Sundberg-Kövamees M, Holme T, Sjögren A
Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden.
Microb Pathog. 1994 Jul;17(1):63-8. doi: 10.1006/mpat.1994.1052.
Specific binding of Streptococcus pneumoniae to two proposed receptor structures was studied in a solid-phase assay. The assay was based on immunodetection of the pneumococci adhering to the receptors coated to microtiter plates. Non-specific binding owing to hydrophobic forces to uncoated wells could be abolished by treatment of the plates with a blocking buffer. Binding of the pneumococcal cells was demonstrated with the glycolipid asialo-GM1 as receptor with a previously suggested specificity for the disaccharide GalNAc beta 1-4Gal. A non-capsulated mutant bound with high efficiency to this receptor. Two capsulated strains also bound well, but with lower efficiency. Binding of the non-capsulated strain was also demonstrated with lactotriaosylceramide as receptor with a suggested specificity for the disaccharide GlcNAc beta 1-3Gal. The binding assay enables the comparison of the adherence of different strains to purified receptor molecules.
在固相分析中研究了肺炎链球菌与两种假定受体结构的特异性结合。该分析基于对粘附在包被于微量滴定板上的受体上的肺炎球菌进行免疫检测。通过用封闭缓冲液处理平板，可以消除由于疏水力导致的未包被孔的非特异性结合。以糖脂脱唾液酸GM1作为受体，证明肺炎球菌细胞具有结合能力，其对二糖GalNAcβ1-4Gal具有先前提出的特异性。一种非荚膜突变体高效结合该受体。两种荚膜菌株也能很好地结合，但效率较低。以乳糖三糖神经酰胺作为受体，也证明了非荚膜菌株的结合能力，其对二糖GlcNAcβ1-3Gal具有假定的特异性。该结合分析能够比较不同菌株对纯化受体分子的粘附情况。
