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

Fallgren, Corina; Utt, Meeme LU and Ljungh, Åsa LU (2001) In Journal of Medical Microbiology 50(6). p.547-557
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Medical Microbiology
volume
50
issue
6
pages
547 - 557
publisher
Lippincott Williams & Wilkins
external identifiers
  • wos:000168877900008
  • scopus:0035010254
ISSN
0022-2615
language
English
LU publication?
yes
id
e1ea31f7-ded7-4c2d-b186-c463a49831f9 (old id 132604)
alternative location
http://jmm.sgmjournals.org/cgi/content/abstract/50/6/547
date added to LUP
2007-07-09 15:52:04
date last changed
2018-01-07 08:50:12
@article{e1ea31f7-ded7-4c2d-b186-c463a49831f9,
  abstract     = {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.},
  author       = {Fallgren, Corina and Utt, Meeme and Ljungh, Åsa},
  issn         = {0022-2615},
  language     = {eng},
  number       = {6},
  pages        = {547--557},
  publisher    = {Lippincott Williams & Wilkins},
  series       = {Journal of Medical Microbiology},
  title        = {Isolation and characterisation of a 17-kDa staphylococcal heparin-binding protein with broad specificity},
  volume       = {50},
  year         = {2001},
}