Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, College of Medicine, Chang-Gung University, Kwei-san, Tao-yuan 333, Taiwan.
FEBS Lett. 2012 May 7;586(9):1294-9. doi: 10.1016/j.febslet.2012.03.024. Epub 2012 Apr 3.
Owing to the weak reactivities of monomeric DManα1 and Galβ1-->3/4GlcNAcβ (I(β)/II(β)) glycotopes with Ralstonia solanacearum lectin (RSL), their recognition roles were previously ignored. In this study, the interaction intensities of RSL toward four monomeric glycotopes LFucα1-->, DManα1--> and I(β)/II(β) within two combining sites were established by both enzyme-linked lectinosorbent and inhibition assays. It was found that high density of LFucα1--> complex enhanced the recognition intensities at LFucα1--> site, polyvalent DManα1--> was essential for binding at the DManα1--> site and polyvalent I(β)/II(β) was required at LFucα1--> site. The peculiar recognition systems of RSL are very different from other well known microbial lectins.
由于单体 DManα1 和 Galβ1-->3/4GlcNAcβ（I(β)/II(β)）糖基与罗尔斯通氏菌凝集素（RSL）的弱反应性，它们的识别作用以前被忽视了。在这项研究中，通过酶联凝集素结合和抑制试验建立了 RSL 对两个结合位点内的四个单体糖基 LFucα1-->, DManα1--> 和 I(β)/II(β)的相互作用强度。结果发现，LFucα1-->复合物的高密度增强了 LFucα1-->位点的识别强度，多价 DManα1-->是结合 DManα1-->位点所必需的，而多价 I(β)/II(β)则是在 LFucα1-->位点所必需的。RSL 的特殊识别系统与其他著名的微生物凝集素非常不同。
