Andersson B, Dahmén J, Frejd T, Leffler H, Magnusson G, Noori G, Edén C S
J Exp Med. 1983 Aug 1;158(2):559-70. doi: 10.1084/jem.158.2.559.
Glycoconjugates containing the disaccharide unit GlcNAc beta 1 leads to 3Gal beta were suggested as receptors for pneumococci adhering to human pharyngeal epithelial cells. The receptor activity was detected both by inhibition of adhesion by an excess of free oligosaccharide and by induction or increase of adhesion after coating of target cells with glycolipid. Studies with free natural and synthetic oligosaccharides identified the disaccharide GlcNAc beta 1 leads to 3Gal beta as one critical binding site. The specificity of recognition was shown inter alia by the lack of inhibitory activity of GlcNAc beta 1 leads to 4Gal beta, which differs only in the linkage of the two sugars. Specific interference with pneumococcal adhesion by administration of soluble receptor sugar may improve our understanding of the role of adhesion in vivo.
含有二糖单位β-1,3连接的N-乙酰葡糖胺（GlcNAc）和β-半乳糖（Gal）的糖缀合物被认为是肺炎球菌黏附人咽上皮细胞的受体。通过过量游离寡糖抑制黏附以及用糖脂包被靶细胞后诱导或增加黏附，均可检测到受体活性。对游离天然和合成寡糖的研究确定二糖β-1,3连接的N-乙酰葡糖胺和β-半乳糖是一个关键结合位点。尤其是β-1,4连接的N-乙酰葡糖胺和β-半乳糖缺乏抑制活性，这表明识别具有特异性，二者仅在两种糖的连接方式上有所不同。通过给予可溶性受体糖特异性干扰肺炎球菌黏附，可能会增进我们对黏附在体内作用的理解。
