Staphylococci Bind Heparin-Binding Host Growth Factors |
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Authors: | Corina Pascu Åsa Ljungh Torkel Wadström |
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Institution: | Department of Medical Microbiology, University of Lund, S?lvegatan 23, S-223 62 Lund, Sweden, SE
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Abstract: | Staphylococcus aureus, which mediated binding to heparan sulfate, and also strains of coagulase-negative staphylococci (CNS) adhered in high numbers
to polymers with end-point attached heparin. A characteristic feature of several cell growth factors is strong affinity for
heparin. In the present study, binding of the 125I-labeled heparin-binding growth factors (HBGF), acidic and basic fibroblast growth factor (aFGF, bFGF), and platelet-derived
growth factor (PDGF) by S. aureus and CNS strains was examined. Staphylococcal strains used in this study bind bFGF and PDGF, but not aFGF. The binding of
bFGF and PDGF was time dependent, influenced by pH and ionic strength for S. aureus Cowan 1. Preincubation of staphylococcal cells with unlabeled bFGF enhanced bFGF binding, but heparin, protamine sulfate,
poly-L-lysine, and suramin were potent inhibitors of 125I-bFGF binding to cells of S. aureus Cowan 1. Glycosaminoglycans of comparable size (chondroitin sulfate), other polysulfated polymers (λ-carrageenan, fucoidan),
and some polysulfated polysaccharides (dextran sulfate, pentosan polysulfate) inhibited binding of both GFs to various extents.
The partial inhibition of binding of both GFs after protease and periodate treatments indicates that both proteinaceous and
other carbohydrate moieties participate in the binding. A lysozyme cell surface extract and bacterial lysates of S. aureus Cowan 1 competitively inhibited binding of 125I-bFGF and 125I-PDGF. These results suggest that staphylococci have the ability to bind two of the HBGFs, bFGF and PDGF, but not aFGF, via
more than one cell structure. These binding structures seem to be exposed on the cell surface and deeply anchored in the cytoplasmic
membrane as well. |
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