Identification by surface plasmon resonance of the mycobacterial lipomannan and lipoarabinomannan domains involved in binding to CD14 and LPS-binding protein
Identification by surface plasmon resonance of the mycobacterial lipomannan and lipoarabinomannan domains involved in binding to CD14 and LPS-binding protein
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DOI：
10.1016/j.febslet.2007.02.056
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发表时间：
2007-04-03
期刊：
影响因子：
3.5
通讯作者：
Legrand, Dominique
中科院分区：
文献类型：
--
作者：
Elass, Elisabeth;Coddeville, Bernadette;Legrand, Dominique
分枝杆菌脂聚糖，脂甘露聚糖（LM）和脂阿拉伯糖甘露聚糖（LAM），通过与toll样受体（TLRs）等模式识别受体的相互作用调节宿主防御机制。我们开发了一种表面等离子体共振实验，通过固定化CD14和lps结合蛋白（LBP）来促进细菌糖脂向TLRs的呈递，来分析堪萨斯分枝杆菌LM或LAM识别的分子基础。LM/LAM对CD14的亲和力均高于LBP。动力学和Scatchard分析与涉及单类结合位点的模型一致。这些相互作用需要脂质锚，而不是LM或LAM的碳水化合物结构域。我们还提供证据表明，加入重组LBP可以通过TLR1/ tlr2依赖机制增强LM或LAM对巨噬细胞基质金属蛋白酶-9的表达和分泌的刺激作用。(c) 2007年欧洲生化学会联合会。Elsevier B.V.版权所有。
The mycobacterial lipoglycans, lipomannan (LM) and lipoarabinomannan (LAM), regulate host defence mechanisms through their interaction with pattern recognition receptors such as Toll-like receptors (TLRs). We have developed a surface plasmon resonance assay to analyse the molecular basis for the recognition of Mycobacterium kansasii LM or LAM, by immobilized CD14 and LPS-binding protein (LBP) both being capable to promote presentation of bacterial glycolipids to TLRs. The affinity of either LM/LAM was higher to CD14 than to LBP. Kinetic and Scatchard analyses were consistent with a model involving a single class of binding sites. These interactions required the lipidic anchor, but not the carbohydrate domains, of LM or LAM. We also provide evidence that addition of recombinant LBP enhanced the stimulatory effect of LM or LAM on matrix metalloproteinase-9 expression and secretion in macrophages, through a TLR1/TLR2-dependent mechanism. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.