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Specific binding of Streptococcus pneumoniae to two receptor saccharide structures
M Sundberg-Kövamees1, T Holme, A Sjögren
1Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden.
Microbial Pathogenesis
|July 1, 1994
Summary
Streptococcus pneumoniae efficiently binds to the glycolipid asialo-GM1, a receptor for the disaccharide GalNAc beta 1-4Gal. This study developed a solid-phase assay to compare pneumococcal strain adherence to purified receptor molecules.
Area of Science:
- Microbiology
- Biochemistry
Background:
- Streptococcus pneumoniae adherence to host cells is crucial for infection.
- Specific interactions with host cell receptors mediate pneumococcal colonization.
Purpose of the Study:
- To investigate the specific binding of Streptococcus pneumoniae to two proposed receptor structures using a solid-phase assay.
- To compare the adherence efficiency of different pneumococcal strains to purified glycolipid receptors.
Main Methods:
- A solid-phase assay utilizing immunodetection of pneumococci adhered to microtiter plates coated with receptor structures.
- Blocking buffer treatment to eliminate non-specific binding due to hydrophobic forces.
- Testing binding of non-capsulated and capsulated S. pneumoniae strains to asialo-GM1 and lactotriaosylceramide.
Main Results:
- Pneumococcal binding was demonstrated with asialo-GM1, a receptor with specificity for GalNAc beta 1-4Gal.
- A non-capsulated S. pneumoniae mutant exhibited high binding efficiency to asialo-GM1.
- Both capsulated and non-capsulated strains bound to lactotriaosylceramide, a receptor for GlcNAc beta 1-3Gal, with varying efficiencies.
Conclusions:
- The developed binding assay effectively quantifies Streptococcus pneumoniae adherence to purified receptor molecules.
- Asialo-GM1 and lactotriaosylceramide serve as specific receptors for S. pneumoniae, with binding influenced by capsular status.