L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of gram-positive bacteria, and activates the lectin pathway of complement
L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of gram-positive bacteria, and activates the lectin pathway of complement
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DOI：
10.4049/jimmunol.172.2.1198
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发表时间：
2004-01-15
影响因子：
4.4
通讯作者：
Schwaeble, WJ
中科院分区：
文献类型：
--
作者：
Lynch, NJ;Roscher, S;Schwaeble, WJ
当碳水化合物识别复合物和相关丝氨酸蛋白酶与病原体表面结合时，补体的凝集素途径被激活。三种识别子成分已被证明可形成活性起始复合物：甘露聚糖结合凝集素 (MBL)、L-ficolin 和 H-ficolin。 MBL 在抗菌宿主防御中的重要性已得到广泛认可，但丝胶蛋白的作用在很大程度上仍不清楚。该报告表明，L-ficolin 与脂磷壁酸 (LTA) 特异性结合，脂磷壁酸是所有革兰氏阳性细菌中发现的一种细胞壁成分。来自金黄色葡萄球菌的固定化 LTA 与血清中的 L-ficolin 复合物结合，这些复合物启动凝集素途径依赖性 C4 周转。 C4 活化与血清 L-ficolin 浓度相关，但与血清 MBL 水平无关。在从其他临床重要细菌（包括化脓链球菌和无乳链球菌）纯化的 LTA 上观察到 L-ficolin 结合和相应的 C4 周转水平。没有 LTA。制剂结合 MBL、H-ficolin 或经典途径识别分子 C1q。免疫学杂志，2004 年，172：1198-1202。
The lectin pathway of complement is activated when a carbohydrate recognition complex and associated serine proteases binds to the surface of a pathogen. Three recognition subcomponents have been shown to form active initiation complexes: mannan-binding lectin (MBL), L-ficolin, and H-ficolin. The importance of MBL in antimicrobial host defense is well recognized, but the role of the ficolins remains largely undefined. This report shows that L-ficolin specifically binds to lipoteichoic acid (LTA), a cell wall component found in all Gram-positive bacteria. Immobilized LTA from Staphylococcus aureus binds L-ficolin complexes from sera, and these complexes initiate lectin pathway-dependent C4 turnover. C4 activation correlates with serum L-ficolin concentration, but not with serum MBL levels. L-ficolin binding and corresponding levels of C4 turnover were observed on LTA purified from other clinically important bacteria, including Streptococcus pyogenes and Streptococcus agalactiae. None of the LTA. preparations bound MBL, H-ficolin, or the classical pathway recognition molecule, C1q. The Journal of Immunology, 2004, 172: 1198-1202.