Recognition of acetylated oligosaccharides by human L-ficolin
Recognition of acetylated oligosaccharides by human L-ficolin
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DOI：
10.1016/j.imlet.2008.03.014
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发表时间：
2008-06-30
影响因子：
4.4
通讯作者：
Sim, Robert B.
中科院分区：
文献类型：
--
作者：
Krarup, Anders;Mitchell, Daniel A.;Sim, Robert B.
补体系统是能够中和入侵病原体的蛋白质级联。其活化途径之一是凝集素途径，其依赖于MBL或纤维胶凝蛋白的结合。之前已经研究了L-纤维胶凝蛋白结合的特异性，并且观察到结合依赖于乙酰基。如果这是唯一的要求，这将使L-纤维胶凝蛋白能够结合大多数哺乳动物糖基化，因为它们含有乙酰化单糖。为了进一步研究，对L-纤维胶凝蛋白进行聚糖阵列分析，其中研究了L-纤维胶凝蛋白与279种不同聚糖的结合。这些结合的L-纤维胶凝蛋白很少高于背景水平，但发现了明确的结构要求。(c)2008 Elsevier B. V.保留所有权利。
The complement system is a protein cascade capable of neutralizing invading pathogens. One of its activation pathways is the lectin pathway which is dependent on the binding of MBL or the ficolins. The specificity of L-ficolin binding has been investigated previously and it was observed that binding is dependent on acetyl groups. If this was the only requirement this would enable L-ficolin to bind to most mammalian glycosylations since they contain acetylated monosaccharides. To investigate this further L-ficolin was subjected to glycan-array analysis in which L-ficolin binding to 279 different glycans was investigated. Few of these bound L-ficolin above background level but clear structural requirements were discovered. (c) 2008 Elsevier B.V. All rights reserved.