Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1988 Aug;56(8):1864–1872. doi: 10.1128/iai.56.8.1864-1872.1988

Specificity of the glucan-binding lectin of Streptococcus cricetus.

D Drake 1, K G Taylor 1, A S Bleiweis 1, R J Doyle 1
PMCID: PMC259494  PMID: 3397177

Abstract

The specificity of the glucan-binding lectin (GBL) of Streptococcus cricetus AHT was determined. Examination of the kinetics of aggregation of cell suspensions with glucans containing various percentages of alpha-1,6, alpha-1,4, alpha-1,3, and alpha-1,2 anomeric linkages revealed that only glucans with at least 80% alpha-1,6 linkages promoted strong aggregation. Moreover, only linear glucans with molecular weights greater than 5 X 10(5) were capable of causing rapid aggregation of the bacteria. The lectin was observed to be present on S. cricetus strains, on Streptococcus sobrinus, and on several Streptococcus mutants strains. Preincubation of suspensions of S. cricetus AHT with glucan T10 (molecular weight of 10,000) before the addition of high-molecular-weight glucan resulted in competitive inhibition in a concentration-dependent manner. Inhibition was achieved also with isomaltopentaose, isomaltohexaose, and isomaltooctaose, but at higher concentrations than glucan T10. In contrast, no inhibition was observed with maltoheptaose, providing additional evidence for the specificity of GBL. Treatment of suspensions of S. cricetus AHT with trypsin before and after aggregation with high-molecular-weight glucan revealed a substantial level of protection of GBL when in a bound state. Collectively, these results indicated that GBL has an absolute affinity for glucans rich in alpha-1,6 linkages and possesses an active site which recognizes internal sequences and accommodates isomaltosaccharides of at least nine residues. This unusual specificity may contribute to the colonization of S. cricetus, S. sobrinus, and S. mutans in glucan-containing plaque in the oral cavity.

Full text

PDF
1864

Images in this article

1867Image
on p.1867

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ayakawa G. Y., Boushell L. W., Crowley P. J., Erdos G. W., McArthur W. P., Bleiweis A. S. Isolation and characterization of monoclonal antibodies specific for antigen P1, a major surface protein of mutans streptococci. Infect Immun. 1987 Nov;55(11):2759–2767. doi: 10.1128/iai.55.11.2759-2767.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Crowley P. J., Fischlschweiger W., Coleman S. E., Bleiweis A. S. Intergeneric bacterial coaggregations involving mutans streptococci and oral actinomyces. Infect Immun. 1987 Nov;55(11):2695–2700. doi: 10.1128/iai.55.11.2695-2700.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Curtiss R., 3rd Genetic analysis of Streptococcus mutans virulence. Curr Top Microbiol Immunol. 1985;118:253–277. doi: 10.1007/978-3-642-70586-1_14. [DOI] [PubMed] [Google Scholar]
  4. Freedman M. L., Guggenheim B. Dextran-induced aggregation in a mutant of Streptococcus sobrinus 6715-13. Infect Immun. 1983 Jul;41(1):264–274. doi: 10.1128/iai.41.1.264-274.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Freedman M. L., Tanzer J. M. Dissociation of plaque formation from glucan-induced agglutination in mutants of Streptococcus mutans. Infect Immun. 1974 Jul;10(1):189–196. doi: 10.1128/iai.10.1.189-196.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gibbons R. J. Adherent interactions which may affect microbial ecology in the mouth. J Dent Res. 1984 Mar;63(3):378–385. doi: 10.1177/00220345840630030401. [DOI] [PubMed] [Google Scholar]
  7. Gibbons R. J., Fitzgerald R. J. Dextran-induced agglutination of Streptococcus mutans, and its potential role in the formation of microbial dental plaques. J Bacteriol. 1969 May;98(2):341–346. doi: 10.1128/jb.98.2.341-346.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gibbons R. J., Houte J. V. Bacterial adherence in oral microbial ecology. Annu Rev Microbiol. 1975;29:19–44. doi: 10.1146/annurev.mi.29.100175.000315. [DOI] [PubMed] [Google Scholar]
  9. Gibbons R. J., Nygaard M. Synthesis of insoluble dextran and its significance in the formation of gelatinous deposits by plaque-forming streptococci. Arch Oral Biol. 1968 Oct;13(10):1249–1262. doi: 10.1016/0003-9969(68)90081-2. [DOI] [PubMed] [Google Scholar]
  10. Gold O. G., Jordan H. V., Van Houte J. A selective medium for Streptococcus mutans. Arch Oral Biol. 1973 Nov;18(11):1357–1364. doi: 10.1016/0003-9969(73)90109-x. [DOI] [PubMed] [Google Scholar]
  11. Guggenheim B., Schroeder H. E. Biochemical and morphological aspects of extracellular polysaccharides produced by cariogenic streptococci. Helv Odontol Acta. 1967 Oct;11(2):131–152. [PubMed] [Google Scholar]
  12. Hamada S., Slade H. D. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol Rev. 1980 Jun;44(2):331–384. doi: 10.1128/mr.44.2.331-384.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Janda W. M., Kuramitsu H. K. Properties of a variant of Streptococcus mutans altered in its ability to interact with glucans. Infect Immun. 1977 May;16(2):575–586. doi: 10.1128/iai.16.2.575-586.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kelstrup J., Funder-Nielsen T. D. Adhesion of dextran to Streptococcus mutans. J Gen Microbiol. 1974 Apr;81(2):485–489. doi: 10.1099/00221287-81-2-485. [DOI] [PubMed] [Google Scholar]
  15. Kuramitsu H. K. Adherence of Streptococcus mutans to dextran synthesized in the presence of extracellular dextransucrase. Infect Immun. 1974 Apr;9(4):764–765. doi: 10.1128/iai.9.4.764-765.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Landale E. C., McCabe M. M. Characterization by affinity electrophoresis of an alpha-1,6-glucan-binding protein from Streptococcus sobrinus. Infect Immun. 1987 Dec;55(12):3011–3016. doi: 10.1128/iai.55.12.3011-3016.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Liljemark W. F., Gibbons R. J. Proportional distribution and relative adherence of Streptococcus miteor (mitis) on various surfaces in the human oral cavity. Infect Immun. 1972 Nov;6(5):852–859. doi: 10.1128/iai.6.5.852-859.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. McCabe M. M., Hamelik R. M. Multiple forms of dextran-binding proteins from Streptococcus mutans. Adv Exp Med Biol. 1978;107:749–759. doi: 10.1007/978-1-4684-3369-2_84. [DOI] [PubMed] [Google Scholar]
  19. McCabe M. M., Hamelik R. M., Smith E. E. Purification of dextran-binding protein from cariogenic Streptococcus mutans. Biochem Biophys Res Commun. 1977 Sep 9;78(1):273–278. doi: 10.1016/0006-291x(77)91250-5. [DOI] [PubMed] [Google Scholar]
  20. McCabe M. M., Smith E. E. Relationship between cell-bound dextransucrase and the agglutination of Streptococcus mutans. Infect Immun. 1975 Sep;12(3):512–520. doi: 10.1128/iai.12.3.512-520.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Michalek S. M., McGhee J. R., Navia J. M. Virulence of Streptococcus mutans: a sensitive method for evaluating cariogenicity in young gnotobiotic rats. Infect Immun. 1975 Jul;12(1):69–75. doi: 10.1128/iai.12.1.69-75.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Michalek S. M., Shiota T., Ikeda T., Navia J. M., McGhee J. R. Virulence of Streptococcus mutans: biochemical and pathogenic characteristics of mutant isolates. Proc Soc Exp Biol Med. 1975 Nov;150(2):498–502. doi: 10.3181/00379727-150-39064. [DOI] [PubMed] [Google Scholar]
  23. Mooser G., Shur D., Lyou M., Watanabe C. Kinetic studies on dextransucrase from the cariogenic oral bacterium Streptococcus mutans. J Biol Chem. 1985 Jun 10;260(11):6907–6915. [PubMed] [Google Scholar]
  24. Mooser G., Wong C. Isolation of a glucan-binding domain of glucosyltransferase (1,6-alpha-glucan synthase) from Streptococcus sobrinus. Infect Immun. 1988 Apr;56(4):880–884. doi: 10.1128/iai.56.4.880-884.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Murchison H., Larrimore S., Curtiss R., 3rd Isolation and characterization of Streptococcus mutans mutants defective in adherence and aggregation. Infect Immun. 1981 Dec;34(3):1044–1055. doi: 10.1128/iai.34.3.1044-1055.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Olson G. A. Dextran receptors as immunogens in caries prophylaxis. Adv Exp Med Biol. 1978;107:771–781. doi: 10.1007/978-1-4684-3369-2_87. [DOI] [PubMed] [Google Scholar]
  27. Olson G. A., Guggenheim B., Small P. A., Jr Antibody-mediated inhibition of dextran-sucrose-induced agglutination of Streptococcus mutans. Infect Immun. 1974 Feb;9(2):273–278. doi: 10.1128/iai.9.2.273-278.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Russell R. R., Coleman D., Dougan G. Expression of a gene for glucan-binding protein from Streptococcus mutans in Escherichia coli. J Gen Microbiol. 1985 Feb;131(2):295–299. doi: 10.1099/00221287-131-2-295. [DOI] [PubMed] [Google Scholar]
  29. Russell R. R., Donald A. C., Douglas C. W. Fructosyltransferase activity of a glucan-binding protein from Streptococcus mutans. J Gen Microbiol. 1983 Oct;129(10):3243–3250. doi: 10.1099/00221287-129-10-3243. [DOI] [PubMed] [Google Scholar]
  30. Russell R. R. Glucan-binding proteins of Streptococcus mutans serotype c. J Gen Microbiol. 1979 May;112(1):197–201. doi: 10.1099/00221287-112-1-197. [DOI] [PubMed] [Google Scholar]
  31. Staat R. H., Langley S. D., Doyle R. J. Streptococcus mutans adherence: presumptive evidence for protein-mediated attachment followed by glucan-dependent cellular accumulation. Infect Immun. 1980 Feb;27(2):675–681. doi: 10.1128/iai.27.2.675-681.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Van Houte J., Gibbons R. J., Pulkkinen A. J. Adherence as an ecological determinant for streptococci in the human mouth. Arch Oral Biol. 1971 Oct;16(10):1131–1141. doi: 10.1016/0003-9969(71)90042-2. [DOI] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES