Immunological response mounted by Aboriginal Australians living in the Northern Territory of Australia against serum opacity factor

The GenBank accession numbers for the sequences reported in this paper are AF367011 ( VT3.2), AF367012 ( VT3.1), AF367013 ( VT2.2), AF367014 ( VT21), AF367015 ( VT37.1) and AF367016 ( 13).

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Abstract

(Group A streptococcus) interacts with host fibronectin via a number of distinct surface components. The streptococcal serum opacity factor (SOF) is a cell-surface protein of which causes opalescence of human serum and mediates bacterial binding to fibronectin. In this study, hexahistidyl-tagged fusion proteins encompassing full-length SOF, and domains of SOF encompassing opacity factor activity and fibronectin-binding regions, were used in the characterization of the Aboriginal immune response to SOF. Anti-SOF serum IgG responses were found to be significantly higher (<00001) in Aboriginal adults and children when compared to a non-Aboriginal adult group. The Aboriginal immune response against the fibronectin-binding region of SOF was significantly reduced when compared to the response against the whole SOF protein and N-terminal domains examined in this study (<0001). This pattern of immune response was also observed in rabbits immunized with recombinant SOF. Comparison of the deduced amino acid sequence of SOF from a number of common Australian isolates with other SOF sequences revealed that the N-terminus of SOF exhibits sequence similarity values ranging from 429% to 965%. The C-terminus containing the fibronectin-binding domain and membrane-spanning regions was more highly conserved, exhibiting sequence similarity values ranging from 846% to 100% within the fibronectin-binding repeats. These data suggest that the immune response against SOF is directed toward the variable N-terminus of the SOF protein. Phylogenetic analysis indicated that the genes of do not exhibit geographical variation.

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2002-01-01
2024-03-28
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References

  1. Beachey E. H. 1981; Bacterial adherence: adhesin–receptor interactions mediating the attachment of bacteria to mucosal surfaces. J Infect Dis 143:325–345 [CrossRef]
    [Google Scholar]
  2. Beall B., Gherardi G., Lovgren M., Facklam R. R., Forwick B. A., Tyrrell G. J. 2000; emm and sof gene sequence variation in relation to serological typing of opacity-factor-positive group A streptococci. Microbiology 146:1195–1209
    [Google Scholar]
  3. Bisno A. L., Stevens D. L. 1996; Streptococcal infections of skin and soft tissues. N Engl J Med 334:240–245 [CrossRef]
    [Google Scholar]
  4. Burnette W. N. 1981; ‘Western blotting’: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to immodified nitrocellulose and radiographic detection with antibody and iodinated protein A. Anal Biochem 112:195–203 [CrossRef]
    [Google Scholar]
  5. Carapetis J., Gardiner D., Currie B., Mathews J. D. 1995; Mulitple strains of Streptococcus pyogenes in skin sores of aboriginal Australians. J Clin Microbiol 33:1471–1472
    [Google Scholar]
  6. Carapetis J. R., Wolff D. R., Currie B. J. 1996; Acute rheumatic fever and rheumatic heart disease in the top end of Australia’s Northern Territory. Med J Aust 164:146–149
    [Google Scholar]
  7. Courtney H. S., Dale J. B., Hasty D. I. 1996; Differential effects of the streptococcal fibronectin-binding protein, FBP54, on adhesion of group A streptococci to human buccal cells and HEp-2 tissue culture cells. Infect Immun 64:2415–2419
    [Google Scholar]
  8. Courtney H. S., Hasty D. L., Li Y., Chiang H. C., Thacker J. L., Dale J. B. 1999; Serum opacity factor is a major fibronectin-binding protein and a virulence determinant of M type 2 Streptococcus pyogenes . Mol Microbiol 32:89–98 [CrossRef]
    [Google Scholar]
  9. Cunningham M. W. 2000; Pathogenesis of group A streptococcal infections. Clin Microbiol Rev 13:470–511 [CrossRef]
    [Google Scholar]
  10. Eernisse D. J. 1992; DNA translator and aligner: hypercard utilities to aid phylogenetic analysis of molecules. Comput Appl Biosci 8:177–184
    [Google Scholar]
  11. Gardiner D. L., Sriprakash K. S. 1996; Molecular epidemiology of impetiginous group A streptococcal infection in aboriginal communities of northern Australia. J Clin Microbiol 34:1448–1452
    [Google Scholar]
  12. Gardiner D., Hartas J., Currie B., Mathews J. D., Kemp D. J., Sriprakash K. S. 1995; Vir typing: a long-PCR typing method for group A streptococci. PCR Methods Appl 4:288–293 [CrossRef]
    [Google Scholar]
  13. Gooder H. 1961; Association of a serum opacity reaction with serological type in Streptococcus pyogenes . J Gen Microbiol 25:347–352 [CrossRef]
    [Google Scholar]
  14. Goodfellow A. M., Hibble M., Talay S. R., Kreikemeyer B., Currie B. J., Sriprakash K. S., Chhatwal G. S. 2000; Distribution and antigenicity of fibronectin binding proteins (SfbI and SfbII) of Streptococcus pyogenes clinical isolates from the northern territory, Australia. J Clin Microbiol 38:389–392
    [Google Scholar]
  15. Hanski E., Caparon M. 1992; Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes . Proc Natl Acad Sci USA 89:6172–6176 [CrossRef]
    [Google Scholar]
  16. Jaffe J., Natanson-Yaron S., Caparon M. G., Hanski E. 1996; Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes , possesses two binding domains. Mol Microbiol 21:373–384 [CrossRef]
    [Google Scholar]
  17. Katerov V., Lindgren P. E., Totolian A. A., Schalen C. 2000; Streptococcal opacity factor: a family of bifunctional proteins with lipoproteinase and fibronectin-binding activities. Curr Microbiol 40:149–156 [CrossRef]
    [Google Scholar]
  18. Kreikemeyer B., Talay S. R., Chhatwal G. S. 1995; Characterization of a novel fibronectin-binding surface protein in group A streptococci. Mol Microbiol 17:137–145 [CrossRef]
    [Google Scholar]
  19. Kreikemeyer B., Martin D. R., Chhatwal G. S. 1999; SfbII protein, a fibronectin binding surface protein of group A streptococci, is a serum opacity factor with high serotype-specific apolipoproteinase activity. FEMS Microbiol Lett 178:305–311 [CrossRef]
    [Google Scholar]
  20. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685 [CrossRef]
    [Google Scholar]
  21. Lindgren P., McGavin M. J., Signaes C., Guss B., Gurusiddappa S., Hoeoek M., Lindberg M. 1993; Two different genes coding for fibronectin-binding proteins from Streptococcus dysgalactiae . The complete nucleotide sequences and characterization of the binding domains. Eur J Biochem 214:819–827 [CrossRef]
    [Google Scholar]
  22. Molinari G., Talay S. R., Valentin-Weigand P., Rohde M., Chhatwal G. S. 1997; The fibronectin-binding protein of Streptococcus pyogenes , SfbI, is involved in the internalization of group A streptococci by epithelial cells. Infect Immun 65:1357–1363
    [Google Scholar]
  23. Rakonjac J. V., Robbins J. C., Fischetti V. A. 1995; DNA sequence of the serum opacity factor of group A streptococci: identification of a fibronectin-binding repeat domain. Infect Immun 63:622–631
    [Google Scholar]
  24. Relf W. A., Martin D. R., Sriprakash K. S. 1992; Identification of sequence types among M-nontypeable group A streptococci. J Clin Microbiol 30:3190–3194
    [Google Scholar]
  25. Relf W. A., Martin D. R., Sriprakash K. S. 1994; Antigenic diversity within a family of M proteins from group A streptococci: evidence for the role of frameshift and compensatory mutations. Gene 144:25–30 [CrossRef]
    [Google Scholar]
  26. Rocha C. L., Fischetti V. A. 1999; Identification and characterization of a novel fibronectin-binding protein on the surface of group A streptococci. Infect Immun 67:2720–2728
    [Google Scholar]
  27. Sambrook J., Fritsch E. F., Maniatis T. 1989 Molecular Cloning: a Laboratory Manual , 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  28. Saravani G. A., Martin D. R. 1990; Opacity factor from group A streptococci is an apoproteinase. FEMS Microbiol Lett 68:35–39 [CrossRef]
    [Google Scholar]
  29. Schulze K., Medina E., Talay S. R., Towers R. J., Chhatwal G. S., Guzman C. A. 2001; Characterization of the domain of fibronectin-binding protein I of Streptococcus pyogenes responsible for elicitation of a protective immune response. Infect Immun 69:622–625 [CrossRef]
    [Google Scholar]
  30. Streeton C. L., Hanna J. N., Messer R. D., Merianos A. 1995; An epidemic of acute post-streptococcal glomerulonephritis among aboriginal children. J Paediatr Child Health 31:245–248 [CrossRef]
    [Google Scholar]
  31. Talay S. R., Valentin-Weigand P., Jerlstrom P. G., Timmis K. N., Chhatwal G. S. 1992; Fibronectin-binding protein of Streptococcus pyogenes : sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect Immun 60:3837–3844
    [Google Scholar]
  32. Top F. H. Jr, Wannamaker L. W. 1968; The serum opacity reaction of Streptococcus pyogenes : frequency of production of streptococcal lipoproteinase by strains of different serological types and the relationship of M protein production. J Hyg 66:49–58 [CrossRef]
    [Google Scholar]
  33. Tung J. S., Knight C. A. 1972; Relative importance of some factors affecting the electrophoretic migration of proteins in sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem 48:153–163 [CrossRef]
    [Google Scholar]
  34. Walker M. J., Birch R. G., Pemberton J. M. 1988; Cloning and characterization of an albicidin resistance gene from Klebsiella oxytoca . Mol Microbiol 2:443–454 [CrossRef]
    [Google Scholar]
  35. Zar H. 1984 Biostatistical Analysis , 2nd edn. Englewood Cliffs, NJ: Prentice Hall;
    [Google Scholar]
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