Home About Browse Search
Svenska


Novel adhesive proteins of pathogenic Staphylococci and their interaction with host proteins

Bjerketorp, Joakim (2004). Novel adhesive proteins of pathogenic Staphylococci and their interaction with host proteins. Diss. (sammanfattning/summary) Uppsala : Sveriges lantbruksuniv., Acta Universitatis agriculturae Sueciae. Agraria, 1401-6249 ; 451
ISBN 91-576-6463-3
[Doctoral thesis]

[img]
Preview
PDF
3MB

Abstract

In this thesis, interactions between bacterial and host proteins have been studied by a phage display approach. Affinity selection of a Staphylococcus aureus shotgun phage display library against human von Willebrand factor (vWf), led to the identification of a novel secreted vWf-binding protein (vWbp). Mature vWbp, which consists of 482 amino acids, could be recovered from an S. aureus culture supernatant. The specific interaction between vWbp and vWf is mediated by a region of 26 amino acids located in the C-terminal part of vWbp. Further characterisation revealed vWbp to be a bifunctional protein capable of inducing coagulation of plasma from several species, but with preference for human and porcine plasma. The coagulating activity was found to reside in the N-terminal part of vWbp, and to be depended on the interaction with prothrombin. Similarly, panning a Staphylococcus lugdunensis phage display library against human vWf resulted in the recognition of a novel vWf-binding protein (vWbl). This protein comprises 2060 amino acids, including a cell wall sorting signal with a surface-anchoring LPXTG-motif. The vWf-binding part of vWbl is located in repetitive domains. The incidence of the genes encoding vWbp and vWbl is very high in clinical isolates of the respective staphylococcal species. In addition, the S. aureus library was sorted against ex vivo biomaterial, and six different staphylococcal protein were identified: coagulase, Efb, protein A, FnbpA, FnbpB, and Sbi. Fibrinogen-binding and β2-glycoprotein I (β2-GPI)-binding phagemid particles were dominating. Proteins adsorbed to different ex vivo central venous catheters were investigated using specific antibodies. Fibrinogen was found to be most abundant, but β2-GPI was also detected on the investigated biomaterials. This is noteworthy in view of S. aureus adherence to biomaterials, but might also implicate a source for induction of disease-causing β2-GPI-autoantibodies. vWf is an essential molecule for platelet adherence and aggregation, especially during rapid blood flow. Thus, it is intriguing that two virulent staphylococcal species, both capable of causing life threatening endocarditis, have evolved proteins with affinity for vWf. Perhaps even more intriguing, both vWbp and vWbl presumably bind the same site in vWf, as indicated by cross-inhibition studies. However, the exact role for these staphylococcal proteins concerning staphylococcal pathogenesis remains to be elucidated.

Authors/Creators:Bjerketorp, Joakim
Title:Novel adhesive proteins of pathogenic Staphylococci and their interaction with host proteins
Year of publishing :May 2004
Volume:451
Number of Pages:56
Papers/manuscripts:
NumberReferences
ALLI. Bjerketorp, J., Nilsson, M., Ljungh, Å., Flock, J.-I., Jacobsson, K. & Frykberg, L. 2002. A novel von Willebrand factor-binding protein expressed by Staphylococcus aureus. Microbiology 148, 2037-2044. II. Bjerketorp, J., Jacobsson, K. & Frykberg, L. 2004. The von Willebrand factor-binding protein (vWbp) of Staphylococcus aureus is a coagulase. FEMS Microbiol. Lett. (In press). III. Nilsson, M., Bjerketorp, J., Wiebensjö, Å., Ljungh, Å., Frykberg, L. & Guss, B. 2004. A von Willebrand factor-binding protein from Staphylococcus lugdunensis. FEMS Microbiol. Lett. (In press). IV. Bjerketorp, J., Rosander, A., Nilsson, M., Jacobsson, K. & Frykberg, L. Sorting a Staphylococcus aureus phage display library against ex vivo biomaterial. (Submitted).
Place of Publication:Uppsala
ISBN for printed version:91-576-6463-3
ISSN:1401-6249
Language:English
Publication Type:Doctoral thesis
Full Text Status:Public
Agris subject categories.:X Agricola extesions > X30 Life sciences
Subjects:Not in use, please see Agris categories
Agrovoc terms:staphylococcus, proteins, microbiological analysis
Keywords:Staphylococcus aureus, Staphylococcus lugdunensis, coagulase-negative staphylococci, phage display, vWf, von Willebrand factor-binding protein, vWbp, receptin, prothrombin activation, coagulase, vWbl, adhesin, LPXTG-motif, bacterial adhesion, intravascular device, biomaterial, beta2-glycoprotein I
URN:NBN:urn:nbn:se:slu:epsilon-268
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-268
ID Code:547
Department:(NL, NJ) > Dept. of Microbiology (until 161231)
Deposited By: Joakim Bjerketorp
Deposited On:03 May 2004 00:00
Metadata Last Modified:02 Dec 2014 10:05

Repository Staff Only: item control page

Downloads

Downloads per year (since September 2012)

View more statistics

Downloads
Hits