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Isolation and characterisation of a 17-kDa staphylococcal heparin-binding protein with broad specificity

In English

Författare

  • Corina Fallgren
  • Meeme Utt
  • Åsa Ljungh

Summary, in English

A previous study reported the ability of staphylococci to bind heparin and heparin-dependent host growth factors. The present study isolated and identified heparin- and basic fibroblast growth factor (bFGF)-binding surface components of S. epidermidis strain RP12 and S. haemolyticus strain SM 131. The staphylococcal heparin-binding component(s) were purified by affinity chromatography on heparin-Sepharose and a major heparin-binding protein, here designated HBP, was identified by immunoblot in these two coagulase-negative staphylococcal (CNS) species. The HBP was shown to be acidic with an approximate pI of 4.6 and a molecular mass around 17 kDa. The binding of heparin to HBP was inhibited by heparin, fucoidan, pentosan polysulphate and various other sulphated polysaccharides, but not by non-sulphated compounds. However, the purified HBP from both S. epidermidis and S. haemolyticus revealed broad specificity, and also bound bFGF, thrombospondin, von Willebrand factor and, weakly, fibrinogen. The N-terminal sequences of the 17-kDa HBP from S. epidermidis and S. haemolyticus showed only limited identity. Comparison of the first 15 amino acid residues derived from either strain with known sequences in the protein databases revealed no close similarities. Taken together, these results suggest that the adhesion of at least some CNS to host sulphated glycosaminoglycans may be mediated by a previously uncharacterised group of surface proteins.

Publiceringsår

2001

Språk

Engelska

Sidor

547-557

Publikation/Tidskrift/Serie

Journal of Medical Microbiology

Volym

50

Issue

6

Dokumenttyp

Artikel i tidskrift

Förlag

Lippincott Williams & Wilkins

Ämne

  • Microbiology in the medical area

Status

Published

Forskningsgrupp

  • Celiac Disease and Diabetes Unit

ISBN/ISSN/Övrigt

  • ISSN: 0022-2615