Crocus sativus lectin recognizes Man3GlcNAc in the N-glycan core structure.
Crocus sativus lectin recognizes Man3GlcNAc in the N-glycan core structure.
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番红花凝集素可识别 N-聚糖核心结构中的 Man3GlcNAc。
DOI：
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发表时间：
2000
影响因子：
4.8
通讯作者：
Y. Lee
中科院分区：
文献类型：
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作者：
Y. Oda;K. Nakayama;B. Abdul;M. Kinoshita;O. Hashimoto;N. Kawasaki;T. Hayakawa;K. Kakehi;N. Tomiya;Y. Lee
番红花凝集素（CSL）是一种真正的甘露糖特异性植物凝集素，具有独特的结合特异性，使其区别于其他凝集素。我们研究了CSL的糖结合特异性详细的溶液相方法（荧光偏振）和三个固相方法（流动注射，表面等离子体共振，和微量滴定板），使用一些不同的糖肽和寡糖。CSL结合N-聚糖核心中的支链甘露三糖结构。用GlcNAc取代Manalpha（1-3）Man分支中的末端Man比掩蔽Manalpha（1-6）Man分支中的末端Man显著降低结合亲和力。最有趣的是，N-聚糖核心结构中的β-Man连接的GlcNAc极大地促进了结合。这种GlcNAc的作用如此强烈，以至于它可以基本上抵消取代对非还原性末端Man残基的负面影响。另一方面，通常与N-聚糖中的Asn连接的GlcNAc和在GlcNAc的6位连接的l-Fuc与结合无关。二等分的GlcNAc既不有助于也不干扰结合。CSL的这种独特的结合特异性为其在分析和制备应用中的使用提供了许多可能性。
Crocus sativus lectin (CSL) is one of the truly mannose-specific plant lectins that has a unique binding specificity that sets it apart from others. We studied sugar-binding specificity of CSL in detail by a solution phase method (fluorescence polarization) and three solid phase methods (flow injection, surface plasmon resonance, and microtiter plate), using a number of different glycopeptides and oligosaccharides. CSL binds the branched mannotriose structure in the N-glycan core. Substitution of the terminal Man in the Manalpha(1-3)Man branch with GlcNAc drastically decreases binding affinity much more than masking of the terminal Man in the Manalpha(1-6)Man branch. Most interestingly, the beta-Man-linked GlcNAc in N-glycan core structure contributes greatly to the binding. The effect of this GlcNAc is so strong that it can substantially offset the negative effect of substitution on the nonreducing terminal Man residues. On the other hand, the GlcNAc that is usually attached to Asn in N-glycans and the l-Fuc linked at the 6-position of the GlcNAc are irrelevant to the binding. A bisecting GlcNAc neither contributes to nor interferes with the binding. This unique binding specificity of CSL offers many possibilities of its use in analytical and preparative applications.