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

Anders Cavallin; Helena Arozenius; Karin Kristensson; Per Antonsson; Daniel E. Otzen; Per Björk; Göran Forsberg

doi:10.1074/jbc.275.3.1665

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

Anders Cavallin, Helena Arozenius, Karin Kristensson, Per Antonsson, Daniel E. Otzen, Per Björk, Göran Forsberg^*

^*Corresponding author for this work

Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset

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27 Citations (Scopus)

Abstract

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 language	English
Journal	Journal of Biological Chemistry
Volume	275
Issue	3
Pages (from-to)	1665-1672
Number of pages	8
ISSN	0021-9258
DOIs	https://doi.org/10.1074/jbc.275.3.1665
Publication status	Published - 21 Jan 2000

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Cavallin, A., Arozenius, H., Kristensson, K., Antonsson, P., Otzen, D. E., Björk, P., & Forsberg, G. (2000). The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. Journal of Biological Chemistry, 275(3), 1665-1672. https://doi.org/10.1074/jbc.275.3.1665

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

abstract = "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.",

author = "Anders Cavallin and Helena Arozenius and Karin Kristensson and Per Antonsson and Otzen, {Daniel E.} and Per Bj{\"o}rk and G{\"o}ran Forsberg",

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Cavallin, A, Arozenius, H, Kristensson, K, Antonsson, P, Otzen, DE, Björk, P & Forsberg, G 2000, 'The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function', Journal of Biological Chemistry, vol. 275, no. 3, pp. 1665-1672. https://doi.org/10.1074/jbc.275.3.1665

The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. / Cavallin, Anders; Arozenius, Helena; Kristensson, Karin et al.
In: Journal of Biological Chemistry, Vol. 275, No. 3, 21.01.2000, p. 1665-1672.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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AU - Cavallin, Anders

AU - Arozenius, Helena

AU - Kristensson, Karin

AU - Antonsson, Per

AU - Otzen, Daniel E.

AU - Björk, Per

AU - Forsberg, Göran

PY - 2000/1/21

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N2 - 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.

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.

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

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