Binding of extracellular matrix molecules by enterococci.
The bacterial surfaces of enterococci are not uniform. This fact is confirmed by several studies and by our results when great differences between individual strains with regard to their cell surface hydrophobicity, binding of eight ECM (extracellular matrix) molecules immobilized on latex beads and four selected ECM molecules in microtiter plates were observed. The strains expressing high binding of ECM molecules (e.g., HJ 18, HJ 23, HJ 24, HJ 26, HJ 28, HJ 36, etc.) were found among Enterococcus faecalis and E. faecium by PAA (particle agglutination assay). On the other hand, weak ECM binders (e.g., HJ 21, HJ 32, HJ 34, HJ 38, HJ 39, HJ 42, HJ 43) were also found. A direct correlation was found between porcine mucin and fetuin binding ability of eight selected strains tested in microtiter plates and by PAA. Moreover, the influence of tunicamycin treatment was different because significant (P < 0.001) blocking effect of tunicamycin was observed with two selected strains (HJ 26 and HJ 36), whereas two strains (HJ 18 and HJ 22) were not significantly affected in their fetuin binding. The treatment of six enterococcal strains with proteolytic enzymes, pronase P, and trypsin, and with sodium metaperiodate also significantly (P < 0.001) decreased their fetuin binding. This suggests that both protein and carbohydrate moieties are involved in the binding of immobilized fetuin. However, the influence of these chemicals on the fetuin binding by individual strains was different.
Department of Microbiology, Institute of Animal Physiology, Slovak Academy of Sciences, Soltésovej 4-6, 040 01 Kosice, Slovakia. styriak@saske.sk
Igor
I
Tyriak
Sa
S
Ljungh
D000372:Agglutination Tests; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001422:Bacterial Adhesion / Q000502:physiology; D013293:Enterococcus faecalis / Q000378:metabolism*; D016984:Enterococcus faecium / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007781:Lactoferrin / Q000378:metabolism; D008863:Microspheres; D009077:Mucins / Q000378:metabolism; D010504:Periodic Acid / Q000494:pharmacology; D011402:Pronase / Q000494:pharmacology; D011485:Protein Binding; D013499:Surface Properties; D014357:Trypsin / Q000494:pharmacology; D014415:Tunicamycin / Q000494:pharmacology; D019096:Vitronectin / Q000378:metabolism; D000509:alpha-Fetoproteins / Q000378:metabolism
D000900:Anti-Bacterial Agents; D016326:Extracellular Matrix Proteins; D009077:Mucins; D019096:Vitronectin; D000509:alpha-Fetoproteins; D010504:Periodic Acid; D014415:Tunicamycin; C009288:metaperiodate; D007781:Lactoferrin; D014357:Trypsin; D011402:Pronase