人源L-纤维胶凝蛋白对乙酰化寡糖的识别
Recognition of acetylated oligosaccharides by human L-ficolin.
作者信息
Krarup Anders, Mitchell Daniel A, Sim Robert B
机构信息
MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford UK.
出版信息
Immunol Lett. 2008 Jun 30;118(2):152-6. doi: 10.1016/j.imlet.2008.03.014. Epub 2008 Apr 28.
Abstract
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.
摘要
补体系统是一种能够中和入侵病原体的蛋白质级联反应。其激活途径之一是凝集素途径，该途径依赖于甘露聚糖结合凝集素（MBL）或纤维胶凝蛋白的结合。此前已经对L-纤维胶凝蛋白结合的特异性进行了研究，发现其结合依赖于乙酰基。如果这是唯一的要求，那么L-纤维胶凝蛋白将能够结合大多数哺乳动物的糖基化产物，因为它们含有乙酰化的单糖。为了进一步研究这一点，对L-纤维胶凝蛋白进行了聚糖阵列分析，其中研究了L-纤维胶凝蛋白与279种不同聚糖的结合情况。这些聚糖中只有少数在背景水平以上与L-纤维胶凝蛋白结合，但发现了明确的结构要求。
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