Advanced

The N-terminal of thrombospondin-1 is essential for coagulase-negative staphylococcal binding

Yanagisawa, Naoko LU ; Li, Dai-Qing LU and Ljungh, Åsa LU (2001) In Journal of Medical Microbiology 50(8). p.712-719
Abstract
Bacterial binding was studied to determine whether thrombospondin-1 (TSP) acts as a ligand in attachment of coagulase-negative staphylococci (CNS). Twenty-five of 27 CNS strains bound soluble TSP. Staphylococcus epidermidis J9P bound 125I-labelled TSP in a dose-dependent manner. Scatchard plot analysis of the binding of TSP by strain J9P revealed two Kd values of 6.4x10-95muM and 2.9x10-85muM. The binding structures of strain J9P were sensitive to protease and were resistant to heat treatment. Unlabelled TSP and recombinant von Willebrand factor inhibited binding of TSP by strain J9P, but other proteins or monosaccharides did not. Heparin inhibited binding of TSP to strain J9P and two other S. epidermidis strains, BD5703 and BD969. Fusion... (More)
Bacterial binding was studied to determine whether thrombospondin-1 (TSP) acts as a ligand in attachment of coagulase-negative staphylococci (CNS). Twenty-five of 27 CNS strains bound soluble TSP. Staphylococcus epidermidis J9P bound 125I-labelled TSP in a dose-dependent manner. Scatchard plot analysis of the binding of TSP by strain J9P revealed two Kd values of 6.4x10-95muM and 2.9x10-85muM. The binding structures of strain J9P were sensitive to protease and were resistant to heat treatment. Unlabelled TSP and recombinant von Willebrand factor inhibited binding of TSP by strain J9P, but other proteins or monosaccharides did not. Heparin inhibited binding of TSP to strain J9P and two other S. epidermidis strains, BD5703 and BD969. Fusion proteins of the type 1 repeats, type 2 repeats, type 3 repeats and C-terminal domain of TSP or the synthetic Arg-Gly-Asp peptide did not inhibit binding of TSP to bacteria. TSP promoted adhesion of S. epidermidis strains when it was immobilised on polymer surfaces. These results indicate that the specific interaction between CNS and TSP may contribute to bacterial adhesion on biomaterial surfaces. The N-terminal heparin-binding domain of TSP appears to be the major region for recognition by CNS. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Medical Microbiology
volume
50
issue
8
pages
712 - 719
publisher
Lippincott Williams & Wilkins
external identifiers
  • wos:000169989500010
  • scopus:0034915966
ISSN
0022-2615
language
English
LU publication?
yes
id
36b462d2-45c1-4f10-b3e9-64a790271dca (old id 132619)
alternative location
http://jmm.sgmjournals.org/cgi/content/abstract/50/8/712
date added to LUP
2007-07-11 09:08:07
date last changed
2018-01-07 08:45:27
@article{36b462d2-45c1-4f10-b3e9-64a790271dca,
  abstract     = {Bacterial binding was studied to determine whether thrombospondin-1 (TSP) acts as a ligand in attachment of coagulase-negative staphylococci (CNS). Twenty-five of 27 CNS strains bound soluble TSP. Staphylococcus epidermidis J9P bound 125I-labelled TSP in a dose-dependent manner. Scatchard plot analysis of the binding of TSP by strain J9P revealed two Kd values of 6.4x10-95muM and 2.9x10-85muM. The binding structures of strain J9P were sensitive to protease and were resistant to heat treatment. Unlabelled TSP and recombinant von Willebrand factor inhibited binding of TSP by strain J9P, but other proteins or monosaccharides did not. Heparin inhibited binding of TSP to strain J9P and two other S. epidermidis strains, BD5703 and BD969. Fusion proteins of the type 1 repeats, type 2 repeats, type 3 repeats and C-terminal domain of TSP or the synthetic Arg-Gly-Asp peptide did not inhibit binding of TSP to bacteria. TSP promoted adhesion of S. epidermidis strains when it was immobilised on polymer surfaces. These results indicate that the specific interaction between CNS and TSP may contribute to bacterial adhesion on biomaterial surfaces. The N-terminal heparin-binding domain of TSP appears to be the major region for recognition by CNS.},
  author       = {Yanagisawa, Naoko and Li, Dai-Qing and Ljungh, Åsa},
  issn         = {0022-2615},
  language     = {eng},
  number       = {8},
  pages        = {712--719},
  publisher    = {Lippincott Williams & Wilkins},
  series       = {Journal of Medical Microbiology},
  title        = {The N-terminal of thrombospondin-1 is essential for coagulase-negative staphylococcal binding},
  volume       = {50},
  year         = {2001},
}