A novel von Willebrand factor binding protein expressed by Staphylococcus aureus
(2002) In Microbiology 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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/132624
- author
- Bjerketorp, Joakim ; Nilsson, Martin ; Ljungh, Åsa LU ; Flock, Jan-Ingmar ; Jacobsson, Karin and Frykberg, Lars
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Microbiology
- 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
- 2016-04-01 11:55:34
- date last changed
- 2022-03-13 02:39:30
@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 = {{Microbiology}},
title = {{A novel von Willebrand factor binding protein expressed by Staphylococcus aureus}},
url = {{https://lup.lub.lu.se/search/files/2705062/624326.pdf}},
volume = {{148}},
year = {{2002}},
}