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  • Letters to the Editor
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Streptococcus pyogenes and phagocytic killing

Nature Medicine volume 8, pages 1044–1045 (2002)Cite this article

An Erratum to this article was published on 01 November 2002

To the editor

Streptococcus pyogenes, one of the most common human bacterial pathogens, has evolved diverse mechanisms that allow the bacteria to evade the immune system and cause disease1. The molecular bases for many of these processes are still not well characterized. Recently, Lei et al.2 described a streptococcal protein, Mac, with homology to the human B2 integrin Mac-1. The streptococcal protein Mac mimics parts of the CD11b/CD18 complement receptor and was suggested to inhibit phagocyte function by blocking interaction of the FcγIIIb receptor (CD16) with specific antibodies and/or complement factors2. Subsequently, we described a novel extracellular cysteine proteinase produced by S. pyogenes3, which we called IdeS, for immunoglobulin G-degrading enzyme of S. pyogenes. IdeS was shown to cleave opsonizing immunoglobulin G (IgG) antibodies bound to streptococcal surface structures, thereby inhibiting the killing of S. pyogenes by phagocytic cells3. As it turns out, IdeS is actually the same as the Mac protein of S. pyogenes2, and this protein is referred to here as Mac/IdeS.

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Figure 1: IdeSC94G binds to PMNs but does not protect against phagocytic killing.

References

  1. Cunningham, M.W. Pathogenesis of group A streptococcal infections. Clin. Microbiol. 13, 470–511 (2000).

    Article  CAS  Google Scholar 

  2. Lei, B. et al. Evasion of human innate and acquired immunity by a bacterial homolog of CD11b that inhibits opsonophagocytosis. Nature Med. 7, 1298–1305 (2001).

    Article  CAS  Google Scholar 

  3. von Pawel-Rammingen, U., Johansson, B.P. & Björck, L. IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. EMBO J. 12, 1607–1615 (2002).

    Article  Google Scholar 

  4. Lancefield, R.C. Current knowledge of type-specific M antigens of group A streptococci. J. Immunol. 89, 307–313 (1962).

    CAS  PubMed  Google Scholar 

  5. Björck, L. et al. Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor. Nature 337, 385–386 (1989).

    Article  Google Scholar 

  6. Fleit, H.B. et al. A soluble form of FcγRIII is present in human serum and other body fluids and is elevated at sites of inflammation. Blood 79, 2721–2728 (1992).

    CAS  PubMed  Google Scholar 

  7. Lei, B., Mackie, S., Lukomski, S. & Musser, J.M. Identification and immunogenicity of group A Streptococcus culture supernatant proteins. Infect. Immun. 68, 6807–6818 (2000).

    Article  CAS  Google Scholar 

  8. Lei, B. et al. Opsonophagocytosis-inhibiting Mac protein of group A Streptococcus: Identification and characteristics of two genetic complexes. Infect. Immun. (in the press).

  9. Huizinga, T.W.J. et al. Soluble Fc γ receptor III in human plasma originates from release by neutrophils. J. Clin. Invest. 86, 416–423 (1990).

    Article  CAS  Google Scholar 

  10. Koene, H.R. et al. Clinical value of soluble IgG Fc receptor type III in plasma from patients with chronic idiopathic neutropenia. Blood 91, 3962–3966 (1998).

    CAS  PubMed  Google Scholar 

  11. Antibody molecules. in Antibodies: A Laboratory Manual. (eds. Harlow, E. & Lane, D.) 10 (Cold Spring Harbor Press, New York, 1988).

  12. Hoe, N.P. et al. Insight into the molecular basis of pathogen abundance: Group A Streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells. Proc. Natl. Acad. Sci. USA 99, 7646–7651 (2002).

    Article  CAS  Google Scholar 

  13. Frank, M.M. Annihilating host defense. Nature Med. 7, 1285–1286 (2002).

    Article  Google Scholar 

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Author information

Authors and Affiliations

  1. Department of Cell and Molecular Biology Section for Molecular Pathogenesis Lund University, Lund, Sweden

    Ulrich von Pawel-Rammingen, Björn P. Johansson, Hans Tapper & Lars Björck

Authors
  1. Ulrich von Pawel-Rammingen
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  2. Björn P. Johansson
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  3. Hans Tapper
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  4. Lars Björck
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Competing interests

The authors are funded by Hansa Medical AB. Hansa Medical has filed a patent application on IdeS. The application is pending.

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von Pawel-Rammingen, U., Johansson, B., Tapper, H. et al. Streptococcus pyogenes and phagocytic killing. Nat Med 8, 1044–1045 (2002). https://doi.org/10.1038/nm1002-1044

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