Skip to main content
Infection and Immunity logoLink to Infection and Immunity
. 1990 Jul;58(7):2276–2282. doi: 10.1128/iai.58.7.2276-2282.1990

Cross-reactivity between the immunodominant determinant of the antigen I component of Streptococcus sobrinus SpaA protein and surface antigens from other members of the Streptococcus mutans group.

R M Goldschmidt 1, R Curtiss 3rd 1
PMCID: PMC258808  PMID: 1694822

Abstract

Most members of the Streptococcus mutans group of microorganisms specify a major cell surface-associated protein, SpaA, that is defined by its antigenic properties. The region of the spaA gene from Streptococcus sobrinus 6715 encoding the immunodominant determinant of the major antigenic component (antigen I) of the SpaA protein has recently been characterized. This study examined whether recognition of the immunodominant determinant is independent of the immunized animal host and whether antibodies elicited by the immunodominant determinant cross-react with cell surface proteins from S. mutans of various serotypes. Mouse and rabbit antisera to the undenatured SpaA protein reacted similarly both with the immunodominant determinant and with other antigenic structures of the protein in Western immunoblots with SpaA polypeptides that were specified by spaA gene fragments expressed in recombinant Escherichia coli. This suggests that the antibody responses of inbred and outbred animals were similar. Furthermore, antibodies raised against both the S. sobrinus SpaA immunodominant determinant expressed by recombinant E. coli and the purified protein from S. sobrinus displayed similar strain specificities and protein band profiles towards cells surface proteins from S. mutans of various serotypes in immunodot and Western blot analyses, respectively. This suggests that for S. sobrinus serotype g, the immune response against the SpaA protein is governed by the immunodominant determinant of antigen I. In addition, it indicates that the SpaA protein domain containing the immunodominant determinant overlaps the domain conferring cross-reactivity to cell surface proteins of S. mutans of various serotypes.

Full text

PDF
2276

Images in this article

Selected References

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

  1. Amann E., Brosius J. "ATG vectors' for regulated high-level expression of cloned genes in Escherichia coli. Gene. 1985;40(2-3):183–190. doi: 10.1016/0378-1119(85)90041-1. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. Babu J. P., Beachey E. H., Hasty D. L., Simpson W. A. Isolation and characterization of a 60-kilodalton salivary glycoprotein with agglutinating activity against strains of Streptococcus mutans. Infect Immun. 1986 Feb;51(2):405–413. doi: 10.1128/iai.51.2.405-413.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Barrett J. F., Barrett T. A., Curtiss R., 3rd Purification and partial characterization of the multicomponent dextranase complex of Streptococcus sobrinus and cloning of the dextranase gene. Infect Immun. 1987 Mar;55(3):792–802. doi: 10.1128/iai.55.3.792-802.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Beighton D., Russell R. R., Hayday H. The isolation of characterization of Streptococcus mutans serotype h from dental plaque of monkeys (Macaca fascicularis). J Gen Microbiol. 1981 Jun;124(2):271–279. doi: 10.1099/00221287-124-2-271. [DOI] [PubMed] [Google Scholar]
  6. Brack C. M., Reynolds E. C. Characterization of a rat salivary sialoglycoprotein complex which agglutinates Streptococcus mutans. Infect Immun. 1987 May;55(5):1264–1273. doi: 10.1128/iai.55.5.1264-1273.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chang A. C., Cohen S. N. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol. 1978 Jun;134(3):1141–1156. doi: 10.1128/jb.134.3.1141-1156.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Curtiss R., 3rd 1984 Kreshover lecture. Genetic analysis of Streptococcus mutans virulence and prospects for an anticaries vaccine. J Dent Res. 1986 Aug;65(8):1034–1045. doi: 10.1177/00220345860650080101. [DOI] [PubMed] [Google Scholar]
  9. Curtiss R., 3rd, Goldschmidt R. M., Fletchall N. B., Kelly S. M. Avirulent Salmonella typhimurium delta cya delta crp oral vaccine strains expressing a streptococcal colonization and virulence antigen. Vaccine. 1988 Apr;6(2):155–160. doi: 10.1016/s0264-410x(88)80020-3. [DOI] [PubMed] [Google Scholar]
  10. Czerkinsky C., Russell M. W., Lycke N., Lindblad M., Holmgren J. Oral administration of a streptococcal antigen coupled to cholera toxin B subunit evokes strong antibody responses in salivary glands and extramucosal tissues. Infect Immun. 1989 Apr;57(4):1072–1077. doi: 10.1128/iai.57.4.1072-1077.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Demuth D. R., Davis C. A., Corner A. M., Lamont R. J., Leboy P. S., Malamud D. Cloning and expression of a Streptococcus sanguis surface antigen that interacts with a human salivary agglutinin. Infect Immun. 1988 Sep;56(9):2484–2490. doi: 10.1128/iai.56.9.2484-2490.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Forester H., Hunter N., Knox K. W. Characteristics of a high molecular weight extracellular protein of Streptococcus mutans. J Gen Microbiol. 1983 Sep;129(9):2779–2788. doi: 10.1099/00221287-129-9-2779. [DOI] [PubMed] [Google Scholar]
  13. Gibbons R. J., Cohen L., Hay D. I. Strains of Streptococcus mutans and Streptococcus sobrinus attach to different pellicle receptors. Infect Immun. 1986 May;52(2):555–561. doi: 10.1128/iai.52.2.555-561.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Goldschmidt R. M., Thoren-Gordon M., Curtiss R., 3rd Regions of the Streptococcus sobrinus spaA gene encoding major determinants of antigen I. J Bacteriol. 1990 Jul;172(7):3988–4001. doi: 10.1128/jb.172.7.3988-4001.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. Helfman D. M., Feramisco J. R., Fiddes J. C., Thomas G. P., Hughes S. H. Identification of clones that encode chicken tropomyosin by direct immunological screening of a cDNA expression library. Proc Natl Acad Sci U S A. 1983 Jan;80(1):31–35. doi: 10.1073/pnas.80.1.31. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Holt R. G., Abiko Y., Saito S., Smorawinska M., Hansen J. B., Curtiss R., 3rd Streptococcus mutans genes that code for extracellular proteins in Escherichia coli K-12. Infect Immun. 1982 Oct;38(1):147–156. doi: 10.1128/iai.38.1.147-156.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [DOI] [PubMed] [Google Scholar]
  19. Laemmli U. K., Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973 Nov 15;80(4):575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  20. Lee S. F., Progulske-Fox A., Bleiweis A. S. Molecular cloning and expression of a Streptococcus mutans major surface protein antigen, P1 (I/II), in Escherichia coli. Infect Immun. 1988 Aug;56(8):2114–2119. doi: 10.1128/iai.56.8.2114-2119.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Lehner T., Russell M. W., Caldwell J., Smith R. Immunization with purified protein antigens from Streptococcus mutans against dental caries in rhesus monkeys. Infect Immun. 1981 Nov;34(2):407–415. doi: 10.1128/iai.34.2.407-415.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Manoil C., Beckwith J. TnphoA: a transposon probe for protein export signals. Proc Natl Acad Sci U S A. 1985 Dec;82(23):8129–8133. doi: 10.1073/pnas.82.23.8129. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Niven C. F., Smiley K. L., Sherman J. M. The Hydrolysis of Arginine by Streptococci. J Bacteriol. 1942 Jun;43(6):651–660. doi: 10.1128/jb.43.6.651-660.1942. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Ogier J. A., Klein J. P., Sommer P., Frank R. M. Identification and preliminary characterization of saliva-interacting surface antigens of Streptococcus mutans by immunoblotting, ligand blotting, and immunoprecipitation. Infect Immun. 1984 Jul;45(1):107–112. doi: 10.1128/iai.45.1.107-112.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Ogundipe J. O., Holt R. G. Molecular and immunochemical characterization of recombinant Escherichia coli containing the spaA gene region of Streptococcus sobrinus. Infect Immun. 1989 Jul;57(7):1906–1915. doi: 10.1128/iai.57.7.1906-1915.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Russell M. W., Bergmeier L. A., Zanders E. D., Lehner T. Protein antigens of Streptococcus mutans: purification and properties of a double antigen and its protease-resistant component. Infect Immun. 1980 May;28(2):486–493. doi: 10.1128/iai.28.2.486-493.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Russell M. W., Mansson-Rahemtulla B. Interaction between surface protein antigens of Streptococcus mutans and human salivary components. Oral Microbiol Immunol. 1989 Jun;4(2):106–111. doi: 10.1111/j.1399-302x.1989.tb00107.x. [DOI] [PubMed] [Google Scholar]
  29. Russell R. R. Distribution of cross-reactive antigens A and B in Streptococcus mutans and other oral streptococci. J Gen Microbiol. 1980 Jun;118(2):383–388. doi: 10.1099/00221287-118-2-383. [DOI] [PubMed] [Google Scholar]
  30. Russell R. R. Wall-associated protein antigens of Streptococcus mutans. J Gen Microbiol. 1979 Sep;114(1):109–115. doi: 10.1099/00221287-114-1-109. [DOI] [PubMed] [Google Scholar]
  31. Shklair I. L., Keene H. J. A biochemical scheme for the separation of the five varieties of Streptococcus mutans. Arch Oral Biol. 1974 Nov;19(11):1079–1081. doi: 10.1016/0003-9969(74)90099-5. [DOI] [PubMed] [Google Scholar]
  32. Smith R., Lehner T., Beverley P. C. Characterization of monoclonal antibodies to Streptococcus mutans antigenic determinants I/II, I, II, and III and their serotype specificities. Infect Immun. 1984 Oct;46(1):168–175. doi: 10.1128/iai.46.1.168-175.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Sommer P., Bruyère T., Ogier J. A., Garnier J. M., Jeltsch J. M., Klein J. P. Cloning of the saliva-interacting protein gene from Streptococcus mutans. J Bacteriol. 1987 Nov;169(11):5167–5173. doi: 10.1128/jb.169.11.5167-5173.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Takahashi I., Okahashi N., Sasakawa C., Yoshikawa M., Hamada S., Koga T. Homology between surface protein antigen genes of Streptococcus sobrinus and Streptococcus mutans. FEBS Lett. 1989 Jun 5;249(2):383–388. doi: 10.1016/0014-5793(89)80664-7. [DOI] [PubMed] [Google Scholar]
  35. Terleckyj B., Willett N. P., Shockman G. D. Growth of several cariogenic strains of oral streptococci in a chemically defined medium. Infect Immun. 1975 Apr;11(4):649–655. doi: 10.1128/iai.11.4.649-655.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. 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