로고
    • Role of the Streptococcus mutans gtf genes in caries induction in the specific-pathogen-free rat model
    • Yamashita Y, Bowen WH, Burne RA, Kuramitsu HK (1993). Role of the Streptococcus mutans gtf genes in caries induction in the specific-pathogen-free rat model. Infect Immun 61:3811-3817.
    • (1993) Infect Immun , vol.61 , pp. 3811-3817
    • Yamashita, Y.1    Bowen, W.H.2    Burne, R.A.3    Kuramitsu, H.K.4
  • 146
    • 0028298752 scopus 로고
    • Novel surface attachment mechanism of the Streptococcus pneumoniae protein PspA
    • Yother J, White JM (1994). Novel surface attachment mechanism of the Streptococcus pneumoniae protein PspA. J Bacteriol 176:2976-2985.
    • (1994) J Bacteriol , vol.176 , pp. 2976-2985
    • Yother, J.1    White, J.M.2
  • 147
    • 0031001179 scopus 로고    scopus 로고
    • Effects of antibodies against cell surface protein antigen PAc-glucosyltransferase fusion proteins on glucan synthesis and cell adhesion of
    • Yu H, Nakano Y, Yamashita Y, Oho T, Koga T (1997). Effects of antibodies against cell surface protein antigen PAc-glucosyltransferase fusion proteins on glucan synthesis and cell adhesion of Streptcoccus mutans. Infect Immun 65:2292-2298.
    • (1997) Streptcoccus Mutans. Infect Immun , vol.65 , pp. 2292-2298
    • Yu, H.1    Nakano, Y.2    Yamashita, Y.3    Oho, T.4    Koga, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.