1887

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Volume 43, Issue 3

The detection of raised levels of IgM to in sera from patients with rheumatoid arthritis Free

Abstract

Summary

An analysis by ELISA of 100 rheumatoid factor (RF)-positive sera selected at random from a collection of sera from patients with various auto-immune diseases and joint pains, and 100 RF-negative sera from the same collection matched by patient age and gender, showed that the RF-positive sera had highly significantly (p ≪ 0.0001) raised levels of IgM antibody, but not IgG antibody, to over those of the RF-negative sera. This response was subsequently found to be associated with sera from patients who clinically had rheumatoid arthritis (RA). Sera from the RA patients had significantly greater amounts (p = 0.026) of IgM antibody to than to the other organisms tested and these values were also highly significantly different (p ≪ 0.0001) from IgM antibody levels in matched RF-negative sera. Sera from RA patients also had significantly greater amounts of IgA to (p ≪ 0.0001) and greater amounts of IgM to (p ≪ 0.0001) and (p ≪ 0.0001) than those in matched RF-negative sera. Other classes of antibody to these organisms and all classes of antibody to were not raised in the sera of RA patients over those of RF-negative controls. The IgM response in RA patients was not specific for only one O serotype of but was associated with all 11 different O serotypes of tested and those of other spp. Moreover, the IgM antibodies to spp. appeared to be independent from C-reactive protein and RF. Fourteen of 27 sera from RA patients had an IgM antibody that reacted with an internal 90-kDa protein of . This antibody was not found in RF-positive sera of patients with Sjogren’s disease or systemic lupus erythematosus, nor in other RF-negative sera, nor in those of healthy people, nor in those with osteoarthritis or ankylosing spondylitis. IgM antibodies capable of reacting with the haemolysin protein Hpm B of were not found in sera of RA patients of unknown HLA status.

  • Received:
  • Accepted:
  • Published Online:
© J. MED. MICROBIOL. 1995
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1995-09-01
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References

  1. Stastny P. Mixed lymphocyte culture typing cells from patients with rheumatoid arthritis. Tissue Antigens 1974; 4:571–579
     [Google Scholar]
  2. Lanchbury J. S. S. Molecular genetics of the HLA-D region component of inherited susceptibility to rheumatoid arthritis. Br J Rheumatol 1988; 27:171–175
     [Google Scholar]
  3. Dearlove S. M., Neumann V., Barr K. Antibody levels to Cl perfringens and response to sulphasalazine in patients with rheumatoid arthritis (RA). Br J Rheumatol 1990; 29: (Abstract, Suppl II) 3
     [Google Scholar]
  4. Zborovsky A., Lempert B., Baranovskaya N., Babayeva A. The clinical significance of immune reactions with some streptococcal antigens in rheumatoid arthritis. J Rheumatol 1990; 17:874–879
     [Google Scholar]
  5. Tsoulfa G., Rook G. A., Van-Embden J. D. Raised serum IgG and IgA antibodies to mycobacterial antigens in rheumatoid arthritis. Ann Rheum Dis 1989; 48:118–123
     [Google Scholar]
  6. Harris E. D. Rheumatoid arthritis. Pathophysiology and implications for therapy. N Engl J Med 1990; 322:1277–1289
     [Google Scholar]
  7. Senior B. W. The special affinity of particular types of Proteus mirabilis for the urinary tract. J Med Microbiol 1979; 12:1–8
     [Google Scholar]
  8. Ebringer A., Ptaszynska T., Corbett M. Antibodies to Proteus in rheumatoid arthritis. Lancet 1985; 2:305–307
     [Google Scholar]
  9. Ebringer A., Cox N. L., Abuljadayel I. Klebsiella antibodies in ankylosing spondylitis and Proteus antibodies in rheumatoid arthritis. Br J Rheumatol 1988; 27: Suppl II72–85
     [Google Scholar]
  10. Ebringer A., Khalafpour S., Wilson C. Rheumatoid arthritis and Proteus: a possible aetiological association. Rheumatol Int 1989; 9:223–228
     [Google Scholar]
  11. Rogers P., Hassan J., Bresnihan B., Feighery C., Whelan A. Antibodies to Proteus in rheumatoid arthritis. Br J Rheumatol 1988; 27: Suppl II90–94
     [Google Scholar]
  12. Deighton C. M., Gray J. W., Bint A. J., Walker D. J. Anti-Proteus antibodies in rheumatoid arthritis same-sexed sibships. Br J Rheumatol 1992; 31:241–245
     [Google Scholar]
  13. McDonagh J., Gray J., Deighton C. M., Sykes H., Walker D. J. Patient medication does not explain elevated anti-Proteus antibodies (Abs) in rheumatoid arthritis (RA). Br J Rheumatol 1992; 31: (Abstracts Suppl) 3
     [Google Scholar]
  14. Wilson C., Corbett M., Ebringer A. Increased isolation of Proteus mirabilis species from rheumatoid arthritis patients compared to osteoarthritis patients and healthy controls. Br J Rheumatol 1990; 29: (Abstracts Suppl II) 99
     [Google Scholar]
  15. McDonagh J., Gray J., Sykes H., Walker D. J., Bint A. J., Deighton C. M. Anti-Proteus antibodies and Proteus organisms in rheumatoid arthritis: a clinical study. Br J Rheumatol 1994; 33:32–35
     [Google Scholar]
  16. Deighton C. M., Gray J., McDonagh J., Walker D. J. Failure to detect urinary anti-Proteus antibodies (Abs) more frequently in rheumatoid arthritis (RA) patients compared with controls. Br J Rheumatol 1992; 31: (Abstracts Suppl I) 4
     [Google Scholar]
  17. Larsson P., Oiling S. O. antigen distribution and sensitivity to the bactericidal effect of normal human serum of Proteus strains from clinical specimens. Med Microbiol Immunol 1977; 163:77–82
     [Google Scholar]
  18. Sussman M. Escherichia coli in human and animal disease. In Sussman M. (ed) The virulence of Escherichia coli. Review and methods Special publications of the Society for General Microbiology. No. 13 London: Academic Press; 19857–45
     [Google Scholar]
  19. Uphoff T. S., Welch R. A. Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes (hpmA and hpmB) reveals sequence similarity with the Serratia marcescens hemolysin genes (shlA and shlB). J Bacteriol 1990; 172:1206–1216
     [Google Scholar]
  20. Welch R. A. Identification of two different hemolysin determinants in uropathogenic Proteus isolates. Infect Immun 1987; 55:2183–2190
     [Google Scholar]
  21. Murphy E. A., Mowat L., Sturrock R. D. Antibodies to Proteus in rheumatoid arthritis. Br J Rheumatol 1991; 30:390
     [Google Scholar]
  22. Senior B. W., Hughes C. Production and properties of haemolysins from clinical isolates of the Proteeae. J Med Microbiol 1988; 25:17–25
     [Google Scholar]
  23. Ebringer A., Cunningham P., Ahmadi K., Wrigglesworth J., Hosseini R., Wilson C. Sequence similarity between HLA-DR1 and DR4 subtypes associated with rheumatoid arthritis and proteus/serratia membrane haemolysin. Ann Rheum Dis 1992; 51:1245–1246
     [Google Scholar]
  24. Ebringer A., Wilson C., Ahmadi K. Molecular similarity and immune response to a Proteus mirabilis membrane haemolysin antigenic determinant in rheumatoid arthritis which is homologous with the HLA-DR1/DR4 susceptibility sequence. Br J Rheumatol 1993; 32: (Abstract Suppl 2) 10
     [Google Scholar]
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The detection of raised levels of IgM to Proteus mirabilis in sera from patients with rheumatoid arthritis
J. Med. Microbiol. 43, 176 (1995); https://doi.org/10.1099/00222615-43-3-176
/content/journal/jmm/10.1099/00222615-43-3-176
/content/journal/jmm/10.1099/00222615-43-3-176
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