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纯化的单体配体-MD-2复合物揭示了革兰氏阴性细菌内毒素激活和拮抗TLR4的分子和结构要求。

Purified monomeric ligand.MD-2 complexes reveal molecular and structural requirements for activation and antagonism of TLR4 by Gram-negative bacterial endotoxins.

作者信息

Gioannini Theresa L, Teghanemt Athmane, Zhang DeSheng, Esparza Gregory, Yu Liping, Weiss Jerrold

机构信息

The Inflammation Program, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, 2501 Crosspark Rd, Coralville, IA, 52241, USA.

出版信息

Immunol Res. 2014 Aug;59(1-3):3-11. doi: 10.1007/s12026-014-8543-y.

Abstract

A major focus of work in our laboratory concerns the molecular mechanisms and structural bases of Gram-negative bacterial endotoxin recognition by host (e.g., human) endotoxin-recognition proteins that mediate and/or regulate activation of Toll-like receptor (TLR) 4. Here, we review studies of wild-type and variant monomeric endotoxin.MD-2 complexes first produced and characterized in our laboratories. These purified complexes have provided unique experimental reagents, revealing both quantitative and qualitative determinants of TLR4 activation and antagonism. This review is dedicated to the memory of Dr. Theresa L. Gioannini (1949-2014) who played a central role in many of the studies and discoveries that are reviewed.

摘要

我们实验室的主要工作重点是宿主(如人类)内毒素识别蛋白识别革兰氏阴性菌内毒素的分子机制和结构基础,这些蛋白介导和/或调节Toll样受体(TLR)4的激活。在此,我们综述了在我们实验室首次产生并表征的野生型和变体单体内毒素-MD-2复合物的研究。这些纯化的复合物提供了独特的实验试剂,揭示了TLR4激活和拮抗作用的定量和定性决定因素。这篇综述是为了纪念特蕾莎·L·乔阿尼尼博士(1949-2014),她在许多被综述的研究和发现中发挥了核心作用。

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