A particle agglutination assay for rapid identification of heparin binding to coagulase-negative staphylococci
| Autor: | Corina Pascu, Torkel Wadström, Åsa Ljungh, Siiri Hirmo |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Microbiology (medical)
Coagulase Dalteparin Hot Temperature Time Factors Staphylococcus Suramin medicine.disease_cause Carrageenan Microbiology Excipients chemistry.chemical_compound Polysaccharides Direct agglutination test Agglutination Tests Endopeptidases medicine Humans Coloring Agents Latex beads biology Sodium periodate Heparin Tunicamycin Periodic Acid Periodic acid Anticoagulants General Medicine Trypan Blue biology.organism_classification Microspheres Anti-Bacterial Agents Culture Media Agglutination (biology) chemistry Luminescent Measurements Staphylococcus haemolyticus Evans Blue |
| Zdroj: | Journal of medical microbiology. 45(4) |
| ISSN: | 0022-2615 |
| Popis: | The heparin-binding properties of six different species of coagulase-negative staphylococci were examined by a particle agglutination assay. Heparin (mol. wt 4000-6000), mildly treated with sodium periodate, was covalently coupled to amino-modified latex beads (0.72 micron diameter). The particle agglutination assay was validated by comparing results with the adhesion (percentage binding of adherent cells) of coagulase-negative staphylococcal strains to heparinised microtitration plates. Of 38 different coagulase-negative staphylococcal strains tested, 30 showed agglutination reactivity with heparin-coated latex beads. Strains of different coagulase-negative staphylococcal species agglutinated heparin-coated latex beads to various extents (e.g., cells of Staphylococcus haemolyticus strains reacted more strongly than cells of S. epidermidis strains). The agglutination reaction was significantly inhibited by fucoidan, suramin, lambda-carrageenan and other sulphated compounds, but not by non-sulphated carbohydrate polymers such as hyaluronic acid. Agglutination of staphylococcal cells with heparin-coated latex beads was completely blocked by a cell-surface extract. These results suggest that structures responsible for heparin binding are exposed on the cell surface. |
| Databáze: | OpenAIRE |
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