Skip to main content
NCBI home page
Infection and Immunity logoLink to Infection and Immunity
. 1995 Apr;63(4):1391–1393. doi: 10.1128/iai.63.4.1391-1393.1995

Deviation of immune response to Chlamydia psittaci outer membrane protein in lipopolysaccharide-hyporesponsive mice.

T D Westbay 1, C C Dascher 1, R C Hsia 1, M Zauderer 1, P M Bavoil 1
PMCID: PMC173164  PMID: 7890400

Abstract

The outcome of infection is determined by both the quantity and the quality of an induced immune response. In particular, it has been demonstrated for selected pathogens that induction of TH1 or TH2 type helper T-cell subsets determines whether an immune response gives rise to protective immunity or disease-associated immunopathology. The nature of the antigen and the type of antigen-presenting cells recruited in the induction of a response are critical factors that influence the quality of the immune response. Of particular interest in this respect is the immune response to bacterial particles and the impact of cell wall-associated lipopolysaccharide (LPS) on that response. Nonspecific activation of macrophages and B lymphocytes by LPS could skew the phenotype of activated antigen-presenting cells and selectively alter the immunoglobulin isotypes and helper T-cell subsets that are induced following infection. In an initial attempt to detect immune deviation associated with LPS stimulation, we have compared the immunoglobulin isotypes of antibodies specific for the cysteine-rich outer membrane protein Omp2 induced in normal and LPS-hyporesponsive mice following immunization with Chlamydia psittaci strain guinea pig inclusion conjunctivitis whole elementary bodies. We report that there is a dramatic shift of Omp2-specific antibody from predominantly immunoglobulin G2a (IgG2a) isotype in LPS-hyporesponsive mice to high levels of IgG1 isotype in LPS-responder strains. The dependence of the IgG1 isotype shift on the LPS responder status is linked to the structure of the antigen and its natural processing pathway since LPS-hyporesponsive mice are not, in general, deficient in IgG1 antibody production. In particular, the antibody response to purified recombinant Omp2 is predominantly of the IgG1 isotype even in LPS-hyporesponsive mice.

Full Text

The Full Text of this article is available as a PDF (178.6 KB).

Selected References

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

  1. Batteiger B. E., Newhall W. J., 5th, Jones R. B. Differences in outer membrane proteins of the lymphogranuloma venereum and trachoma biovars of Chlamydia trachomatis. Infect Immun. 1985 Nov;50(2):488–494. doi: 10.1128/iai.50.2.488-494.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brade L., Nurminen M., Mäkelä P. H., Brade H. Antigenic properties of Chlamydia trachomatis lipopolysaccharide. Infect Immun. 1985 May;48(2):569–572. doi: 10.1128/iai.48.2.569-572.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
  4. Caldwell H. D., Hitchcock P. J. Monoclonal antibody against a genus-specific antigen of Chlamydia species: location of the epitope on chlamydial lipopolysaccharide. Infect Immun. 1984 May;44(2):306–314. doi: 10.1128/iai.44.2.306-314.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dhir S. P., Hakomori S., Kenny G. E., Grayston J. T. Immunochemical studies on chlamydial group antigen (presence of a 2-keto-3-deoxycarbohydrate as immunodominant group). J Immunol. 1972 Jul;109(1):116–122. [PubMed] [Google Scholar]
  6. Dhir S. P., Kenny G. E., Grayston J. T. Characterization of the group antigen of Chlamydia trachomatis. Infect Immun. 1971 Dec;4(6):725–730. doi: 10.1128/iai.4.6.725-730.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Janeway C. A., Jr, Carding S., Jones B., Murray J., Portoles P., Rasmussen R., Rojo J., Saizawa K., West J., Bottomly K. CD4+ T cells: specificity and function. Immunol Rev. 1988 Jan;101:39–80. doi: 10.1111/j.1600-065x.1988.tb00732.x. [DOI] [PubMed] [Google Scholar]
  8. Lugtenberg B., Meijers J., Peters R., van der Hoek P., van Alphen L. Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands. FEBS Lett. 1975 Oct 15;58(1):254–258. doi: 10.1016/0014-5793(75)80272-9. [DOI] [PubMed] [Google Scholar]
  9. Mosmann T. R., Coffman R. L. Heterogeneity of cytokine secretion patterns and functions of helper T cells. Adv Immunol. 1989;46:111–147. doi: 10.1016/s0065-2776(08)60652-5. [DOI] [PubMed] [Google Scholar]
  10. Newhall W. J., Batteiger B., Jones R. B. Analysis of the human serological response to proteins of Chlamydia trachomatis. Infect Immun. 1982 Dec;38(3):1181–1189. doi: 10.1128/iai.38.3.1181-1189.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Paul W. E., Seder R. A. Lymphocyte responses and cytokines. Cell. 1994 Jan 28;76(2):241–251. doi: 10.1016/0092-8674(94)90332-8. [DOI] [PubMed] [Google Scholar]
  12. Scott P., Kaufmann S. H. The role of T-cell subsets and cytokines in the regulation of infection. Immunol Today. 1991 Oct;12(10):346–348. doi: 10.1016/0167-5699(91)90063-Y. [DOI] [PubMed] [Google Scholar]
  13. Snapper C. M., Paul W. E. Interferon-gamma and B cell stimulatory factor-1 reciprocally regulate Ig isotype production. Science. 1987 May 22;236(4804):944–947. doi: 10.1126/science.3107127. [DOI] [PubMed] [Google Scholar]
  14. Sultzer B. M., Castagna R., Bandekar J., Wong P. Lipopolysaccharide nonresponder cells: the C3H/HeJ defect. Immunobiology. 1993 Apr;187(3-5):257–271. doi: 10.1016/S0171-2985(11)80343-8. [DOI] [PubMed] [Google Scholar]
  15. Vitetta E. S., Ohara J., Myers C. D., Layton J. E., Krammer P. H., Paul W. E. Serological, biochemical, and functional identity of B cell-stimulatory factor 1 and B cell differentiation factor for IgG1. J Exp Med. 1985 Nov 1;162(5):1726–1731. doi: 10.1084/jem.162.5.1726. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Watson J., Kelly K., Largen M., Taylor B. A. The genetic mapping of a defective LPS response gene in C3H/HeJ mice. J Immunol. 1978 Feb;120(2):422–424. [PubMed] [Google Scholar]
  17. Westbay T. D., Dascher C. C., Hsia R. C., Bavoil P. M., Zauderer M. Dissociation of immune determinants of outer membrane proteins of Chlamydia psittaci strain guinea pig inclusion conjunctivitis. Infect Immun. 1994 Dec;62(12):5614–5623. doi: 10.1128/iai.62.12.5614-5623.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES