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Chapter 31 : Role of Sucrose Metabolism in the Cariogenicity of the Mutans Streptococci

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Role of Sucrose Metabolism in the Cariogenicity of the Mutans Streptococci, Page 1 of 2

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Abstract:

Dental caries constitutes the most common, and very likely the most expensive, of human diseases. Two members of the mutans streptococci (MS), and , are the most common human cariogenic pathogens. Several enzymes or enzyme systems in the MS are associated with the metabolism of sucrose, and most may be involved in the virulence of these oral pathogens. All MS have glucosyltransferases (GTFs) responsible for the synthesis of extracellular homopolymers of glucose which may be water soluble or insoluble, depending on the proportion of α-1,3 linkages present. The amino acid sequences of the proteins predicted by the respective scrA genes shared only 45% identity, whereas the corresponding sucrose phosphate hydrolase (SPH) proteins predicted by the genes shared ~ 70% amino acid identity. An extremely useful feature of recombinant DNA technology is the ability to manipulate cloned genetic determinants from a particular organism, to replace the wild-type determinant with the altered one, and then to test the effects of such manipulation on the phenotype associated with that determinant. Such a process requires an ability to introduce DNA into the organism under study. Finally, the availability of gene transfer systems and appropriate vector molecules will permit comparative analyses of the regulation of sucrose metabolism in the MS.

Citation: LeBlanc D. 1994. Role of Sucrose Metabolism in the Cariogenicity of the Mutans Streptococci, p 465-477. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch31

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Chromosomal DNA
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Figure 1

Metabolism of sucrose by MS. Abbreviations: FTF, fructosyltransferase; GTF, glucosyl-transferase; MSM, membrane-associated transport proteins of the operon ( ); TTS, very low affinity, non-PTS, third (sucrose) transport system ( ); EH, EII, EII, and EII, trehalose-, sucrose-, glucose-, and fructose-specific enzyme IIs, respectively, of the PTS; Sue, sucrose; Suc-6-P, sucrose phosphorylated in the C-6 position of the glucose moiety; Suc-12-P, sucrose phosphorylated in the C-6 position of the fructose moiety; Glu, glucose; Glu-l-P and Glu-6-P, glucose phosphorylated in the C-1 and C-6 positions, respectively; Fru, fructose; Fru-6-P and Fru-1,6-diP, fructose phosphorylated in the C-6 position and in both the C-1 and C-6 carbon positions, respectively; P-Glu, phosphoglucose; Gly-3-P, glyceraldehyde-3-phosphate; DHAP, dihydroxyacetone phosphate; PEP, phosphoenolpyruvate; PTS, PEP-dependent phosphotransferase system; EI∼P and HPr∼P, phosphorylated EI (enzyme I) and HPr (heat-stable protein), respectively, which are cytoplasmic phosphocarrier proteins of the PTS providing phosphate groups for all sugar-specific Ells; EtOH, ethanol.

Citation: LeBlanc D. 1994. Role of Sucrose Metabolism in the Cariogenicity of the Mutans Streptococci, p 465-477. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch31
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References

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1. Chassy, B. M.,, and E. V. Porter. 1982. Sucrose-6-phosphate hydrolase from Streptococcus mutans. Methods Enzymol. 90:556559.
2. Chen, Y. M. 1993. Genetic analysis of scrA and scrB from Streptococcus sobrinus strain 6715. Ph.D. thesis. University of Texas Health Science Center at San Antonio, San Antonio.
3. Chen, Y. M.,, and D. J. LeBlanc. 1992. Genetic analysis of scrA and scrB from Streptococcus sobrinus 6715. Infect. Immun. 60:37393746.
4. Chen, Y.-Y. M.,, L. N. Lee,, and D. J. LeBlanc. 1993. Sequence analysis of scrA and scrB from Streptococcus sobrinus 6715. Infect. Immun. 61:26022610.
5. Churchward, G.,, D. Belin,, and Y. Nagamine. 1984. A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors. Gene 31:165171.
6. Ellwood, D. C.,, and I. R. Hamilton. 1982. Properties of Streptococcus mutans Ingbritt growing on limiting sucrose in a chemostat: repression of the phosphoenolpyruvate phosphotransferase transport system. Infect. Immun. 36:576581.
7. Ellwood, D. C.,, J. R. Hunter,, and V. M. C. Longyear. 1974. Growth of Streptococcus mutans in a chemostat. Arch. Oral Biol. 19:659664.
8. Fitzgerald, R. J.,, and P. H. Keyes. 1960. Demonstration of the etiologic role of streptococci in experimental caries in the hamster. J. Am. Dent. Assoc. 61:919.
9. Gibbons, R. J. 1964. Bacteriology of caries. J. Dent. Res. 46(Suppl.):10211028.
10. Hayakawa, M.,, H. Aoki,, and H. K. Kuramitsu. 1986. Isolation and characterization of the sucrose-6-phosphate hydrolase gene from Streptococcus mutans. Infect. Immun. 53:582586.
11. Hillman, J. D. 1978. Lactate dehydrogenase mutans of Streptococcus mutans; isolation and preliminary characterization. Infect. Immun. 21:206212.
12. Keyes, P. H. 1960. The infectious and transmissible nature of experimental dental caries. Findings and implications. Arch. Oral Biol. 1:304320.
13. Kuramitsu, H. K. 1973. Characterization of invertase activity from cariogenic Streptococcus mutans. J. Bacteriol. 115:10031010.
14. Kuramitsu, H. K.,, T. Shiroza,, S. Sato,, and M. Hayakawa,. 1987. Genetic analysis of Streptococcusmutans glucosyltransferases, p. 209211. In J. J. Ferretti, and R. Curtiss III (ed.), Streptococcal Genetics. American Society for Microbiology, Washington, D.C..
15. LeBlanc, D. J.,, Y.-Y. M. Chen,, and L. N. Lee. 1993. Identification and characterization of a mobilization gene in the streptococcal plasmid, pVA380-l. Plasmid 30:296302.
16. LeBlanc, D. J.,, L. N. Lee,, and A. Abu-AI-Jaibat. 1992. Molecular, genetic, and functional analysis of the basic replicon of pVA380-l, a plasmid of oral streptococcal origin. Plasmid 28:130145.
17. LeBlanc, D. J.,, L. N. Lee,, and J. M. Inamine. 1991. Cloning and nucleotide base sequence analysis of a spectinomycin adenyltransferase AAD(9) determinant from Enterococcus faecalis. Antimicrob. Agents Chemother. 35:18041810.
18. Lodge, J.,, and G. R. Jacobson. 1988. Starvation-induced stimulation of sugar uptake in Streptococcus mutans is due to an effect on the activities of preexisting proteins of the phosphotransferase system. Infect. Immun. 56:25942600.
19. Loesche, W. J., 1986. Role of Streptococcus mutans in human dental decay. Microbiol. Rev. 50: 353380.
20. Lunsford, R. D.,, and F. L. Macrina. 1986. Molecular cloning and characterization of scrB, the structural gene for the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system sucrose-6-phosphate hydrolase. J. Bacteriol. 166:426434.
21. McKay, L. L.,, K. A. Baldwin,, and J. D. Efstathiou. 1976. Transductional evidence for plasmid linkage of lactose metabolism in Streptococcus lactis C2. Appl. Environ. Microbiol. 32:4552.
22. Mikx, F. H. M.,, and M. Svanberg,. 1978. Considerations about microbial interactions in relation to modification of the microflora of dental plaque, p. 109118. In B. G. Bibby, and R. J. Shem (ed.), Proceedings, Methods of Caries Prediction, special supplement to Microbial Abstracts. Information Retrieval, Inc., Washington, D.C..
23. Munro, C.,, S. M. Michalek,, and F. L. Macrina. 1991. Cariogenicity of Streptococcus mutans V403 glucosyltransferase and fructosyltransferase mutants constructed by allelic exchange. Infect. Immun. 59:23162323.
24. Powell, I. B.,, M. G. Achen,, A. J. Hillier,, and B. E. Davidson. 1988. A simple and rapid method for genetic transformation of lactic streptococci by electroporation. Appl. Environ. Microbiol. 54: 655660.
25. Poy, F.,, and G. R. Jacobson. 1990. Evidence that a low-affinity sucrose phosphotransferase activity in Streptococcus mutans GS-5 is a high-affinity trehalose uptake system. Infect. Immun. 58: 14791480.
26. Reizer, J.,, M. H. Saier, Jr.,, J. Deutscher,, F. Grenier,, J. Thompson,, and W. Henstenberg. 1988. The phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: properties, mechanism, and regulation. Crit. Rev. Microbiol. 15:297338.
27. Robeson, J. P.,, R. G. Barletta,, and R. Curtiss III. 1983. Expression of a Streptococcus mutans glucosyltransferase gene in Escherichia coli. J. Bacteriol. 153:211221.
28. Russell, R. R. B.,, J. Aduse-Opoku,, I. C. Sutcliffe,, L. Tao,, and J. J. Ferretti. 1992. A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism. J. Biol. Chem. 267:46314637.
29. Sato, S.,, and H. K. Kuramitsu. 1986. Isolation and characterization of a fructosyltransferase gene from Streptococcus mutans GS5. Infect. Immun. 52:166170.
30. Sato, Y.,, and H. K. Kuramitsu. 1988. Sequence analysis of the Steptococcus mutans scrB gene. Infect. Immun. 56:19561960.
31. Sato, Y.,, F. Poy,, G. R. Jacobson,, and H. K. Kuramitsu. 1989. Characterization and sequence analysis of the scrA gene encoding enzyme IIscr of the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system. J. Bacteriol. 171:263271.
32. Schroeder, V. A.,, S. M. Michalek,, and F. L Macrina. 1989. Biochemical characterization and evaluation of virulence of a fructosyltransferase-deficient mutant of Streptococcus mutans V403. Infect. Immun. 57:35603569.
33. Slee, A. M.,, and J. M. Tanzer. 1979. Phosphoenolpyruvate-dependent sucrose phosphotransferase activity in Streptococcus mutans NCTC 10449. Infect. Immun. 24:821828.
34. Slee, A. M.,, and J. M. Tanzer. 1980. Effect of growth conditions on sucrose phosphotransferase activity of Streptococcus mutans. Infect. Immun. 27:922927.
35. Slee, A. M.,, and J. M. Tanzer. 1982. Sucrose transport by Streptococcus mutans: evidence for multiple transport systems. Biochim. Biophys. Acta 692:415424.
36. Socransky, S. S.,, A. D. Manganielli,, D. Propas,, V. Orum,, and J. van Houte. 1977. Bacteriological studies of developing supragingival dental plaque. J. Periodontal Res. 12:90106.
37. St. Martin, E. J.,, and C. L. Wittenberger. 1979. Characterization of a phosphoenolpyruvate-dependent sucrose phosphotransferase system in Streptococcus mutans. Infect. Immun. 24:865868.
38. St. Martin, E. J.,, and C. L. Wittenberger. 1979. Regulation and function of sucrose 6-phosphate hydrolase in Streptococcus mutans. Infect. Immun. 26:487491.
39. Tanzer, J. M., 1992. Microbiology of dental caries, p. 377424. In J. Slots, and M. Taubman (ed.), Contemporary Oral Microbiology and Immunology. Mosby Year Book, St. Louis.
40. Tanzer, J. M.,, A. T. Brown,, and M. F. Mclnerney. 1973. Identification, preliminary characterization, and evidence for regulation of invertase in Streptococcus mutans. J. Bacteriol. 116:192202.
41. Tao, L.,, I. C. Sutcliffe,, R. R. B. Russell,, and J. J. Ferretti. 1993. Transport of sugars, including sucrose, by the msm transport system of Streptococcus mutans. J. Dent. Res. 72:13861390.
42. Trieu-Cuot, P.,, and P. Courvalin. 1983. Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3'-5'-aminoglycoside phosphotransferase type III. Gene 23:331341.
43. Yamashita, Y.,, N. Hanada,, and T. Takehara. 1989. Purification of a fourth glucosyltransferase from Streptococcus sobrinus. J. Bacteriol. 171:62656270.

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