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Related Experiment Videos

Staphylococci bind heparin-binding host growth factors

C Pascu1, A Ljungh, T Wadström

  • 1Department of Medical Microbiology, University of Lund, Sweden.

Current Microbiology
|April 1, 1996
PubMed
Summary
This summary is machine-generated.

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Staphylococcus aureus and coagulase-negative staphylococci bind heparin-binding growth factors (HBGFs) like basic fibroblast growth factor (bFGF) and platelet-derived growth factor (PDGF). These bacteria utilize multiple cell surface structures for binding these essential growth factors.

Area of Science:

  • Microbiology
  • Biochemistry
  • Cell Biology

Background:

  • Staphylococcus aureus and coagulase-negative staphylococci (CNS) can bind to heparin.
  • Several cell growth factors, including heparin-binding growth factors (HBGFs), exhibit a strong affinity for heparin.
  • Understanding bacterial interactions with HBGFs is crucial for comprehending host-pathogen dynamics and potential therapeutic targets.

Purpose of the Study:

  • To investigate the binding capabilities of Staphylococcus aureus and CNS strains to specific HBGFs: acidic fibroblast growth factor (aFGF), basic fibroblast growth factor (bFGF), and platelet-derived growth factor (PDGF).
  • To characterize the nature of the binding interactions, including time dependence, and the influence of environmental factors like pH and ionic strength.
  • To identify the bacterial cell structures involved in HBGF binding and the chemical moieties mediating these interactions.

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Main Methods:

  • Radiolabeling of HBGFs (aFGF, bFGF, PDGF) with 125I for binding assays.
  • Incubation of Staphylococcus aureus and CNS strains with labeled HBGFs under varying conditions.
  • Inhibition assays using unlabeled HBGFs, heparin, protamine sulfate, poly-L-lysine, suramin, and various glycosaminoglycans and polysulfated polymers.
  • Enzymatic and chemical treatments (protease, periodate) of bacterial cells to probe binding structures.
  • Competitive inhibition assays using bacterial cell surface extracts and lysates.

Main Results:

  • Staphylococcal strains demonstrated binding to bFGF and PDGF, but not aFGF.
  • Binding of bFGF and PDGF was time-dependent and influenced by pH and ionic strength in Staphylococcus aureus Cowan 1.
  • Heparin, protamine sulfate, poly-L-lysine, and suramin significantly inhibited 125I-bFGF binding.
  • Various glycosaminoglycans and polysulfated polysaccharides showed varying degrees of inhibition for both growth factors.
  • Protease and periodate treatments partially inhibited growth factor binding, suggesting involvement of both protein and carbohydrate moieties.
  • Bacterial cell surface extracts and lysates competitively inhibited the binding of 125I-bFGF and 125I-PDGF.

Conclusions:

  • Staphylococci possess the ability to bind specific HBGFs, namely bFGF and PDGF, but not aFGF.
  • The binding mechanism involves multiple bacterial cell surface structures, potentially including both protein and carbohydrate components.
  • These binding structures are exposed on the cell surface and may be anchored within the cytoplasmic membrane.