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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.

Papageorgiou AC, Tranter HS, Acharya KR
J Mol Biol 277 61-79 (1998)
Cited: 92 times
EuropePMC logo PMID: 9514739

Abstract

Staphylococcal enterotoxin B is a member of a family of toxins known as superantigens that activate a large number of T-cells (up to 20%) by cross-linking MHC class II molecules with T-cell receptors in a Vbeta-restricted fashion. The crystal structure of staphylococcal enterotoxin B presented here has been determined at 1.5 A resolution, the highest resolution so far for a superantigen. The final model contains 1948 protein atoms and 177 water molecules and has excellent geometry with root-mean-square (rms) deviation of 0.007 A and 1.73 degrees in bond lengths and bond angles, respectively. The overall fold is similar to that of other microbial superantigens, but as it lacks the zinc-binding site found in other members of this family, such as staphylococcal enterotoxin A, C2 and D, this enterotoxin possesses only one MHC class II binding site. Comparison of the crystal structure of free SEB and in complex with an MHC class II molecule revealed no major changes in the MHC-binding site upon complex formation. However, a number of water molecules found in the free SEB may be displaced in the complex or contribute further to its stability. Detailed analysis of the TcR-binding site of SEB, SEA and SEC2 shows significant differences which may account for the ability of each superantigen to bind specific Vbeta sequences.

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  2. Biological Toxins as the Potential Tools for Bioterrorism. Janik E, Ceremuga M, Saluk-Bijak J, Bijak M. Int J Mol Sci 20 E1181 (2019)
  3. Potent Neutralization of Staphylococcal Enterotoxin B In Vivo by Antibodies that Block Binding to the T-Cell Receptor. Chen G, Karauzum H, Long H, Carranza D, Holtsberg FW, Howell KA, Abaandou L, Zhang B, Jarvik N, Ye W, Liao GC, Gross ML, Leung DW, Amarasinghe GK, Aman MJ, Sidhu SS. J Mol Biol 431 4354-4367 (2019)
  4. Soluble T cell receptor Vβ domains engineered for high-affinity binding to staphylococcal or streptococcal superantigens. Sharma P, Wang N, Kranz DM. Toxins (Basel) 6 556-574 (2014)

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  1. Staphylococcal enterotoxins. Balaban N, Rasooly A. Int J Food Microbiol 61 1-10 (2000)
  2. Food poisoning and Staphylococcus aureus enterotoxins. Argudín MÁ, Mendoza MC, Rodicio MR. Toxins (Basel) 2 1751-1773 (2010)
  3. Staphylococcus aureus and its food poisoning toxins: characterization and outbreak investigation. Hennekinne JA, De Buyser ML, Dragacci S. FEMS Microbiol Rev 36 815-836 (2012)
  4. Blood Groups in Infection and Host Susceptibility. Cooling L. Clin Microbiol Rev 28 801-870 (2015)
  5. Staphylococcal enterotoxins. Pinchuk IV, Beswick EJ, Reyes VE. Toxins (Basel) 2 2177-2197 (2010)
  6. Microbial superantigens: from structure to function. Papageorgiou AC, Acharya KR. Trends Microbiol 8 369-375 (2000)
  7. Staphylococcal and streptococcal superantigens: molecular, biological and clinical aspects. Alouf JE, Müller-Alouf H. Int J Med Microbiol 292 429-440 (2003)
  8. Mechanisms of staphylococcal enterotoxin-induced emesis. Hu DL, Nakane A. Eur J Pharmacol 722 95-107 (2014)
  9. Understanding the mechanism of action of bacterial superantigens from a decade of research. Lavoie PM, Thibodeau J, Erard F, Sékaly RP. Immunol Rev 168 257-269 (1999)
  10. Gammadelta T cells: innately adaptive immune cells? Ferreira LM. Int Rev Immunol 32 223-248 (2013)
  11. The staphylococcal enterotoxin (SE) family: SEB and siblings. Krakauer T, Stiles BG. Virulence 4 759-773 (2013)
  12. Superantigen bacterial toxins: state of the art. Müller-Alouf H, Carnoy C, Simonet M, Alouf JE. Toxicon 39 1691-1701 (2001)
  13. Protein transport across the cell wall of monoderm Gram-positive bacteria. Forster BM, Marquis H. Mol Microbiol 84 405-413 (2012)
  14. The natural history of ubiquitin and ubiquitin-related domains. Burroughs AM, Iyer LM, Aravind L. Front Biosci (Landmark Ed) 17 1433-1460 (2012)
  15. CD28: direct and critical receptor for superantigen toxins. Kaempfer R, Arad G, Levy R, Hillman D, Nasie I, Rotfogel Z. Toxins (Basel) 5 1531-1542 (2013)
  16. FDA-approved immunosuppressants targeting staphylococcal superantigens: mechanisms and insights. Krakauer T. Immunotargets Ther 6 17-29 (2017)

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