A von Willebrand factor-binding protein from Staphylococcus lugdunensis

被引：45

作者：

Nilsson, M

Bjerketorp, J

Wiebensjö, Å

Ljungh, Å

Frykberg, L

Guss, B ^{[1
]}

机构：

[1] Swedish Univ Agr Sci, Dept Microbiol, SE-75007 Uppsala, Sweden

[2] Lund Univ, Dept Med Microbiol Dermatol & Infect, SE-22362 Lund, Sweden

来源：

FEMS MICROBIOLOGY LETTERS | 2004年 / 234卷 / 01期

关键词：

coagulase-negative staphylococci; Staphylococcus lugdunensis; phage display; von Willebrand factor; adhesin; LPXTG motif;

D O I：

10.1016/j.femsle.2004.03.024

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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. Published by Elsevier B.V. All rights reserved.

引用

页码：155 / 161

页数：7

共 28 条

[1] The YSIRK-G/S motif of staphylococcal protein A and its role in efficiency of signal peptide processing [J].