A von Willebrand factor-binding protein from Staphylococcus lugdunensis
(2004) In FEMS Microbiology Letters 234(1). p.155-161- Abstract
- In the present study, a phage display library covering the genome of Staphylococcus lugdunensis, was affinity-selected against von Willebrand factor (vWf). This led to the identification of a gene, vwbl, encoding a Putative cell surface protein of 2060 amino acids, denoted vWbl. The deduced protein has an overall organisation typical of staphylococcal cell Surface proteins, with an N-terminal signal peptide, and a C-terminal cell wall sorting signal. The vWf-binding part is located in repetitive domains and antibodies against vWbl or vWf can inhibit the binding. Southern blot analysis showed that vwbl was present in the 12 S. lugdunensis strains tested. (C) 2004 Federation of European Microbiological Societies.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/279441
- author
- Nilsson, M ; Bjerketorp, J ; Wiebensjo, A ; Ljungh, Åsa LU ; Frykberg, L and Guss, B
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- von Willebrand factor, display, phage, coagulase-negative staphylococci, Staphylococcus lugdunensis, adhesin, LPXTG motif
- in
- FEMS Microbiology Letters
- volume
- 234
- issue
- 1
- pages
- 155 - 161
- publisher
- Oxford University Press
- external identifiers
-
- pmid:15109734
- wos:000221218300022
- scopus:1942470014
- ISSN
- 1574-6968
- DOI
- 10.1016/j.femsle.2004.03.024
- language
- English
- LU publication?
- yes
- id
- 0aaac118-bdbe-4062-9e6e-4f11cbacc920 (old id 279441)
- date added to LUP
- 2016-04-01 15:25:00
- date last changed
- 2022-01-28 05:16:07
@article{0aaac118-bdbe-4062-9e6e-4f11cbacc920, abstract = {{In the present study, a phage display library covering the genome of Staphylococcus lugdunensis, was affinity-selected against von Willebrand factor (vWf). This led to the identification of a gene, vwbl, encoding a Putative cell surface protein of 2060 amino acids, denoted vWbl. The deduced protein has an overall organisation typical of staphylococcal cell Surface proteins, with an N-terminal signal peptide, and a C-terminal cell wall sorting signal. The vWf-binding part is located in repetitive domains and antibodies against vWbl or vWf can inhibit the binding. Southern blot analysis showed that vwbl was present in the 12 S. lugdunensis strains tested. (C) 2004 Federation of European Microbiological Societies.}}, author = {{Nilsson, M and Bjerketorp, J and Wiebensjo, A and Ljungh, Åsa and Frykberg, L and Guss, B}}, issn = {{1574-6968}}, keywords = {{von Willebrand factor; display; phage; coagulase-negative staphylococci; Staphylococcus lugdunensis; adhesin; LPXTG motif}}, language = {{eng}}, number = {{1}}, pages = {{155--161}}, publisher = {{Oxford University Press}}, series = {{FEMS Microbiology Letters}}, title = {{A von Willebrand factor-binding protein from Staphylococcus lugdunensis}}, url = {{http://dx.doi.org/10.1016/j.femsle.2004.03.024}}, doi = {{10.1016/j.femsle.2004.03.024}}, volume = {{234}}, year = {{2004}}, }