Specific binding of Streptococcus pneumoniae to two receptor saccharide structures.
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.
Sundberg-Kövamees
M
M
Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden.
Holme
T
T
Sjögren
A
A
D001422:Bacterial Adhesion / Q000502:physiology*; D002240:Carbohydrate Sequence; D004187:Disaccharides / Q000378:metabolism*; D005677:G(M1) Ganglioside / Q000378:metabolism*; D007124:Immunoenzyme Techniques; D008969:Molecular Sequence Data; D013296:Streptococcus pneumoniae / Q000378:metabolism*
D004187:Disaccharides; D005677:G(M1) Ganglioside; C018835:asialo GM1 ganglioside