Work

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

Year: 1997

Type: article

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.

Source: Biochemical Journal

DOI: 10.1042/bj3270825

Authors: Cecilia RYDÉN, Hui-Shan TUNG, Victor NIKOLAEV, Åke ENGSTRÖM, Åke OLDBERG

Institutions: Uppsala University, Lund University

Language: English

Topic: Bone and Dental Protein Studies

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: bronze

Funders: Medical Research Council, Socialstyrelsen