期刊
JOURNAL OF INFECTIOUS DISEASES
卷 198, 期 3, 页码 344-348出版社
OXFORD UNIV PRESS INC
DOI: 10.1086/589776
关键词
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资金
- NIAID NIH HHS [R01 AI064611, AI55882, AI064611, R21 AI055882-03, R01 AI064611-04, R21 AI055882] Funding Source: Medline
- NIGMS NIH HHS [T32 GM07283, T32 GM007283-26, T32 GM007283] Funding Source: Medline
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 (V beta) leads to massive release of inflammatory molecules and potentially to toxic shock syndrome (TSS). Previously, we generated soluble forms of different V beta 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 V beta 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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