由亲和力成熟的可变结构域重复序列组成的单链蛋白对多种葡萄球菌超抗原的中和作用。
Neutralization of multiple staphylococcal superantigens by a single-chain protein consisting of affinity-matured, variable domain repeats.
作者信息
Yang Xi, Buonpane Rebecca A, Moza Beenu, Rahman A K M Nur-ur, Wang Ningyan, Schlievert Patrick M, McCormick John K, Sundberg Eric J, Kranz David M
机构信息
Department of Biochemistry, University of Illinois, Urbana, Illinois 61801, USA.
出版信息
J Infect Dis. 2008 Aug 1;198(3):344-8. doi: 10.1086/589776.
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.
摘要
金黄色葡萄球菌分泌多种毒素，这些毒素作为超抗原，可刺激宿主的大部分T细胞。毒素与T细胞受体β链（Vβ）的可变域结合会导致炎症分子大量释放，并可能引发中毒性休克综合征（TSS）。此前，我们生成了对超抗原有高亲和力的不同Vβ域的可溶性形式。然而，中和多种毒素需要一种具有更广泛谱的拮抗剂。在本研究中，我们将Vβ域串联表达为单链蛋白，并用单一制剂中和了具有临床重要性的超抗原葡萄球菌肠毒素B和TSS毒素-1。
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