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脂蛋白是金黄色葡萄球菌细胞壁成分中主要的Toll样受体2配体。

Lipoprotein is a predominant Toll-like receptor 2 ligand in Staphylococcus aureus cell wall components.

作者信息

Hashimoto Masahito, Tawaratsumida Kazuki, Kariya Hiroyuki, Aoyama Kazue, Tamura Toshihide, Suda Yasuo

机构信息

Department of Nanostructure and Advanced Materials, Kagoshima University, Korimoto 1-21-40, Kagoshima 890-0065, Japan.

出版信息

Int Immunol. 2006 Feb;18(2):355-62. doi: 10.1093/intimm/dxh374. Epub 2005 Dec 22.

Abstract

Lipoteichoic acid (LTA) derived from Staphylococcus aureus is reported to be a ligand of Toll-like receptor 2 (TLR2). In this study, we demonstrated that lipoproteins obtained from S. aureus are potent activators of TLR2. A fraction obtained by Triton X-114 phase partitioning activated cells through TLR2. The fraction contained proteins and LTA. The activity was detected in compounds in a mass range of 12-40 kDa. Proteinase K digested the active compounds into lower molecular weight active materials <10 kDa. In contrast, hydrofluoric acid treatment, which decomposes LTA, did not alter the molecular mass of the active compounds. Further, most of the activity was abrogated by lipoprotein lipase digestion. These results suggested that lipoproteins are predominant TLR2 ligands in S. aureus cell wall components.

摘要

据报道,源自金黄色葡萄球菌的脂磷壁酸(LTA)是Toll样受体2(TLR2)的配体。在本研究中,我们证明从金黄色葡萄球菌获得的脂蛋白是TLR2的有效激活剂。通过Triton X-114相分配获得的一个组分通过TLR2激活细胞。该组分含有蛋白质和LTA。在12 - 40 kDa质量范围内的化合物中检测到该活性。蛋白酶K将活性化合物消化成分子量小于10 kDa的低分子量活性物质。相反,分解LTA的氢氟酸处理并未改变活性化合物的分子量。此外,大多数活性被脂蛋白脂肪酶消化消除。这些结果表明脂蛋白是金黄色葡萄球菌细胞壁成分中主要的TLR2配体。

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