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Neutralization of Multiple Staphylococcal Superantigens by a Single-Chain Protein Consisting of Affinity-Matured, Variable Domain Repeats
Journal article   Open access   Peer reviewed

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 and David M Kranz
The Journal of infectious diseases, Vol.198(3), pp.344-348
08/01/2008
DOI: 10.1086/589776
PMCID: PMC2649774
PMID: 18522504
url
https://doi.org/10.1086/589776View
Published (Version of record) Open Access

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.

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