1887

Chapter 7 : Structural Evidence for Zinc and Peptide Dependence in Superantigen-Major Histocompatibility Complex Class II Interaction

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $15.00

Preview this chapter:
Zoom in
Zoomout

Structural Evidence for Zinc and Peptide Dependence in Superantigen-Major Histocompatibility Complex Class II Interaction, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555815844/9781555814243_Chap07-1.gif /docserver/preview/fulltext/10.1128/9781555815844/9781555814243_Chap07-2.gif

Abstract:

Bacterial superantigens (SAgs) are small, highly mitogenic proteins that cross-link antigen-presenting cells (APCs) and T cells by binding simultaneously to the immunoreceptors major histocompatibility complex (MHC) class II and the T-cell receptors (TCRs) leading to the stimulation of large numbers of T cells. The advantages for microbes of secreting SAgs are not very well understood, but apart from disturbing the normal immune response they might prolong survival by promoting local inflammation, thereby increasing the blood and nutrient supply. The ability of SAgs to activate the immune system systemically became clear when evidence was presented that the interaction took place outside the antigen groove. SEA is an interesting SAg because it can interact with both the generic site on the α-chain of MHC class II and the zinc-dependent site on the β-chain of major histocompatibility complex (MHC) class II. The crystal structure shows that SED forms homodimers where two carboxy-terminal β-sheets from two SED molecules are packed against each other burying a large solvent-inaccessible area. At high concentrations the streptococcal SAg pyrogenic exotoxins (SPE-C) has the ability to cross-link two MHC molecules through a high-affinity, zinc-dependent interaction with the β-chain due to homodimer formation using residues in its amino-terminal domain (SPE-C probably binds MHC as a monomer under physiological conditions). Approximately two-thirds of the buried surface area is contributed by interaction with the β1-helix on MHC and one-third by the antigenic peptide, strongly implying that the peptide plays an important role in binding the SAg.

Citation: Walse B. 2007. Structural Evidence for Zinc and Peptide Dependence in Superantigen-Major Histocompatibility Complex Class II Interaction, p 103-120. In Kotb M, Fraser J (ed), Superantigens. ASM Press, Washington, DC. doi: 10.1128/9781555815844.ch7

Key Concept Ranking

MHC Class II
0.47456455
Tumor Necrosis Factor alpha
0.4387641
0.47456455
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Image of Figure 1.
Figure 1.

Sequence alignment of a subset of SAgs. The alignment was created as a structural alignment by superpositioning different SAg structures. Secondary structural elements for SEA are indicated below the sequences. Residues involved in the zinc-dependent high-affinity interaction with the β-chain of MHC class II are indicated with black boxes and residues involved in the low-affinity interaction with the α-chain of MHC class II are indicated with gray boxes. The HExxH motif in SEC2, SEC3, and SPE-A is outlined with black lines.

Citation: Walse B. 2007. Structural Evidence for Zinc and Peptide Dependence in Superantigen-Major Histocompatibility Complex Class II Interaction, p 103-120. In Kotb M, Fraser J (ed), Superantigens. ASM Press, Washington, DC. doi: 10.1128/9781555815844.ch7
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 2.
Figure 2.

Family tree of streptococcal and staphylococcal SAgs. The tree was created using ClustalW ( ).

Citation: Walse B. 2007. Structural Evidence for Zinc and Peptide Dependence in Superantigen-Major Histocompatibility Complex Class II Interaction, p 103-120. In Kotb M, Fraser J (ed), Superantigens. ASM Press, Washington, DC. doi: 10.1128/9781555815844.ch7
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555815844.ch07
1. Abrahmsén, L.,, M. Dohlsten,, S. Segren,, P. Bjork,, E. Jonsson, and, T. Kalland. 1995. Characterization of two distinct MHC class II binding sites in the superantigen staphylococcal enterotoxin A. EMBO J. 14(13):29782986.
2. Alberts, I. L.,, K. Nadassy, and, S. J. Wodak. 1998. Analysis of zinc binding sites in protein crystal structures. Protein Sci. 7(8):17001716.
3. Al-Daccak, R.,, K. Mehindate,, F. Damdoumi,, P. Etongue-Mayer,, H. Nilsson,, P. Antonsson,, M. Sundstrom,, M. Dohlsten,, R. P. Sekaly, and, W. Mourad. 1998. Staphylococcal enterotoxin D is a promiscuous superantigen offering multiple modes of interactions with the MHC class II receptors. J. Immunol. 160(1):225232.
4. Alouf, J. E., and, H. Muller-Alouf. 2003. Staphylococcal and streptococcal superantigens: molecular, biological and clinical aspects. Int. J. Med. Microbiol. 292(7–8):429440.
5. Andersen, P. S.,, P. M. Lavoie,, R. P. Sekaly,, H. Churchill,, D. M. Kranz,, P. M. Schlievert,, K. Karjalainen, and, R. A. Mariuzza. 1999. Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes. Immunity 10(4):473483.
6. Arcus, V. L.,, R. Langley,, T. Proft,, J. D. Fraser, and, E. N. Baker. 2002. The three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome. J. Biol. Chem. 277(35):3227432281.
7. Arcus, V. L.,, T. Proft,, J. A. Sigrell,, H. M. Baker,, J. D. Fraser, and, E. N. Baker. 2000. Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus pyogenes. J. Mol. Biol. 299(1):157168.
8. Artiushin, S. C.,, J. F. Timoney,, A. S. Sheoran, and, S. K. Muthupalani. 2002. Characterization and immunogenicity of pyrogenic mitogens SePE-H and SePE-I of Streptococcus equi. Microb. Pathog. 32(2):7185.
9. Baker, H. M.,, T. Proft,, P. D. Webb,, V. L. Arcus,, J. D. Fraser, and, E. N. Baker. 2004. Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin j can use a common binding surface for T-cell receptor binding and dimerization. J. Biol. Chem. 279: 3857138576.
10. Baker, M. D.,, I. Gendlina,, C. M. Collins, and, K. R. Acharya. 2004. Crystal structure of a dimeric form of streptococcal pyrogenic exotoxin a (Spea1) Protein Sci. 13:22852290.
11. Baker, M. D.,, D. M. Gutman,, A. C. Papageorgiou,, C. M. Collins, and, K. R. Acharya. 2001. Structural features of a zinc binding site in the superantigen strepococcal pyrogenic exotoxin A (SpeA1): implications for MHC class II recognition. Protein Sci. 10(6):12681273.
12. Baker, M. D.,, A. C. Papageorgiou,, R. W. Titball,, J. Miller,, S. White,, B. Lingard,, J. J. Lee,, D. Cavanagh,, M. A. Kehoe,, J. H. Robinson, and, K. R. Acharya. 2002. Structural and functional role of threonine 112 in a superantigen Staphylococcus aureus enterotoxin B. J. Biol. Chem. 277:27562762.
13. Bergdoll, M. S. 1970. Enterotoxins, p. 265326. In T. C. Montie,, S. Kadio, and, S. J. Ajil (ed.), Microbial Toxins. Academic Press Inc., New York, N.Y.
14. Bolin, D. R.,, A. L. Swain,, R. Sarabu,, S. J. Berthel,, P. Gillespie,, N. J. Huby,, R. Makofske,, L. Orze-chowski,, A. Perrotta,, K. Toth,, J. P. Cooper,, N. Jiang,, F. Falcioni,, R. Campbell,, D. Cox,, D. Gaizband,, C. J. Belunis,, D. Vidovic,, K. Ito,, R. Crowther,, U. Kammlott,, X. Zhang,, R. Palermo,, D. Weber,, J. Guenot,, Z. Nagy, and, G. L. Olson. 2000. Peptide and peptide mimetic inhibitors of antigen presentation by HLA-DR class II MHC molecules. Design, structure-activity relationships, and X-ray crystal structures. J. Med. Chem. 43:21352148.
15. Cavallin, A.,, H. Arozenius,, K. Kristensson,, P. Antonsson,, D. E. Otzen,, P. Bjork, and, G. Forsberg. 2000. The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. J. Biol. Chem. 275(3):16651672.
16. Cavallin, A.,, K. Petersson, and, G. Forsberg. 2003. Spectrophotometric methods for the determination of superantigen structure and stability. Methods Mol. Biol. 214:5563.
17. Chi, Y. I.,, I. Sadler,, L. M. Jablonski,, S. D. Callantine,, C. F. Deobald,, C. V. Stauffacher, and, G. A. Bohach. 2002. Zinc-mediated dimerization and its effect on activity and conformation of staphylococcal enterooxin type C. J. Biol. Chem. 277(25):2283922846.
18. Choi, Y. W.,, A. Herman,, D. DiGiusto,, T. Wade,, P. Marrack, and, J. Kappler. 1990. Residues of the variable region of the T-cell-receptor beta-chain that interact with S. aureus toxin superantigens. Nature 346(6283):471473.
19. Cole, B. C., and, C. L. Atkin. 1991. The Mycoplasma arthritidis T-cell mitogen, MAM: a model superantigen. Immunol. Today 12(8):271276.
20. Cole, B. C.,, K. L. Knudtson,, A. Oliphant,, A. D. Sawitzke,, A. Pole,, M. Manohar,, L. S. Benson,, E. Ahmed, and, C. L. Atkin. 1996. The sequence of the Mycoplasma arthritidis superantigen, MAM: identification of functional domains and comparison with microbial superantigens and plant lectin mitogens. J. Exp. Med. 183(3):11051110.
21. Deckhut, A. M.,, Y. Chien,, M. A. Blackman, and, D. L. Woodland. 1994. Evidence for a functional interaction between the beta chain of major histocompatibility complex class II and the T cell receptor alpha chain during recognition of a bacterial superantigen. J. Exp. Med. 180(5):19311935.
22. DeLano, W. L. 2002. The PyMOL Molecular Graphics System (2002) on World Wide Web. @http:// www.pymol.org.
23. Dellabona, P.,, J. Peccoud,, J. Kappler,, P. Marrack,, C. Benoist, and, D. Mathis. 1990. Superantigens interact with MHC class II molecules outside of the antigen groove. Cell 62(6):11151121.
24. Dessen, A.,, C. M. Lawrence,, S. Cupo,, D. M. Zaller, and, D. C. Wiley. 1997. X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II. Immunity 7(4):473481.
25. Dinges, M. M.,, P. M. Orwin, and, P. M. Schlievert. 2000. Exotoxins of Staphylococcus aureus. Clin. Microbiol. Rev. 13(1):1634.
26. Dohlsten, M.,, G. Hedlund, and, T. Kalland. 1991. Staphylococcal-enterotoxin-dependent cell-mediated cytotoxicity. Immunol. Today 12(5):147150.
27. Dohlsten, M.,, G. Hedlund,, H. O. Sjogren, and, R. Carlsson. 1988. Two subsets of human CD4+ T helper cells differing in kinetics and capacities to produce interleukin 2 and interferon-gamma can be defined by the Leu-18 and UCHL1 monoclonal antibodies. Eur. J. Immunol. 18(8):11731178.
28. Dowd, J. E.,, R. W. Karr, and, D. R. Karp. 1996. Functional activity of staphylococcal enterotoxin A requires interactions with both the alpha and beta chains of HLA-DR. Mol. Immunol. 33(16):12671274.
29. Earhart, C. A.,, D. T. Mitchell,, D. L. Murray,, D. M. Pinheiro,, M. Matsumura,, P. M. Schlievert, and, D. H. Ohlendorf. 1998. Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity. Biochemistry 37:71947202.
30. Earhart, C. A.,, G. M. Vath,, M. Roggiani,, P. M. Schlievert, and, D. H. Ohlendorf. 2000. Structure of streptococcal pyrogenic exotoxin A reveals a novel metal cluster. Protein Sci. 9(9):18471851.
31. Etongue-Mayer, P.,, M. A. Langlois,, M. Ouellette,, H. Li,, S. Younes,, R. Al-Daccak, and, W. Mourad. 2002. Involvement of zinc in the binding of Mycoplasma arthritidis-derived mitogen to the proximity of the HLA-DR binding groove regardless of histidine 81 of the beta chain. Eur. J. Immunol. 32(1):5058.
32. Fernandez, M. M.,, M. C. De Marzi,, P. Berguer,, D. Burzyn,, R. J. Langley,, I. Piazzon,, R. A. Mariuzza, and, E. L. Malchiodi. 2006. Binding of natural variants of staphylococcal superantigens SEG and SEI to TCR and MHC class II molecule. Mol. Immunol. 43(7):927938.
33. Ferretti, J. J.,, W. M. McShan,, D. Ajdic,, D. J. Savic,, G. Savic,, K. Lyon,, C. Primeaux,, S. Sezate,, A. N. Suvorov,, S. Kenton,, H. S. Lai,, S. P. Lin,, Y. Qian,, H. G. Jia,, F. Z. Najar,, Q. Ren,, H. Zhu,, L. Song,, J. White,, X. Yuan,, S. W. Clifton,, B. A. Roe, and, R. McLaughlin. 2001. Complete genome sequence of an M1 strain of Streptococcus pyogenes. Proc. Natl. Acad. Sci. USA 98(8):46584663.
34. Fields, B. A.,, E. L. Malchiodi,, H. Li,, X. Ysern,, C. V. Stauffacher,, P. M. Schlievert,, K. Karjalainen, and, R. A. Mariuzza. 1996. Crystal structure of a T-cell receptor beta-chain complexed with a superantigen. Nature 384(6605):188192.
35. Fischer, H.,, M. Dohlsten,, M. Lindvall,, H. O. Sjogren, and, R. Carlsson. 1989. Binding of staphylococcal enterotoxin A to HLA-DR on B cell lines. J. Immunol. 142(9):31513157.
36. Fleischer, B., and, H. Schrezenmeier. 1988. T cell stimulation by staphylococcal enterotoxins. Clonally variable response and requirement for major histocompatibility complex class II molecules on accessory or target cells. J. Exp. Med. 167(5):16971707.
37. Fleischer, B.,, H. Schrezenmeier, and, P. Conradt. 1989. T lymphocyte activation by staphylococcal entero-toxins: role of class II molecules and T cell surface structures. Cell. Immunol. 120:92101.
38. Fraser, J. D. 1989. High-affinity binding of staphylococcal enterotoxins A and B to HLA-DR. Nature 339(6221):221223.
39. Fraser, J. D.,, V. L. Arcus,, E. N. Baker, and, T. Proft. 2003. Bacterial superantigens and immune evasion, p. 171200. In B. Henderson and, P.C. F. Oyston (ed.), Bacterial Evasion of Host Immune Responses. Cambridge University Press, Cambridge, United Kingdom.
40. Fraser, J. D.,, R. G. Urban,, J. L. Strominger, and, H. Robinson. 1992. Zinc regulates the function of two superantigens. Proc. Natl. Acad. Sci. USA 89(12):55075511.
41. Garcia, K. C.,, L. Teyton, and, I. A. Wilson. 1999. Structural basis of T cell recognition. Annu. Rev. Immunol. 17:369397.
42. Gronenborn, A. M.,, D. R. Filpula,, N. Z. Essig,, A. Achari,, M. Whitlow,, P. T. Wingfield, and, G. M. Clore. 1991. A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Science 253(5020):657661.
43. Håkansson, M.,, P. Antonsson,, P. Bjork, and, L. A. Svensson. 2001. Cooperative zinc binding in a staphylococcal enterotoxin A mutant mimics the SEA-MHC class II interaction J. Biol. Inorg. Chem. 6:757762.
44. Håkansson, M.,, K. Petersson,, H. Nilsson,, G. Forsberg,, P. Bjork,, P. Antonsson, and, L. A. Svensson. 2000. The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules. J. Mol. Biol. 302(3):527537.
45. Hamad, A. R.,, P. Marrack, and, J. W. Kappler. 1997. Transcytosis of staphylococcal superantigen toxins. J. Exp. Med. 185(8):14471454.
46. Hennecke, J., and, D. C. Wiley. 2001. T cell receptor-MHC interactions up close. Cell 104(1):14.
47. Herman, A.,, N. Labrecque,, J. Thibodeau,, P. Marrack,, J. W. Kappler, and, R. P. Sekaly. 1991. Identification of the staphylococcal enterotoxin A superantigen binding site in the beta 1 domain of the human histo-compatibility antigen HLA-DR. Proc. Natl. Acad. Sci. USA 88(22):99549958.
48. Hogan, R. J.,, J. VanBeek,, D. R. Broussard,, S. L. Surman, and, D. L. Woodland. 2001. Identification of MHC class II-associated peptides that promote the presentation of toxic shock syndrome toxin-1 to T cells. J. Immunol. 166(11):65146522.
49. Hudson, K. R.,, R. E. Tiedemann,, R. G. Urban,, S. C. Lowe,, J. L. Strominger, and, J. D. Fraser. 1995. Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II. J. Exp. Med. 182(3):711720.
50. Jardetzky, T. S.,, J. H. Brown,, J. C. Gorga,, L. J. Stern,, R. G. Urban,, Y. I. Chi,, C. Stauffacher,, J. L. Strominger, and, D. C. Wiley. 1994. Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen. Nature 368(6473):711718.
51. Jiang, W., and, J. S. Bond. 1992. Families of metalloendopeptidases and their relationships. FEBS Lett. 312:110114.
52. Kappler, J.,, B. Kotzin,, L. Herron,, E. W. Gelfand,, R. D. Bigler,, A. Boylston,, S. Carrel,, D. N. Posnett,, Y. Choi, and, P. Marrack. 1989. V beta-specific stimulation of human T cells by staphylococcal toxins. Science 244(4906):811813.
53. Karp, D. R., and, E. O. Long. 1992. Identification of HLA-DR1 beta chain residues critical for binding staphylococcal enterotoxins A and E. J. Exp. Med. 175(2):415424.
54. Kiefer, L. L.,, S. A. Paterno, and, C. A. Fierke. 1995. Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency. J. Am. Chem. Soc. 117:68316837.
55. Kim, J.,, R. G. Urban,, J. L. Strominger, and, D. C. Wiley. 1994. Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1. Science 266(5192):18701874.
56. Kotzin, B. L.,, D. Y. Leung,, J. Kappler, and, P. Marrack. 1993. Superantigens and their potential role in human disease. Adv. Immunol. 54:99166.
57. Kozono, H.,, D. Parker,, J. White,, P. Marrack, and, J. Kappler. 1995. Multiple binding sites for bacterial superantigens on soluble class II MHC molecules. Immunity 3(2):187196.
58. Krupka, H. I.,, B. W. Segelke,, R. G. Ulrich,, S. Ringhofer,, M. Knapp, and, B. Rupp. 2002. Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC-IIalpha. Protein Sci. 11:642651.
59. Kumaran, D.,, S. Eswaramoorthy,, W. Furey,, M. Sax, and, S. Swaminathan. 2001. Structure of staphylococcal enterotoxin C2 at various pH levels. Acta Crystallogr. D Biol. Crystallogr. 57:12701275.
60. Kuroda, M.,, T. Ohta,, I. Uchiyama,, T. Baba,, H. Yuzawa,, I. Kobayashi,, L. Cui,, A. Oguchi,, K. Aoki,, Y. Nagai,, J. Lian,, T. Ito,, M. Kanamori,, H. Matsumaru,, A. Maruyama,, H. Murakami,, A. Hosoyama,, Y. Mizutani-Ui,, N. K. Takahashi,, T. Sawano,, R. Inoue,, C. Kaito,, K. Sekimizu,, H. Hirakawa,, S. Kuhara,, S. Goto,, J. Yabuzaki,, M. Kanehisa,, A. Yamashita,, K. Oshima,, K. Furuya,, C. Yoshino,, T. Shiba,, M. Hattori,, N. Ogasawara,, H. Hayashi, and, K. Hiramatsu. 2001. Whole genome sequencing of meticillin-resistant Staphylococcus aureus. Lancet 357(9264):12251240.
61. Langford, M. P.,, G. J. Stanton, and, H. M. Johnson. 1978. Biological effects of staphylococcal enterotoxin A on human peripheral lymphocytes. Infect. Immun. 22(1):6268.
62. Langlois, M. A.,, Y. El Fakhry, and, W. Mourad. 2003. Zinc-binding sites in the N terminus of Mycoplasma arthritidis-derived mitogen permit the dimer formation required for high affinity binding to HLA-DR and for T cell activation. J. Biol. Chem. 278(25):2230922315.
63. Li, H.,, A. Llera,, D. Tsuchiya,, L. Leder,, X. Ysern,, P. M. Schlievert,, K. Karjalainen, and, R. A. Mariuzza. 1998. Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B. Immunity 9(6):807816.
64. Li, Y.,, H. Li,, N. Dimasi,, J. K. McCormick,, R. Martin,, P. Schuck,, P. M. Schlievert, and, R. A. Mariuzza. 2001. Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II. Immunity 14(1):93104.
65. Llewelyn, M.,, S. Sriskandan,, M. Peakman,, D. R. Ambrozak,, D. C. Douek,, W. W. Kwok,, J. Cohen, and, D. M. Altmann. 2004. HLA class II polymorphisms determine responses to bacterial superantigens. J. Immunol. 172(3):17191726.
66. Manders, S. M. 1998. Toxin-mediated streptococcal and staphylococcal disease. J. Am. Acad. Dermatol. 39(3):383398.
67. Marrack, P., and, J. Kappler. 1990. The staphylococcal enterotoxins and their relatives. Science 248(4956):705711.
68. Merritt, E. A., and, W. G. Hol. 1995. AB5 toxins. Curr. Opin. Struct. Biol. 5(2):165171.
69. Mitchell, D. T.,, D. G. Levitt,, P. M. Schlievert, and, D. H. Ohlendorf. 2000. Structural evidence for the evolution of pyrogenic toxin superantigens. J. Mol. Evol. 51(6):520531.
70. Miyoshi-Akiyama, T.,, K. Imanishi, and, T. Uchiyama. 1993. Purification and partial characterization of a product from Yersinia pseudotuberculosis with the ability to activate human T cells. Infect. Immun. 61(9):39223927.
71. Miyoshi-Akiyama, T.,, J. Zhao,, H. Kato,, K. Kikuchi,, K. Totsuka,, Y. Kataoka,, M. Katsumi, and, T. Uchiyama. 2003. Streptococcus dysgalactiae-derived mitogen (SDM), a novel bacterial superantigen: characterization of its biological activity and predicted tertiary structure. Mol. Microbiol. 47(6):15891599.
72. Nilsson, H.,, P. Bjork,, M. Dohlsten, and, P. Antonsson. 1999. Staphylococcal enterotoxin H displays unique MHC class II-binding properties. J. Immunol. 163(12):66866693.
73. Papageorgiou, A. C., and, K. R. Acharya. 2000. Microbial superantigens: from structure to function. Trends Microbiol. 8(8):369375.
74. Papageorgiou, A. C.,, K. R. Acharya, R. Shapiro,, E. F. Passalacqua,, R. D. Brehm, and, H. S. Tranter. 1995. Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site. Structure 3(8):769779.
75. Papageorgiou, A. C.,, M. D. Baker,, J. D. McLeod,, S. K. Goda,, C. N. Manzotti,, D. M. Sansom,, H. S. Tranter, and, K. R. Acharya. 2004. Identification of a secondary zinc-binding site in staphylococcal enterotoxin C2. Implications for superantigen recognition. J. Biol. Chem. 279(2):12971303.
76. Papageorgiou, A. C.,, R. D. Brehm,, D. D. Leonidas,, H. S. Tranter, and, K. R. Acharya. 1996. The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 A resolution. J. Mol. Biol. 260:553569.
77. Papageorgiou, A. C.,, C. M. Collins,, D. M. Gutman,, J. B. Kline,, S. M. O’Brien,, H. S. Tranter, and, K. R. Acharya. 1999. Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeA1) by MHC class II molecules and T-cell receptors. EMBO J. 18(1):921.
78. Papageorgiou, A. C.,, C. P. Quinn,, D. Beer,, R. D. Brehm,, H. S. Tranter,, P. F. Bonventre, and, K. R. Acharya. 1996. Crystal structure of a biologically inactive mutant of toxic shock syndrome toxin-1 at 2.5 A resolution. Protein Sci. 5:17371741.
79. Papageorgiou, A. C.,, H. S. Tranter, and, K. R. Acharya. 1998. Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors. J. Mol. Biol. 277:6179.
80. Peavy, D. L.,, W. H. Adler, and, R. T. Smith. 1970. The mitogenic effects of endotoxin and staphylococcal enterotoxin B on mouse spleen cells and human peripheral lymphocytes. J. Immunol. 105(6):14531458.
81. Petersson, K.,, G. Forsberg, and, B. Walse. 2004. Interplay between superantigens and immunoreceptors. Scand. J. Immunol. 59(4):345355.
82. Petersson, K.,, M. Håkansson,, H. Nilsson,, G. Forsberg,, L. A. Svensson,, A. Liljas, and, B. Walse. 2001. Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence. EMBO J. 20(13):33063312.
83. Petersson, K.,, H. Pettersson,, N. J. Skartved,, B. Walse, and, G. Forsberg. 2003. Staphylococcal enterotoxin H induces Valpha-specific expansion of T cells. J. Immunol. 170(8):4148U54.
84. Petersson, K.,, M. Thunnissen,, G. Forsberg, and, B. Walse. 2002. Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules. Structure 10:16191626.
85. Pless, D. D.,, G. Ruthel,, E. K. Reinke,, R. G. Ulrich, and, S. Bavari. 2005. Persistence of zinc-binding bacterial superantigens at the surface of antigen-presenting cells contributes to the extreme potency of these superantigens as T-cell activators. Infect. Immun. 73(9):53585366.
86. Pontzer, C. H.,, J. K. Russell, and, H. M. Johnson. 1991. Structural basis for differential binding of staphylococcal enterotoxin A and toxic shock syndrome toxin 1 to class II major histocompatibility molecules. Proc. Natl. Acad. Sci. USA 88(1):125128.
87. Prasad, G. S.,, C. A. Earhart,, D. L. Murray,, R. P. Novick,, P. M. Schlievert, and, D. H. Ohlendorf. 1993. Structure of toxic shock syndrome toxin 1. Biochemistry 32(50):1376113766.
88. Prasad, G. S.,, R. Radhakrishnan,, D. T. Mitchell,, C. A. Earhart,, M. M. Dinges,, W. J. Cook,, P. M. Schlievert, and, D. H. Ohlendorf. 1997. Refined structures of three crystal forms of toxic shock syndrome toxin-1 and of a tetramutant with reduced activity. Protein Sci. 6:12201227.
89. Proft, T.,, V. L. Arcus,, V. Handley,, E. N. Baker, and, J. D. Fraser. 2001. Immunological and biochemical characterization of streptococcal pyrogenic exotoxins I and J (SPE-I and SPE-J) from Streptococcus pyogenes. J. Immunol. 166(11):67116719.
90. Proft, T.,, S. L. Moffatt,, C. J. Berkahn, and, J. D. Fraser. 1999. Identification and characterization of novel superantigens from Streptococcus pyogenes. J. Exp. Med. 189(1):89102.
91. Proft, T.,, S. L. Moffatt,, K. D. Weller,, A. Paterson,, D. Martin, and, J. D. Fraser. 2000. The streptococcal superantigen SMEZ exhibits wide allelic variation, mosaic structure, and significant antigenic variation. J. Exp. Med. 191(10):17651776.
92. Proft, T.,, P. D. Webb,, V. Handley, and, J. D. Fraser. 2003. Two novel superantigens found in both group a and group C streptococcus. Infect. Immun. 71(3):13611369.
93. Roussel, A.,, B. F. Anderson,, H. M. Baker,, J. D. Fraser, and, E. N. Baker. 1997. Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules. Nat. Struct. Biol. 4(8):635643.
94. Russell, J. K.,, C. H. Pontzer, and, H. M. Johnson. 1990. The I-A beta b region (65–85) is a binding site for the superantigen, staphylococcal enterotoxin A. Biochem. Biophys. Res. Commun. 168(2):696701.
95. Schad, E. M.,, A. C. Papageorgiou,, L. A. Svensson, and, K. R. Acharya. 1997. A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity. J. Mol. Biol. 269(2):270280.
96. Schad, E. M.,, I. Zaitseva,, V. N. Zaitsev,, M. Dohlsten,, T. Kalland,, P. M. Schlievert,, D. H. Ohlendorf, and, L. A. Svensson. 1995. Crystal structure of the superantigen staphylococcal enterotoxin type A. EMBO J. 14:3292301.
97. Sundberg, E., and, T. S. Jardetzky. 1999. Structural basis for HLA-DQ binding by the streptococcal superantigen SSA. Nat. Struct. Biol. 6(2):123129.
98. Sundberg, E. J.,, P. S. Andersen,, P. M. Schlievert,, K. Karjalainen, and, R. A. Mariuzza. 2003. Structural, energetic, and functional analysis of a protein-protein interface at distinct stages of affinity maturation. Structure 11(9):11511161.
99. Sundberg, E. J.,, H. Li,, A. S. Llera,, J. K. McCormick,, J. Tormo,, P. M. Schlievert,, K. Karjalainen, and, R. A. Mariuzza. 2002. Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes. Structure 10(5):687699.
100. Sundberg, E. J.,, Y. Li, and, R. A. Mariuzza. 2002. So many ways of getting in the way: diversity in the molecular architecture of superantigen-dependent T-cell signaling complexes. Curr. Opin. Immunol. 14(1):3644.
101. Sundberg, E. J.,, M. W. Sawicki,, S. Southwood,, P. S. Andersen,, A. Sette, and, R. A. Mariuzza. 2002. Minor structural changes in a mutated human melanoma antigen correspond to dramatically enhanced stimulation of a CD4+ tumor-infiltrating lymphocyte line. J. Mol. Biol. 319(2):449461.
102. Sundstrom, M.,, L. Abrahmsen,, P. Antonsson,, K. Mehindate,, W. Mourad, and, M. Dohlsten. 1996. The crystal structure of staphylococcal enterotoxin type D reveals Zn2+ -mediated homodimerization. EMBO J. 15(24):68326840.
103. Sundstrom, M.,, D. Hallen,, A. Svensson,, E. Schad,, M. Dohlsten, and, L. Abrahmsen. 1996. The co-crystal structure of staphylococcal enterotoxin type A with Zn2 + at 2.7 A resolution. Implications for major histocompatibility complex class II binding. J. Biol. Chem. 271(50):3221232216.
104. Swaminathan, S.,, W. Furey,, J. Pletcher, and, M. Sax. 1992. Crystal structure of staphylococcal enterotoxin B, a superantigen. Nature 359(6398):801806.
105. Swaminathan, S.,, W. Furey,, J. Pletcher, and, M. Sax. 1995. Residues defining V beta specificity in staphylococcal enterotoxins. Nat. Struct. Biol. 2: 680686.
106. Thompson, J. D.,, D. G. Higgins, and, T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22(22):46734680.
107. Tiedemann, R. E., and, J. D. Fraser. 1996. Cross-linking of MHC class II molecules by staphylococcal enterotoxin A is essential for antigen-presenting cell and T cell activation. J. Immunol. 157(9):39583966.
108. Tiedemann, R. E.,, R. J. Urban,, J. L. Strominger, and, J. D. Fraser. 1995. Isolation of HLA-DR1.(staphylococcal enterotoxin A)2 trimers in solution. Proc. Natl. Acad. Sci. USA 92(26):1215612159.
109. Trowsdale, J. 2005. HLA genomics in the third millennium. Curr. Opin. Immunol. 17(5):498504.
110. Wen, R.,, D. R. Broussard,, S. Surman,, T. L. Hogg,, M. A. Blackman, and, D. L. Woodland. 1997. Car-boxy-terminal residues of major histocompatibility complex class II-associated peptides control the presentation of the bacterial superantigen toxic shock syndrome toxin-1 to T cells. Eur. J. Immunol. 27(3):772781.
111. Wen, R.,, G. A. Cole,, S. Surman,, M. A. Blackman, and, D. L. Woodland. 1996. Major histocompatibility complex class II-associated peptides control the presentation of bacterial superantigens to T cells. J. Exp. Med. 183(3):10831092.
112. White, J.,, A. Herman,, A. M. Pullen,, R. Kubo,, J. W. Kappler, and, P. Marrack. 1989. The V beta-specific superantigen staphylococcal enterotoxin B: stimulation of mature T cells and clonal deletion in neonatal mice. Cell 56(1):2735.
113. Wikstrom, M.,, T. Drakenberg,, S. Forsen,, U. Sjobring, and, L. Bjorck. 1994. Three-dimensional solution structure of an immunoglobulin light chain-binding domain of protein L. Comparison with the IgG-binding domains of protein G. Biochemistry 33(47):1401114017.
114. Woodland, D. L.,, R. Wen, and, M. A. Blackman. 1997. Why do superantigens care about peptides? Immunol. Today 18(1):1822.
115. Zavala-Ruiz, Z.,, I. Strug,, M. W. Anderson,, J. Gorski, and, L. J. Stern. 2004. A polymorphic pocket at the P10 position contributes to peptide binding specificity in class II MHC proteins. Chem. Biol. 11:13951402.
116. Zavala-Ruiz, Z.,, I. Strug,, B. D. Walker,, P. J. Norris, and, L. J. Stern. 2004. A hairpin turn in a class II MHC-bound peptide orients residues outside the binding groove for T cell recognition. Proc. Natl. Acad. Sci. USA 101:1327913284.
117. Zavala-Ruiz, Z.,, E. J. Sundberg,, J. D. Stone,, D. B. DeOliveira,, I. C. Chan,, J. Svendsen,, R. A. Mariuzza, and, L. J. Stern. 2003. Exploration of the P6/P7 region of the peptide-binding site of the human class II major histocompatibility complex protein HLA-DR1 J. Biol. Chem. 278:4490444912.
118. Zhao, Y.,, Z. Li,, S. J. Drozd,, Y. Guo,, W. Mourad, and, H. Li. 2004. Crystal structure of Mycoplasma arthritidis mitogen complexed with HLA-DR1 reveals a novel superantigen fold and a dimerized superantigen-MHC complex. Structure 12(2):277288.

Tables

Generic image for table
Table 1.

Crystal structures of bacterial SAgs and their complexes

Citation: Walse B. 2007. Structural Evidence for Zinc and Peptide Dependence in Superantigen-Major Histocompatibility Complex Class II Interaction, p 103-120. In Kotb M, Fraser J (ed), Superantigens. ASM Press, Washington, DC. doi: 10.1128/9781555815844.ch7

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error