Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1988 Jan;56(1):64–70. doi: 10.1128/iai.56.1.64-70.1988

Streptococcus sanguis surface antigens and their interactions with saliva.

R J Lamont 1, B Rosan 1, G M Murphy 1, C T Baker 1
PMCID: PMC259235  PMID: 3335410

Abstract

Saliva-binding molecules of Streptococcus sanguis and their receptors were investigated. Streptococcal cell surfaces were extracted with a barbital buffer and examined immunochemically. Strains G9B and Blackburn, which adhere specifically to saliva-coated hydroxyapatite via immunologically related adhesins, possess 80-, 62-, and 52-kilodalton (kDa), and 52-, 42-, and 29-kDa polypeptides, respectively, which correlate with adhesion to saliva-coated hydroxyapatite. Nonadherent strains Adh- and M-5 lack these antigens. In an immunoblot overlay, the putative adhesins bound to a 73-kDa receptor present in submandibular saliva but not in parotid saliva. G9B also contains a 160-kDa surface protein which bound to an unidentified receptor in both submandibular and parotid saliva samples. Blackburn barbital-extracted components bound to 78- and 70-kDa receptors in parotid saliva. These bacterial-salivary interactions may be important in the regulation of oral ecology.

Full text

PDF
64

Images in this article

66Image
on p.66
66Image
on p.66
66Image
on p.66
67Image
on p.67
67Image
on p.67
67Image
on p.67
67Image
on p.67
68Image
on p.68

Selected References

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

  1. Appelbaum B., Golub E., Holt S. C., Rosan B. In vitro studies of dental plaque formation: adsorption of oral streptococci to hydroxyaptite. Infect Immun. 1979 Aug;25(2):717–728. doi: 10.1128/iai.25.2.717-728.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Appelbaum B., Rosan B. Cell surface proteins of oral streptococci. Infect Immun. 1984 Oct;46(1):245–250. doi: 10.1128/iai.46.1.245-250.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Babu J. P., Beachey E. H., Simpson W. A. Inhibition of the interaction of Streptococcus sanguis with hexadecane droplets by 55- and 60-kilodalton hydrophobic proteins of human saliva. Infect Immun. 1986 Aug;53(2):278–284. doi: 10.1128/iai.53.2.278-284.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bergey E. J., Levine M. J., Reddy M. S., Bradway S. D., Al-Hashimi I. Use of the photoaffinity cross-linking agent N-hydroxysuccinimidyl-4-azidosalicylic acid to characterize salivary-glycoprotein-bacterial interactions. Biochem J. 1986 Feb 15;234(1):43–48. doi: 10.1042/bj2340043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  6. Carlsson J. A numerical taxonomic study of human oral streptococci. Odontol Revy. 1968;19(2):137–160. [PubMed] [Google Scholar]
  7. Carlsson J., Grahnén H., Jonsson G., Wikner S. Establishment of Streptococcus sanguis in the mouths of infants. Arch Oral Biol. 1970 Dec;15(12):1143–1148. doi: 10.1016/0003-9969(70)90005-1. [DOI] [PubMed] [Google Scholar]
  8. Clark W. B., Gibbons R. J. Influence of salivary components and extracellular polysaccharide synthesis from sucrose on the attachment of Streptococcus mutans 6715 to hydroxyapatite surfaces. Infect Immun. 1977 Nov;18(2):514–523. doi: 10.1128/iai.18.2.514-523.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Cowan M. M., Taylor K. G., Doyle R. J. Kinetic analysis of Streptococcus sanguis adhesion to artificial pellicle. J Dent Res. 1986 Oct;65(10):1278–1283. doi: 10.1177/00220345860650101501. [DOI] [PubMed] [Google Scholar]
  10. De Jong M. H., Van der Hoeven J. S. The growth of oral bacteria on saliva. J Dent Res. 1987 Feb;66(2):498–505. doi: 10.1177/00220345870660021901. [DOI] [PubMed] [Google Scholar]
  11. Eifert R., Rosan B., Golub E. Optimization of an hydroxyapatite adhesion assay for Streptococcus sanguis. Infect Immun. 1984 May;44(2):287–291. doi: 10.1128/iai.44.2.287-291.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Elder B. L., Fives-Taylor P. Characterization of monoclonal antibodies specific for adhesion: isolation of an adhesin of Streptococcus sanguis FW213. Infect Immun. 1986 Nov;54(2):421–427. doi: 10.1128/iai.54.2.421-427.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Fachon-Kalweit S., Elder B. L., Fives-Taylor P. Antibodies that bind to fimbriae block adhesion of Streptococcus sanguis to saliva-coated hydroxyapatite. Infect Immun. 1985 Jun;48(3):617–624. doi: 10.1128/iai.48.3.617-624.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Facklam R. R. Physiological differentiation of viridans streptococci. J Clin Microbiol. 1977 Feb;5(2):184–201. doi: 10.1128/jcm.5.2.184-201.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hogg S. D., Embery G. Blood-group-reactive glycoprotein from human saliva interacts with lipoteichoic acid on the surface of Streptococcus sanguis cells. Arch Oral Biol. 1982;27(3):261–268. doi: 10.1016/0003-9969(82)90060-7. [DOI] [PubMed] [Google Scholar]
  16. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  17. Levine M. J., Herzberg M. C., Levine M. S., Ellison S. A., Stinson M. W., Li H. C., van Dyke T. Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans. Infect Immun. 1978 Jan;19(1):107–115. doi: 10.1128/iai.19.1.107-115.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Liljemark W. F., Bloomquist C. G. Isolation of a protein-containing cell surface component from Streptococcus sanguis which affects its adherence to saliva-coated hydroxyapatite. Infect Immun. 1981 Nov;34(2):428–434. doi: 10.1128/iai.34.2.428-434.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. MacKay B. J., Denepitiya L., Iacono V. J., Krost S. B., Pollock J. J. Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans. Infect Immun. 1984 Jun;44(3):695–701. doi: 10.1128/iai.44.3.695-701.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. McBride B. C., Gisslow M. T. Role of sialic acid in saliva-induced aggregation of Streptococcus sanguis. Infect Immun. 1977 Oct;18(1):35–40. doi: 10.1128/iai.18.1.35-40.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Morris E. J., Ganeshkumar N., McBride B. C. Cell surface components of Streptococcus sanguis: relationship to aggregation, adherence, and hydrophobicity. J Bacteriol. 1985 Oct;164(1):255–262. doi: 10.1128/jb.164.1.255-262.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Morris E. J., Ganeshkumar N., Song M., McBride B. C. Identification and preliminary characterization of a Streptococcus sanguis fibrillar glycoprotein. J Bacteriol. 1987 Jan;169(1):164–171. doi: 10.1128/jb.169.1.164-171.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Morris E. J., McBride B. C. Adherence of Streptococcus sanguis to saliva-coated hydroxyapatite: evidence for two binding sites. Infect Immun. 1984 Feb;43(2):656–663. doi: 10.1128/iai.43.2.656-663.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Murray P. A., Levine M. J., Tabak L. A., Reddy M. S. Specificity of salivary-bacterial interactions: II. Evidence for a lectin on Streptococcus sanguis with specificity for a NeuAc alpha 2, 3Ga1 beta 1, 3Ga1NAc sequence. Biochem Biophys Res Commun. 1982 May 31;106(2):390–396. doi: 10.1016/0006-291x(82)91122-6. [DOI] [PubMed] [Google Scholar]
  25. Nagata K., Nakao M., Shibata S., Shizukuishi S., Nakamura R., Tsunemitsu A. Purification and characterization of galactosephilic component present on the cell surfaces of Streptococcus sanguis ATCC 10557. J Periodontol. 1983 Mar;54(3):163–172. doi: 10.1902/jop.1983.54.3.163. [DOI] [PubMed] [Google Scholar]
  26. Nesbitt W. E., Doyle R. J., Taylor K. G. Hydrophobic interactions and the adherence of Streptococcus sanguis to hydroxylapatite. Infect Immun. 1982 Nov;38(2):637–644. doi: 10.1128/iai.38.2.637-644.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Robinovitch M. R., Malamud D., Rosan B., Golub E. E., Lancy P., Jr Identification of a Streptococcus sanguis receptor for salivary agglutinins. J Dent Res. 1986 Feb;65(2):98–104. doi: 10.1177/00220345860650021901. [DOI] [PubMed] [Google Scholar]
  28. Rosan B. Antigens of Streptococcus sanguis. Infect Immun. 1973 Feb;7(2):205–211. doi: 10.1128/iai.7.2.205-211.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Rosan B., Appelbaum B., Golub E., Malamud D., Mandel I. D. Enhanced saliva-mediated bacterial aggregation and decreased bacterial adhesion in caries-resistant versus caries-susceptible individuals. Infect Immun. 1982 Dec;38(3):1056–1059. doi: 10.1128/iai.38.3.1056-1059.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Rosan B., Malamud D., Appelbaum B., Golub E. Characteristic differences between saliva-dependent aggregation and adhesion of streptococci. Infect Immun. 1982 Jan;35(1):86–90. doi: 10.1128/iai.35.1.86-90.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Rundegren J. Calcium-dependent salivary agglutinin with reactivity to various oral bacterial species. Infect Immun. 1986 Jul;53(1):173–178. doi: 10.1128/iai.53.1.173-178.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Socransky S. S., Manganiello A. D., Propas D., Oram V., van Houte J. Bacteriological studies of developing supragingival dental plaque. J Periodontal Res. 1977 Mar;12(2):90–106. doi: 10.1111/j.1600-0765.1977.tb00112.x. [DOI] [PubMed] [Google Scholar]
  33. Stinson M. W., Levine M. J., Cavese J. M., Prakobphol A., Murray P. A., Tabak L. A., Reddy M. S. Adherence of Streptococcus sanguis to salivary mucin bound to glass. J Dent Res. 1982 Dec;61(12):1390–1393. doi: 10.1177/00220345820610120101. [DOI] [PubMed] [Google Scholar]
  34. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES