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Identification of the binding sequence for Staphylococcus aureus in bone sialoprotein
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences. (Friman, Infektionssjukdomar)
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1997 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 327, no 3, 825-829 p.Article in journal (Refereed) Published
Abstract [ar]

Bone sialoprotein is a glycoprotein of the bone and dentine extracellular matrix. This protein consists of 320 amino acids, of which 25% are glutamic and aspartic acid residues. Sialic acid, containing oligosaccharides and tyrosine sulphate residues, supplies additional polyanionic properties. Staphylococcal cells, isolated from patients suffering from infection of bone tissue, bind the bone-derived sialoprotein, an interaction which is specifically inhibited by the recombinant bone sialoprotein core protein. We have previously shown that the 150 N-terminal amino acid residues of bone sialoprotein are responsible for the binding to staphylococcal cells. By using recombinant deleted variants of bone sialoprotein and synthetic peptides, we have now localized the staphylococcal binding site to less than 10 residues within the N-terminal part of the protein.

Place, publisher, year, edition, pages
1997. Vol. 327, no 3, 825-829 p.
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Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-55385OAI: oai:DiVA.org:uu-55385DiVA: diva2:83293
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2017-12-04Bibliographically approved

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218863/
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