Staphylococcus aureus bacteria, isolated from bone and joint infections, specifically interact with bone sialoprotein (BSP), a glycoprotein of bone and dentine extracellular matrix, via a cell-surface protein of Mr 97000 [Yacoub, Lindahl, Rubin, Wendel, Heinegård and Rydén, (1994) Eur. J. Biochem. 222, 919-925]. Amino acid sequences of seven trypsin fragments from the 97000-Mr BSP-binding protein were determined. A gene encoding a protein encompassing all seven peptide sequences was identified from chromosomal DNA isolated from S. aureus strain O24. This gene encodes a protein with 1171 amino acids, called BSP-binding protein (Bbp), which displays similarity to recently described proteins of the Sdr family from S. aureus. SdrC, SdrD and SdrE encode putative cell-surface proteins with no described ligand specificity. Bbp also shows similarity to a fibrinogen-binding protein from S. epidermidis called Fbe. A serine-aspartic acid repeat sequence was found close to the cell-wall-anchoring Leu-Pro-Xaa-Thr-Gly sequence in the C-terminal end of the protein. Escherichia coli cells were transformed with an expression vector containing a major part of the bbp gene fused to the gene for glutathione S-transferase. The affinity-purified fusion protein bound radiolabelled native BSP, and inhibited the binding of radiolabelled BSP to staphylococcal cells. Serum from patients suffering from bone and joint infection contained antibodies that reacted with the fusion protein of the BSP-binding protein, indicating that the protein is expressed during an infection and is immunogenic. The S. aureus Bbp protein may be important in the localization of bacteria to bone tissue, and thus might be of relevance in the pathogenicity of osteomyelitis.
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Research Article|
January 25 2000
A bone sialoprotein-binding protein from Staphylococcus aureus: a member of the staphylococcal Sdr family
Hui-shan TUNG
;
Hui-shan TUNG
*
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 575, SE-751 23 Uppsala, Sweden
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Bengt GUSS
;
Bengt GUSS
†
Department of Microbiology, Swedish University of Agricultural Sciences, Box 7025, SE-750 07 Uppsala, Sweden
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Ulf HELLMAN
;
Ulf HELLMAN
‡
Ludwig Institute for Cancer Research, Box 595, Biomedical Center, SE-751 24 Uppsala, Sweden
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Lena PERSSON
;
Lena PERSSON
*
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 575, SE-751 23 Uppsala, Sweden
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Kristofer RUBIN
;
Kristofer RUBIN
*
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 575, SE-751 23 Uppsala, Sweden
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Cecilia RYDÉN
Cecilia RYDÉN
1
*
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 575, SE-751 23 Uppsala, Sweden§
Department of Infectious Diseases, Academical Hospital, SE-751 85 Uppsala, Sweden1
To whom correspondence should be addressed, at the Department of Medical Biochemistry and Microbiology, Uppsala University (Cecilia.Ryden@medkem.uu.se).
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Biochem J (2000) 345 (3): 611-619.
Article history
Received:
June 24 1999
Revision Received:
September 29 1999
Accepted:
November 15 1999
Citation
Hui-shan TUNG, Bengt GUSS, Ulf HELLMAN, Lena PERSSON, Kristofer RUBIN, Cecilia RYDÉN; A bone sialoprotein-binding protein from Staphylococcus aureus: a member of the staphylococcal Sdr family. Biochem J 1 February 2000; 345 (3): 611–619. doi: https://doi.org/10.1042/bj3450611
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