Staphylococcus aureus causing osteomyelitis binds to a nonapeptide sequence in bone sialoprotein.

C Rydén; H S Tung; V Nikolaev; A Engström; A Oldberg

doi:10.1042/bj3270825

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PubMed · 9581562

Staphylococcus aureus causing osteomyelitis binds to a nonapeptide sequence in bone sialoprotein.

C Rydén·H S Tung·V Nikolaev·A Engström·A Oldberg

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Abstract

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.

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Amino Acid Sequence Binding Sites Glutathione Transferase Humans Integrin-Binding Sialoprotein Molecular Sequence Data Osteomyelitis Peptides Recombinant Fusion Proteins Sequence Deletion Sialoglycoproteins Staphylococcal Infections Staphylococcus aureus Journal Article Research Support, Non-U.S. Gov't

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C Rydén, H S Tung, V Nikolaev, A Engström, A Oldberg. 1997-11-01. Staphylococcus aureus causing osteomyelitis binds to a nonapeptide sequence in bone sialoprotein.. https://doi.org/10.1042/bj3270825

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