Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Article
  • Published:

Residues defining Vβ specificity in staphylococcal enterotoxins

Nature Structural Biology volume 2, pages 680–686 (1995)Cite this article

Abstract

The three-dimensional structure of staphylococcal enterotoxin C2 has been determined at 2.7 Å resolution by X-ray diffraction, while the structures of enterotoxins A and E have been modelled based on their sequence homology to other staphylococcal enterotoxins. The T-cell receptor-binding sites of staphylococcal enterotoxin (SE) B and SEC2 are compared and the stereochemical interactions likely to be responsible for their differing Vβ specificities are identified. A similar comparison is made between SEA and SEE.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Bergdoll, M.S. Staphylococcal intoxications. In Food borne infections and intoxications.(Ed. Reimann, H. & Bryan, F.L.), 443–494 (Academic Press, New York; 1979).

    Google Scholar 

  2. Johnson, H.M., Russell, J.F. & Pontzer, C.H. Superantigens in human disease. Scientific American 92–101 (1992).

    Article  CAS  Google Scholar 

  3. Kotzin, B.L., Leung, D.Y., Kappler, J. & Marrack, P. Superantigens and their potential role in human disease. Advances in Immunology 54, 99–166 (1993).

    Article  CAS  Google Scholar 

  4. Kappler, J.W., Herman, A., Clements, J. & Marrack, P. Mutations defining functional regions of the superantigen staphylococcal enterotoxin B. J. exp. Med. 175, 387–396 (1992).

    Article  CAS  Google Scholar 

  5. Mollick, J.A., McMasters, R.L., Grossman, D. & Rich, R.R. Localization of a site on bacterial superantigens that determine T cell receptor β-chain specificity. J. Exp. Med. 177, 283–293 (1993).

    Article  CAS  Google Scholar 

  6. Irwin, M.J., Hudson, K.R., Fraser, J.D. & Gascoigne, N.R. Enterotoxin residues determining T-cell receptor Vβ binding specificity. Nature 359, 841–843 (1992).

    Article  CAS  Google Scholar 

  7. Swaminathan, S., Furey, W., Pletcher, J. & Sax, M. Crystal structure of staphylococcal enterotoxin B, a superantigen. Nature 359, 801–806 (1992).

    Article  CAS  Google Scholar 

  8. Murzin, A.G. OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12, 861–867 (1993).

    Article  CAS  Google Scholar 

  9. Hoffmann, M. et al. Predictions of T-cell receptor and major histocompatibility complex binding sites on staphylococcal enterotoxin C1. Infection and Immunity 62, 3396–3407 (1994).

    CAS  PubMed  PubMed Central  Google Scholar 

  10. Acharya, K.R. et al. Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1. Nature 367, 94–97 (1994).

    Article  CAS  Google Scholar 

  11. Prasad, G.S., Earhart, C.A., Murray, D.L., Novick, R.R., Schlivert, P.M. & Ohlendorf, D.H. Structure of toxic shock syndrome toxin 1. Biochemistry 32, 13761–13766 (1993).

    Article  CAS  Google Scholar 

  12. Marrack, P. & Kappler, J. The staphylococcal enterotoxins and their relatives. Science 248, 705–711 (1990).

    Article  CAS  Google Scholar 

  13. Jones, T.A. A graphics model building and refinement system for macromolecules. J. appl. Crystallogr. 11, 268–272 (1978).

    Article  CAS  Google Scholar 

  14. Brünger, A.T., Kuriyan, J. & Karplus, M. Crystallographic R factor refinement by molecular dynamics. Science 235, 458–460 (1987).

    Article  Google Scholar 

  15. Fraser, J.D., Urban, R.G., Strominger, J.L. & Robinson, H. Zinc regulates the function of two superantigens. Proc. natn. Acad. Sci. U.S.A. 89, 5507–5511 (1992).

    Article  CAS  Google Scholar 

  16. Fraser, J.D. Structural model of staphylococcal enterotoxin A interaction with MHC class II antigens. In Superantigens: A pathogen′s view of the immune system, 7. (Ed. Huber, B.T. & Palmer,E. ) 7–29 (Cold Spring Harbor Press; 1993).

    Google Scholar 

  17. Karp, D.R. & Long, E.O. Identification of HLA-DR1 b chain residues critical for binding staphylococcal enterotoxins A and E. J. exp. Med. 175, 415–424 (1992).

    Article  CAS  Google Scholar 

  18. Jardetzky, T.S. et al. Three-dimensional structure of a human class II histocompatibilty molecule complexed with superantigen. Nature 368, 711–718 (1994).

    Article  CAS  Google Scholar 

  19. Turner, T.N., Smith, C.L. & Bohach, G.A. Residues 20, 22 & 26 determine the subtype specificities of staphylococcal enterotoxin C1 & C2. Infection & Immunity 60, 694–697 (1992).

    CAS  Google Scholar 

  20. Swaminathan, S., Furey, W., Pletcher, J. & Sax, M., X-ray studies on two new crystal forms of staphylococcal enterotoxin C2. Acta. Crystallogr.D, in the press.

  21. Weissman, L. in Computational Crystallography (ed. Sayre, D.) 56–63 (Clarendon Press, Oxford; 1982).

    Google Scholar 

  22. Fitzgerald, P.M.D. MERLOT: an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. appl. Crystallogr. 21, 273–278 (1988).

    Article  CAS  Google Scholar 

  23. Read, R.J., Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A42, 140–149 (1986).

    Article  CAS  Google Scholar 

  24. Wang, B.C. Resolution of phase ambiguity. Meths of Enzymol. 115, 90–106 (1985).

    Article  CAS  Google Scholar 

  25. Furey, W. & Swaminathan, S. PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules. in Macromolecular crystallography, Meths of Enzymol. (Eds Carter, C. & Sweet, B.) in the press (Academic Press, Orlando; 1995).

    Google Scholar 

  26. Engh, R.A. & Huber, R. Accurate bond and angle parameters for X-ray protein-structure refinement. Acta. Crystallogr. A47, 392–400 (1991).

    Article  CAS  Google Scholar 

  27. Jones, C.L. & Khan, S.A. Nucleotide sequence of the enterotoxin B gene from staphylococcus aureus. J.Bacteriol. 166, 29–33 (1986).

    Article  CAS  Google Scholar 

  28. Bohach, G.A. & Schlievert, P.M. Nucleotide sequence of the staphylococcal enterotoxin C1 gene and relatedness to other pyrogenic toxins. Mol.Gen. Genet. 209, 15–20 (1987)

    Article  CAS  Google Scholar 

  29. Bohach, G.A. & Schlievert, P.M. Conservation of the biologically active portions of enterotoxins C1 and C2. Infection & Immunity 57, 2249–2252 (1989).

    CAS  Google Scholar 

  30. Hovde, C.J., Hackett, S.R. & Bohach, G.A. Nucleotide sequence of the staphylococcal enterotoxin C3 gene: Sequence comparison of all three type C staphylococcal enterotoxins. Mol. gen. Genet. 220, 329–333 (1990).

    Article  CAS  Google Scholar 

  31. Carson, M. RIBBONS 2.0. J. appl Crystallogr. 24, 958–961 (1991).

    Article  Google Scholar 

  32. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J.appl. Crystallogr. 24, 946–950 (1991).

    Article  Google Scholar 

  33. Ferrin, T.E. et al. THE MIDAS display system. J. molec. Graphics 6, 13–27 (1988).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Biocrystallography Laboratory, VA Medical Center, PO Box 12055, University Drive C, Pittsburgh, Pennsylvania, 15240

    S. Swaminathan, William Furey, James Pletcher & Martin Sax

  2. Department of Crystallography, University of Pittsburgh, Pittsburgh, Pennsylvania, 15260, USA

    S. Swaminathan, William Furey, James Pletcher & Martin Sax

Authors
  1. S. Swaminathan
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. William Furey
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. James Pletcher
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Martin Sax
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Swaminathan, S., Furey, W., Pletcher, J. et al. Residues defining Vβ specificity in staphylococcal enterotoxins. Nat Struct Mol Biol 2, 680–686 (1995). https://doi.org/10.1038/nsb0895-680

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsb0895-680

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing