Neutralization of multiple Staphylococcal superantigens by a single-chain protein consisting of affinity-matured, variable domain repeats

Xi Yang, Rebecca A. Buonpane, Beenu Moza, A. K.M.Nur Ur Rahman, Ningyan Wang, Patrick M. Schlievert, John K. McCormick, Eric J. Sundberg, David M. Kranz

Research output: Contribution to journalArticle

Abstract

Staphylococcus aureus secretes various toxins that act as superantigens by stimulating a large fraction of the host's T cells. Toxin binding to variable domains of T cell receptor β chains (Vβ) leads to massive release of inflammatory molecules and potentially to toxic shock syndrome (TSS). Previously, we generated soluble forms of different Vβ domains with a high affinity for binding superantigens. However, a broader spectrum antagonist is required for the neutralization of multiple toxins. In the present study, we expressed Vβ domains in tandem as a single-chain protein and neutralized the clinically important superantigens staphylococcal enterotoxin B and TSS toxin-1 with a single agent.

Original languageEnglish (US)
Pages (from-to)344-348
Number of pages5
JournalJournal of Infectious Diseases
Volume198
Issue number3
DOIs
StatePublished - Aug 1 2008

ASJC Scopus subject areas

  • Immunology and Allergy
  • Infectious Diseases

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    Yang, X., Buonpane, R. A., Moza, B., Rahman, A. K. M. N. U., Wang, N., Schlievert, P. M., McCormick, J. K., Sundberg, E. J., & Kranz, D. M. (2008). Neutralization of multiple Staphylococcal superantigens by a single-chain protein consisting of affinity-matured, variable domain repeats. Journal of Infectious Diseases, 198(3), 344-348. https://doi.org/10.1086/589776