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Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeA1) by MHC class II molecules and T-cell receptors.

Papageorgiou AC, Collins CM, Gutman DM, Kline JB, O'Brien SM, Tranter HS, Acharya KR
EMBO J 18 9-21 (1999)
Cited: 43 times
EuropePMC logo PMID: 9878045

Abstract

Streptococcal pyrogenic exotoxin A (SpeA) is a superantigen produced by Streptococcus pyogenes and is associated with severe infections characterized by rash, hypotension, multiorgan failure and a high mortality rate. In this study, an allelic form of this toxin, SpeA1, was crystallized with four molecules in the crystallographic asymmetric unit and its crystal structure was determined at 2.6 A resolution. The crystallographic R-factor was 19.4% (33 497 reflections) for 7031 protein atoms and 88 water molecules. The overall structure of SpeA1 is considerably similar to that of other prototype microbial superantigens, either of staphylococcal or streptococcal origin, but has greatest similarity to staphylococcal enterotoxin C (SEC). Based on structural and mutagenesis data, we have mapped several important residues on the toxin molecule, which are involved in the recognition of major histocompatibility complex (MHC) class II molecules and T-cell receptors. Also, the toxin appears to possess a potential zinc-binding site which may have implications in binding to particular MHC class II molecules. Finally, we propose models for SpeA1-MHC class II and SpeA1-T-cell receptor association and the relevance of this phenomenon to the superantigenic action of this toxin is considered.

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  9. Three-dimensional structural location and molecular functional effects of missense SNPs in the T cell receptor Vbeta domain. Wang Z, Moult J. Proteins 53 748-757 (2003)
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  13. Are superantigens the cause of cytokine storm and viral sepsis in severe COVID-19? Observations and hypothesis. Scaglioni V, Soriano ER. Scand J Immunol 92 e12944 (2020)
  14. Cloning, expression and interaction of human T-cell receptors with the bacterial superantigen SSA. De Marzí MC, Fernández MM, Sundberg EJ, Molinero L, Zwirner NW, Llera AS, Mariuzza RA, Malchiodi EL. Eur J Biochem 271 4075-4083 (2004)
  15. Superantigen natural affinity maturation revealed by the crystal structure of staphylococcal enterotoxin G and its binding to T-cell receptor Vbeta8.2. Fernández MM, Bhattacharya S, De Marzi MC, Brown PH, Kerzic M, Schuck P, Mariuzza RA, Malchiodi EL. Proteins 68 389-402 (2007)
  16. Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor {beta} chain. Fernández MM, Cho S, De Marzi MC, Kerzic MC, Robinson H, Mariuzza RA, Malchiodi EL. J Biol Chem 286 1189-1195 (2011)
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  20. Crystal structure of a dimeric form of streptococcal pyrogenic exotoxin A (SpeA1). Baker MD, Gendlina I, Collins CM, Acharya KR. Protein Sci 13 2285-2290 (2004)
  21. Elevated risk of invasive group A streptococcal disease and host genetic variation in the human leucocyte antigen locus. Parks T, Elliott K, Lamagni T, Auckland K, Mentzer AJ, Guy R, Cartledge D, Strakova L, Connor DO, Pollard AJ, Neville MJ, Mahajan A, Ashrafian H, Chapman SJ, Hill AVS, Sriskandan S, Knight JC. Genes Immun 21 63-70 (2020)
  22. Mutagenesis, biochemical, and biophysical characterization of Mycoplasma arthritidis-derived mitogen. Li H, Zhao Y, Guo Y, Vanvranken SJ, Li Z, Eisele L, Mourad W. Mol Immunol 44 763-773 (2007)
  23. Mutational effects on protein folding stability and antigenicity: the case of streptococcal pyrogenic exotoxin A. Carra JH, Welcher BC, Schokman RD, David CS, Bavari S. Clin Immunol 108 60-68 (2003)
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  26. Streptococcal pyrogenic exotoxin G gene in blood and pharyngeal isolates of Streptococcus dysgalactiae subspecies equisimilis has a limited role in pathogenesis. Korem M, Hidalgo-Grass C, Michael-Gayego A, Nir-Paz R, Salameh S, Moses AE. J Microbiol Immunol Infect 47 292-296 (2014)
  27. Identification of a Thiol-Disulfide Oxidoreductase (SdbA) Catalyzing Disulfide Bond Formation in the Superantigen SpeA in Streptococcus pyogenes. Lee SF, Li L, Jalal N, Halperin SA. J Bacteriol 203 e0015321 (2021)


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