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Purification of a bone sialoprotein-binding protein from Staphylococcus aureus
1Department of Medical and Physiological Chemistry, University of Uppsala, Sweden.
European Journal of Biochemistry
|June 15, 1994
Summary
Researchers purified a Staphylococcus aureus cell-wall protein that binds bone sialoprotein (BSP). This protein may explain how bacteria target bone infections like osteomyelitis.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Staphylococcus aureus infections often affect bone and joint tissues.
- Bone sialoprotein (BSP) is selectively bound by S. aureus strains from these infections.
Purpose of the Study:
- To purify and characterize the S. aureus cell-wall protein responsible for binding BSP.
- To investigate the protein's role in bacterial tropism in osteomyelitis.
Main Methods:
- Solubilization of staphylococcal cell-wall components using LiCl.
- Purification using preparative SDS/PAGE, Mono-Q anion-exchange chromatography, and BSP-Sepharose affinity chromatography.
- Analysis of purified protein by SDS/PAGE and protein-overlay experiments.
Main Results:
- A M(r) 97,000 polypeptide was purified, exhibiting specific binding to BSP.
- This protein was absent in S. aureus and Staphylococcus epidermidis strains lacking BSP-binding capacity.
- The purified protein demonstrated affinity for BSP in vitro.
Conclusions:
- A novel S. aureus cell-surface BSP-binding protein has been identified.
- This protein is likely involved in the specific targeting of S. aureus to bone tissue.
- The findings offer insights into the pathogenesis of osteomyelitis.