TY - JOUR
T1 - Neutralization of multiple Staphylococcal superantigens by a single-chain protein consisting of affinity-matured, variable domain repeats
AU - Yang, Xi
AU - Buonpane, Rebecca A.
AU - Moza, Beenu
AU - Rahman, A. K.M.Nur Ur
AU - Wang, Ningyan
AU - Schlievert, Patrick M.
AU - McCormick, John K.
AU - Sundberg, Eric J.
AU - Kranz, David M.
N1 - Funding Information:
Received 13 August 2007; accepted 14 February 2008; electronically published 2 June 2008. Potential conflicts of interest: none reported. Financial support: National Institutes of Health (grants AI064611 to D.M.K. and AI55882 to E.J.S.; training grant T32 GM07283 to R.A.B.); Canadian Institute of Health Research (grant MOP-64176 and New Investigator award to J.K.M); Boston Biomedical Research Institute (Scholar Award to B.M.). Reprints or correspondence: Dr. David M. Kranz, Department of Biochemistry, University of Illinois, 600 S. Mathews, Urbana, IL 61801 ([email protected]).
PY - 2008/8/1
Y1 - 2008/8/1
N2 - 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.
AB - 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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U2 - 10.1086/589776
DO - 10.1086/589776
M3 - Article
C2 - 18522504
AN - SCOPUS:48749096140
SN - 0022-1899
VL - 198
SP - 344
EP - 348
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
IS - 3
ER -