1887

Abstract

A genomic library of , strain G9B, was constructed and expressed in using a λgt11 expression vector. The amplified library was probed with polyclonal anti-G9B IgG and 13 antigen-positive clones were isolated. A lysate of one clone, designated PP39, absorbed the adhesion-inhibitory activity of anti-G9B IgG. This clone contained an insert of approximately 2000 bp and expressed unique 200 and 53 kDa proteins that reacted with monospecific anti-adhesin antibody. The 200 kDa protein also reacted with anti--galactosidase IgG, indicating that it is a fusion protein of which 84 kDa represents the streptococcal adhesin. The 84 and 53 kDa proteins are similar in size to the major polypeptides in a streptococcal antigen complex which is associated with the adhesion of G9B to salivacoated hydroxyapatite. The 53 kDa fragment may result from post-translational cleavage of the recombinant polypeptide.

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1989-03-01
2024-12-05
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References

  1. Bergey E.J., Levine M.J., Reddy M.S., Bradway S.D., Al-Hashimi I. 1986; Use of the photoaffinity cross-linking agent A'-hydroxysuccini- midyl-4-azidosalicylic acid to characterize salivary- glycoprotein-bacterial interactions. Biochemical Journal 234:43–48
    [Google Scholar]
  2. Cowan M.M., Taylor K.G., Doyle R.J. 1986; Kinetic analysis of Streptococcus sanguis adhesion to artificial pellicle. Journal of Dental Research 65:1278–1283
    [Google Scholar]
  3. Cowan M.M., Taylor K.G., Doyle R.J. 1987; Energetics of the initial phase of adhesion of Streptococcus sanguis to hydroxylapatite. Journal of Bacteriology 169:2995–3000
    [Google Scholar]
  4. Curtiss R. III Murchison H.M., Nesbitt W.E., Barrett J.F., Michalek S.M. 1985; Use of mutants and gene cloning to identify and character-ize colonization mechanisms of Streptococcus mutants . In Molecular Basis of Oral Microbial Adhesion pp. 187–193 Mergenhagen S.E., Rosan B. Edited by Washington, DC: American Society for Microbiology;
    [Google Scholar]
  5. Douglas C.W.I., Russell R.R.B. 1984; Effect of specific antisera upon Streptococcus mutans adherence to saliva-coated hydroxyapatite. FEMS Microbiology Letters 25:211–214
    [Google Scholar]
  6. Doyle R.J., Nesbitt W.E., Taylor K.G. 1982; On the mechanism of adherence of Streptococcus sanguis to hydroxylapatite. FEMS Microbiology Letters 15:1–5
    [Google Scholar]
  7. Eifert R., Rosan B., Golub E. 1984; Optimization of an hydroxyapatite adhesion assay for Streptococcus sanguis . Infection and Immunity 44:287–291
    [Google Scholar]
  8. Elder B.L., Fives-Taylor P. 1986; Characterization of monoclonal antibodies specific for adhesion: isolation of an adhesin of Streptococcus sanguis FW213. Infection and Immunity 54:421–427
    [Google Scholar]
  9. Fachon-Kalweit S., Elder B.L., Fives-Taylor P. 1985; Antibodies that bind to fimbriae block adhesion of Streptococcus sanguis to saliva-coated hydroxyapatite. Infection and Immunity 48:617–624
    [Google Scholar]
  10. Facklam R.R. 1977; Physiological differentiation of viridans streptococci. Journal of Clinical Microbiology 5:184–201
    [Google Scholar]
  11. Fives-Taylor P. 1982; Isolation and characterization of a Streptococcus sanguis FW213 mutant nonadherent to saliva-coated hydroxyapatite beads. In Microbiology-1982 pp. Schlessinger D. Edited by Washington, DC: American Society for Microbiology;
    [Google Scholar]
  12. Fives-Taylor P.M., Thompson D.W. 1985; surface properties of Streptococcus sanguis FW213 mutants nonadherent to saliva-coated hydroxyapatite. Infection and Immunity 47:752–759
    [Google Scholar]
  13. Fives-Taylor P.M., Macrina F.L., Pritchard T., Peene S.S. 1987; Expression of Streptococcus sanguis antigens in Escherichia coli: cloning of a structural gene for adhesion fimbriae. Infection and Immunity 55:123–128
    [Google Scholar]
  14. Ganeshkumar N., Song M., Mcbride B.C. 1988; Cloning of a Streptococcus sanguis adhesin which mediates binding to saliva-coated hydroxyapatite. Infection and Immunity 56:1150–1157
    [Google Scholar]
  15. Gibbons R.J., Van Houte J. 1971; Selective bacterial adherence to oral epithelial surfaces and its role as an ecological determinant. Infection and Immunity 3:567–573
    [Google Scholar]
  16. Gibbons R.J., Moreno E.C., Etherden I. 1983; Concentration-dependent multiple binding sites on saliva-treated hydroxyapatite for Streptococcus sanguis . Infection and Immunity 39:280–289
    [Google Scholar]
  17. Hamada S., Slade H.D. 1980; Biology, immunology, and cariogenicity of Streptococcus mutans . Microbiological Reviews 44:331–384
    [Google Scholar]
  18. Handley P.S., Carter P.L., Wyatt J.E., Hesketh L.M. 1985; surface structures (peritri- chous fibrils and tufts of fibrils) found on Streptococcus sanguis strains may be related to their ability to coaggregate with other oral genera. Infection and Immunity 41:217–227
    [Google Scholar]
  19. Laemmli U.K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature; London: 227680–685
    [Google Scholar]
  20. Lamont R.J., Rosan B., Murphy G.M., Baker C.T. 1988a; Streptococcus sanguis surface antigens and their interactions with saliva. Infection and Immunity 56:64–70
    [Google Scholar]
  21. Lamont R.J., Rosan B., Baker C.T., Murphy G.M. 1988b; Characterization of an adhesin antigen of Streptococcus sanguis G9B . Infection and Immunity 56:2417–2423
    [Google Scholar]
  22. Liljemark W.F., Bloomquist C.G. 1981; Isolation of a protein-containing cell surface component from Streptococcus sanguis which affects its adherence to saliva-coated hydroxyapatite. Infection and Immunity 34:428–434
    [Google Scholar]
  23. Maniatis T., Fritsch E.F., Sambrook J. 1982 Molecular Cloning: a Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  24. Morris E.J., Mcbride B.C. 1984; Adherence of Streptococcus sanguis to saliva-coated hydroxyapatite: evidence for two binding sites. Infection and Immunity 43:656–663
    [Google Scholar]
  25. Morris E.J., Ganeshkumar N., Mcbride B.C. 1985; Cell surface components of Streptococcus sanguis: relationship to aggregation, adherence, and hydrophobicity. Journal of Bacteriology 164:255–262
    [Google Scholar]
  26. Morris E.J., Ganeshkumar N., Song M., Mcbride B.C. 1987; Identification and preliminary characterization of a Streptococcus sanguis fibrillar glycoprotein. Journal of Bacteriology 169:164–171
    [Google Scholar]
  27. Ogier J.A., Klein J.P., Sommer P., Frank R.M. 1984; Identification and preliminary characterization of saliva-interacting surface antigens of Streptococcus mutans by immunoblotting, ligand blotting, and immunoprecipitation. Infection and Immunity 45:107–112
    [Google Scholar]
  28. Olmsted J.B. 1981; Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples. Journal of Biological Chemistry 256:11955–11957
    [Google Scholar]
  29. Rosan B. 1973; Antigens of Streptococcus sanguis . Infection and Immunity 7205–211
    [Google Scholar]
  30. Rosan B. 1976; Relationship of cell wall composition of group H streptococci andStreptococcus sanguisto their serological properties. Infection and Immunity 13:1144–1153
    [Google Scholar]
  31. Rosan B. 1978; A comparison of the phenol water and Rantz and Randall teichoic acid antigens in Group H streptococci. In Secretory Immunity and Infection pp. 791–802 Mcghee J.R., Mestecky J., Babb J.L. Edited by New York: Plenum;
    [Google Scholar]
  32. Rosan B., Appelbaum B., Campbell L.K., Knox K.W., Wicken A.J. 1982; Chemostat studies of the effect of environmental control on Streptococcus sanguis adherence to hydroxyapatite. Infection and Immunity 35:64–70
    [Google Scholar]
  33. Rosan B., Eifert R., Golub E. 1985; Bacterial surfaces, salivary pellicles, and plaque formation. In Molecular Basis of Oral Microbial Adhesion pp. Mergenhagen S.E., Rosan B. Edited by Washington, DC: American Society for Microbiology;
    [Google Scholar]
  34. Thanh V.H., Young R.A., Davis R.W. 1985; Constructing and screening cDNA libraries in AgtlO and Igtl 1. In DNA Cloning: a Practical Approach 1 pp. 49–78 Glover D.M. Edited by Oxford: IRL Press;
    [Google Scholar]
  35. Towbin H., Staehelin T., Gordon J. 1979; Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of sciences of the united states of america 76:4350–4354
    [Google Scholar]
  36. Wyatt J.E., Hesketh L.M., Handley P.S. 1987; Lack of correlation between, fibrils, hydro- phobicity, and adhesion for strains of Streptococcus sanguis biotypes I and II. Microbios 50:7–15
    [Google Scholar]
  37. Young R.A., Davis R.W. 1983; Efficient isolation of genes by using antibody probes. Proceedings of the National Academy of Sciences of the United States of America 80:1194–1198
    [Google Scholar]
  38. Young R.A., Bloom B.R., Grosskinsky C.M., Ivanyi J., Thomas D., Davis R.W. 1985; Dissection of Mycobacterium tuberculosis antigens using recombinant DNA. Proceedings of the National Academy of Sciences of the United States of America 82:2583–2587
    [Google Scholar]
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