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A novel von Willebrand factor binding protein expressed by Staphylococcus aureus

Bjerketorp, Joakim; Nilsson, Martin; Ljungh, Åsa LU ; Flock, Jan-Ingmar; Jacobsson, Karin and Frykberg, Lars (2002) In Microbiology1994-01-01+01:00 148. p.2037-2044
Abstract
When a shotgun phage-display library of Staphylococcus aureus Newman was affinity selected (panned) against recombinant von Willebrand factor (vWf), a novel von Willebrand factor binding protein (vWbp) was found. Experimental data indicate that the interaction between vWbp and vWf is very specific and mediated by a region of 26 aa residues in the C-terminal part of vWbp. vWbp has an N-terminal secretory signal sequence but no cell wall anchoring motif, suggesting a soluble extracellular location. Mature vWbp could be purified from the culture supernatant and the identity of the protein was confirmed by N-terminal sequencing. vWbp migrates with an apparent molecular mass of 66 kDa and the deduced protein consists of 482 aa. The gene... (More)
When a shotgun phage-display library of Staphylococcus aureus Newman was affinity selected (panned) against recombinant von Willebrand factor (vWf), a novel von Willebrand factor binding protein (vWbp) was found. Experimental data indicate that the interaction between vWbp and vWf is very specific and mediated by a region of 26 aa residues in the C-terminal part of vWbp. vWbp has an N-terminal secretory signal sequence but no cell wall anchoring motif, suggesting a soluble extracellular location. Mature vWbp could be purified from the culture supernatant and the identity of the protein was confirmed by N-terminal sequencing. vWbp migrates with an apparent molecular mass of 66 kDa and the deduced protein consists of 482 aa. The gene encoding vWbp, named vwb, was present in all S. aureus strains investigated. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Microbiology1994-01-01+01:00
volume
148
pages
2037 - 2044
publisher
MAIK Nauka/Interperiodica
external identifiers
  • pmid:12101292
  • wos:000176710700008
  • scopus:0036062019
ISSN
1465-2080
language
English
LU publication?
yes
id
2dcba8f5-1ad1-4e9e-be04-7fef76a9d0c5 (old id 132624)
alternative location
http://mic.sgmjournals.org/cgi/content/abstract/148/7/2037
date added to LUP
2007-07-09 15:26:55
date last changed
2017-08-27 03:57:55
@article{2dcba8f5-1ad1-4e9e-be04-7fef76a9d0c5,
  abstract     = {When a shotgun phage-display library of Staphylococcus aureus Newman was affinity selected (panned) against recombinant von Willebrand factor (vWf), a novel von Willebrand factor binding protein (vWbp) was found. Experimental data indicate that the interaction between vWbp and vWf is very specific and mediated by a region of 26 aa residues in the C-terminal part of vWbp. vWbp has an N-terminal secretory signal sequence but no cell wall anchoring motif, suggesting a soluble extracellular location. Mature vWbp could be purified from the culture supernatant and the identity of the protein was confirmed by N-terminal sequencing. vWbp migrates with an apparent molecular mass of 66 kDa and the deduced protein consists of 482 aa. The gene encoding vWbp, named vwb, was present in all S. aureus strains investigated.},
  author       = {Bjerketorp, Joakim and Nilsson, Martin and Ljungh, Åsa and Flock, Jan-Ingmar and Jacobsson, Karin and Frykberg, Lars},
  issn         = {1465-2080},
  language     = {eng},
  pages        = {2037--2044},
  publisher    = {MAIK Nauka/Interperiodica},
  series       = {Microbiology1994-01-01+01:00},
  title        = {A novel von Willebrand factor binding protein expressed by Staphylococcus aureus},
  volume       = {148},
  year         = {2002},
}