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  • Title: Neutralization of multiple staphylococcal superantigens by a single-chain protein consisting of affinity-matured, variable domain repeats.
    Author: Yang X, Buonpane RA, Moza B, Rahman AK, Wang N, Schlievert PM, McCormick JK, Sundberg EJ, Kranz DM.
    Journal: J Infect Dis; 2008 Aug 01; 198(3):344-8. PubMed ID: 18522504.
    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 beta chains (Vbeta) leads to massive release of inflammatory molecules and potentially to toxic shock syndrome (TSS). Previously, we generated soluble forms of different Vbeta 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 Vbeta 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.
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