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Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.

<div class='caption-title'>X-ray structure of the SEE-TCR complex.</div>
<div class='caption-title'>Presentation of the buried surface areas in the SEE-TCR interface.</div>
<div class='caption-title'>Comparison between structurally determined CDR2 loops.</div>
Rödström KE, Regenthal P, Lindkvist-Petersson K
OpenAccess logo PLoS One 10 e0131988 (2015)
Cited: 11 times
EuropePMC logo PMID: 26147596

Abstract

T cells are crucial players in cell-mediated immunity. The specificity of their receptor, the T cell receptor (TCR), is central for the immune system to distinguish foreign from host antigens. Superantigens are bacterial toxins capable of inducing a toxic immune response by cross-linking the TCR and the major histocompatibility complex (MHC) class II and circumventing the antigen specificity. Here, we present the structure of staphylococcal enterotoxin E (SEE) in complex with a human T cell receptor, as well as the unligated T cell receptor structure. There are clear structural changes in the TCR loops upon superantigen binding. In particular, the HV4 loop moves to circumvent steric clashes upon complex formation. In addition, a predicted ternary model of SEE in complex with both TCR and MHC class II displays intermolecular contacts between the TCR α-chain and the MHC, suggesting that the TCR α-chain is of importance for complex formation.

Articles - 4udt mentioned but not cited (3)

  1. Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition. Rödström KE, Regenthal P, Lindkvist-Petersson K. PLoS One 10 e0131988 (2015)
  2. Two common structural motifs for TCR recognition by staphylococcal enterotoxins. Rödström KEJ, Regenthal P, Bahl C, Ford A, Baker D, Lindkvist-Petersson K. Sci Rep 6 25796 (2016)
  3. Computational discovery of binding mode of anti-TRBC1 antibody and predicted key amino acids of TRBC1. Saetang J, Sangkhathat S, Jangphattananont N, Khopanlert W, Julamanee J, Tipmanee V. Sci Rep 12 1760 (2022)


Reviews citing this publication (2)

  1. Staphylococcal enterotoxins and enterotoxin-like toxins with special reference to dairy products: An overview. Benkerroum N. Crit Rev Food Sci Nutr 58 1943-1970 (2018)
  2. Allergy-A New Role for T Cell Superantigens of Staphylococcus aureus? Abdurrahman G, Schmiedeke F, Bachert C, Bröker BM, Holtfreter S. Toxins (Basel) 12 E176 (2020)

Articles citing this publication (6)

  1. Antibodies and superantibodies in patients with chronic rhinosinusitis with nasal polyps. Chen JB, James LK, Davies AM, Wu YB, Rimmer J, Lund VJ, Chen JH, McDonnell JM, Chan YC, Hutchins GH, Chang TW, Sutton BJ, Kariyawasam HH, Gould HJ. J Allergy Clin Immunol 139 1195-1204.e11 (2017)
  2. Structural assessment of HLA-A2-restricted SARS-CoV-2 spike epitopes recognized by public and private T-cell receptors. Wu D, Kolesnikov A, Yin R, Guest JD, Gowthaman R, Shmelev A, Serdyuk Y, Dianov DV, Efimov GA, Pierce BG, Mariuzza RA. Nat Commun 13 19 (2022)
  3. Thermal stability and structural changes in bacterial toxins responsible for food poisoning. Regenthal P, Hansen JS, André I, Lindkvist-Petersson K. PLoS One 12 e0172445 (2017)
  4. IL-15 Trans-Presentation Is an Autonomous, Antigen-Independent Process. Kenesei Á, Volkó J, Szalóki N, Mocsár G, Jambrovics K, Balajthy Z, Bodnár A, Tóth K, Waldmann TA, Vámosi G. J Immunol 207 2489-2500 (2021)
  5. Staphylococcus enterotoxin profile of China isolates and the superantigenicity of some novel enterotoxins. Shen M, Li Y, Zhang L, Dai S, Wang J, Li Y, Zhang L, Huang J. Arch Microbiol 199 723-736 (2017)
  6. Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells. Sebestyén V, Nagy É, Mocsár G, Volkó J, Szilágyi O, Kenesei Á, Panyi G, Tóth K, Hajdu P, Vámosi G. Int J Mol Sci 23 3313 (2022)


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