Aarhus University Seal

The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review


  • Anders Cavallin, Active Biotech Research AB
  • ,
  • Helena Arozenius, Active Biotech Research AB
  • ,
  • Karin Kristensson, Active Biotech Research AB
  • ,
  • Per Antonsson, Active Biotech Research AB
  • ,
  • Daniel E. Otzen
  • Per Björk, Active Biotech Research AB
  • ,
  • Göran Forsberg, Active Biotech Research AB

The superantigens staphylococcal enterotoxin A and E (SEA and SEE) can activate a large number of T-cells. SEA and SEE have approximately 80% sequence identity but show some differences in their biological function. Here, the two superantigens and analogues were characterized biophysically. SEE was shown to have a substantially higher thermal stability than SEA. Both SEA and SEE were thermally stabilized by 0.1 mM Zn2+ compared with Zn2+- reduced conditions achieved using 1 mM EDTA or specific replacements that affect Zn2+ coordination. The higher stability of SEE was only partly caused by the T-cell receptor (TCR) binding regions, whereas regions in the vicinity of the major histocompatibility complex class II binding sites affected the stability to a greater extent. SEE exhibited a biphasic denaturation between pH 5.0-6.5, influenced by residues in the TCR binding regions. Interestingly, enzyme-linked immunosorbent assay, isoelectric focusing, and circular dichroism analysis indicated that conformational changes had occurred in the SEA/E chimerical constructs relative to SEA and SEE. Thus, it is proposed that the Zn2+ binding site is very important for the stability and potency of SEA and SEE, whereas residues in the TCR binding site have a substantial influence on the molecular conformation to control specificity and function.

Original languageEnglish
JournalJournal of Biological Chemistry
Pages (from-to)1665-1672
Number of pages8
Publication statusPublished - 21 Jan 2000

See relations at Aarhus University Citationformats

ID: 139496739