1887

Abstract

A phage display library made from DNA was sorted against a central venous catheter (CVC) that had been removed from a patient 2 days after insertion. After the first panning, approximately 50 % of the clones encoded proteins known to interact with mammalian proteins. After the second and third pannings, fibrinogen-binding and β-glycoprotein I (β-GPI)-binding phage particles were clearly dominating. Proteins adsorbed to different CVCs were investigated using specific antibodies. Among the proteins probed for, fibrinogen was most abundant, but, interestingly, β-GPI was also detected on all tested CVCs.

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2004-10-01
2019-11-22
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References

  1. Barbucci, R. & Magnani, A. ( 1994;). Conformation of human plasma proteins at polymer surfaces: the effectiveness of surface heparinization. Biomaterials 15, 955–962.[CrossRef]
    [Google Scholar]
  2. Bjerketorp, J., Nilsson, M., Ljungh, Å., Flock, J. I., Jacobsson, K. & Frykberg, L. ( 2002;). A novel von Willebrand-binding protein expressed by Staphylococcus aureus. Microbiology 148, 2037–2044.
    [Google Scholar]
  3. Bodén, M. K. & Flock, J. I. ( 1989;). Fibrinogen-binding protein/clumping factor from Staphylococcus aureus. Infect Immun 57, 2358–2363.
    [Google Scholar]
  4. Bodén, M. K. & Flock, J. I. ( 1994;). Cloning and characterization of a gene for a 19 kDa fibrinogen-binding protein from Staphylococcus aureus. Mol Microbiol 4, 599–606.
    [Google Scholar]
  5. Borchman, D., Harris, E. N., Pierangeli, S. S. & Lamba, O. P. ( 1995;). Interactions and molecular structure of cardiolipin and beta 2-glycoprotein 1 (beta 2-GP1). Clin Exp Immunol 102, 373–378.
    [Google Scholar]
  6. Chamley, L. W., Duncalf, A. M., Konarkovska, B., Mitchell, M. D. & Johnson, P. M. ( 1999;). Conformationally altered β2-glycoprotein I is the antigen for anti-cardiolipin autoantibodies. Clin Exp Immunol 155, 571–576.
    [Google Scholar]
  7. Chonn, A., Semple, S. C. & Cullis, P. R. ( 1995;). Beta 2-glycoprotein I is a major protein associated with very rapidly cleared liposomes in vivo, suggesting a significant role in the immune clearance of ‘‘non-self’’ particles. J Biol Chem 270, 25845–25849.[CrossRef]
    [Google Scholar]
  8. Courtney, J. M., Lamba, N. M., Sundaram, S. & Forbes, C. D. ( 1994;). Biomaterials for blood-contacting applications. Biomaterials 15, 737–744.[CrossRef]
    [Google Scholar]
  9. Dickinson, R. B., Nagel, J. A., McDevitt, D., Foster, T. J., Proctor, R. A. & Cooper, S. L. ( 1995;). Quantitative comparison of clumping factor- and coagulase-mediated Staphylococcus aureus adhesion to surface-bound fibrinogen under flow. Infect Immun 63, 3143–3150.
    [Google Scholar]
  10. Fabrizi, F., Sangiorgio, R., Pontoriero, G., Corti, M., Tentori, F., Troina, E. & Locatelli, F. ( 1999;). Antiphospholipid (aPL) antibodies in end-stage renal disease. J Nephrol 12, 89–94.
    [Google Scholar]
  11. Fischer, B. E., Schlokat, U., Reiter, M., Mundt, W. & Dorner, F. ( 1997;). Biochemical and functional characterization of recombinant von Willebrand factor produced on a large scale. Cell Mol Life Sci 53, 943–950.[CrossRef]
    [Google Scholar]
  12. Francois, P., Schrenzel, J., Stoerman-Chopard, C., Favre, H., Herrmann, M., Foster, T. J., Lew, D. P. & Vaudaux, P. ( 2000;). Identification of plasma proteins adsorbed on hemodialysis tubing that promote Staphylococcus aureus adhesion. J Lab Clin Med 135, 32–42.[CrossRef]
    [Google Scholar]
  13. Fuquay, J. I., Loo, D. T. & Barnes, D. W. ( 1986;). Binding of Staphylococcus aureus by human serum spreading factor in an in vitro assay. Infect Immun 52, 714–717.
    [Google Scholar]
  14. Galli, M., Comfurius, P., Maassen, C., Hemker, H. C., de Baets, M. H., van Breda-Vriesman, P. J., Barbui, T., Zwaal, R. F. & Bevers, E. M. ( 1990;). Anticardiolipin antibodies (ACA) directed not to cardiolipin but to a plasma protein cofactor. Lancet 335, 1544–1547.[CrossRef]
    [Google Scholar]
  15. Hartleib, J., Kohler, N., Dickinson, R. B. & 7 other authors ( 2000;). Protein A is the von Willebrand factor binding protein on Staphylococcus aureus. Blood 96, 2149–2156.
    [Google Scholar]
  16. Heilmann, C., Herrmann, M., Kehrel, B. E. & Peters, G. ( 2002;). Platelet-binding domains in 2 fibrinogen-binding proteins of Staphylococcus aureus identified by phage display. J Infect Dis 186, 32–39.[CrossRef]
    [Google Scholar]
  17. Herrmann, M., Vaudaux, P. E., Pittet, D., Auckenthaler, R., Lew, P. D., Schumacher-Perdreau, F., Peters, G. & Waldvogel, F. A. ( 1988;). Fibronectin, fibrinogen, and laminin act as mediators of adherence of clinical staphylococcal isolates to foreign material. J Infect Dis 158, 693–701.[CrossRef]
    [Google Scholar]
  18. Herrmann, M., Suchard, S. J., Boxer, L. A., Waldvogel, F. A. & Lew, P. D. ( 1991;). Thrombospondin binds to Staphylococcus aureus and promotes staphylococcal adherence to surfaces. Infect Immun 59, 279–288.
    [Google Scholar]
  19. Herrmann, M., Hartleib, J., Kehrel, B., Montgomery, R. R., Sixma, J. J. & Peters, G. ( 1997;). Interaction of von Willebrand factor with Staphylococcus aureus. J Infect Dis 176, 984–991.[CrossRef]
    [Google Scholar]
  20. Jacobsson, K. & Frykberg, L. ( 1995;). Cloning of ligand-binding domains of bacterial receptors by phage display. Biotechniques 18, 878–885.
    [Google Scholar]
  21. Jacobsson, K. & Frykberg, L. ( 1996;). Phage display shot-gun cloning of ligand-binding domains of prokaryotic receptors approaches 100 % correct clones. Biotechniques 20, 1070–1081.
    [Google Scholar]
  22. Jacobsson, K. & Frykberg, L. ( 1998;). Gene VIII-based, phage-display vectors for selection against complex mixtures of ligands. Biotechniques 24, 294–301.
    [Google Scholar]
  23. Jacobsson, K. & Frykberg, L. ( 2001;). Shotgun phage display cloning. Comb Chem High Throughput Screen 4, 135–143.
    [Google Scholar]
  24. Jacobsson, K., Rosander, A., Bjerketorp, J. & Frykberg, L. ( 2003;). Shotgun Phage Display – selection for bacterial receptins or other exported proteins. Biol Proced Online 5, 123–135.[CrossRef]
    [Google Scholar]
  25. Jönsson, K., Signäs, C., Müller, H. P. & Lindberg, M. ( 1991;). Two different genes encode fibronectin binding proteins in Staphylococcus aureus.The complete nucleotide sequence and characterization of the second gene. Eur J Biochem 202, 1041–1048.[CrossRef]
    [Google Scholar]
  26. Kaida, S., Miyata, T., Yoshizawa, Y., Kawabata, S., Morita, T., Igarashi, H. & Iwanaga, S. ( 1987;). Nucleotide sequence of the staphylocoagulase gene: its unique COOH-terminal 8 tandem repeats. J Biochem (Tokyo) 102, 1177–1186.
    [Google Scholar]
  27. Kato, H. & Enjyoji, K. ( 1991;). Amino acid sequence and location of the disulfide bonds in bovine beta 2-glycoprotein I: the presence of five Sushi domains. Biochemistry 30, 11687–11694.[CrossRef]
    [Google Scholar]
  28. Kawabata, S., Morita, T., Miyata, T., Iwanaga, S. & Igarashi, H. ( 1986;). Isolation and characterization of staphylocoagulase chymotryptic fragment.Localization of the procoagulant- and prothrombin-binding domain of this protein. J Biol Chem 261, 1427–1433.
    [Google Scholar]
  29. Kronvall, G. & Jönsson, K. ( 1999;). Receptins: a novel term for an expanding spectrum of natural and engineered microbial proteins with binding properties for mammalian proteins. J Mol Recognit 12, 38–44.[CrossRef]
    [Google Scholar]
  30. Kuroda, M., Ohta, T., Uchiyama, I. & 34 other authors ( 2001;). Whole genome sequencing of meticillin-resistant Staphylococcus aureus. Lancet 357, 1225–1240.[CrossRef]
    [Google Scholar]
  31. Li, Z. & Krilis, S. A. ( 2003;). Anti-β2-glycoprotein I antibodies and the antiphospholipid syndrome. Autoimmun Rev 2, 229–234.[CrossRef]
    [Google Scholar]
  32. Malik, P., Terry, T. D., Gowda, L. R., Langara, A., Petukhov, S. A., Symmons, M. F., Welsh, L. C., Marvin, D. A. & Perham, R. N. ( 1996;). Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage. J Mol Biol 260, 9–21.[CrossRef]
    [Google Scholar]
  33. McDevitt, D., Vaudaux, P. & Foster, T. J. ( 1992;). Genetic evidence that bound coagulase of Staphylococcus aureus is not clumping factor. Infect Immun 60, 1514–1523.
    [Google Scholar]
  34. McIntyre, J. A. & Wagenknecht, D. R. ( 2003;). Antiphospholipid antibodies and renal transplantation: a risk assessment. Lupus 12, 555–559.[CrossRef]
    [Google Scholar]
  35. McNeil, H. P., Simpson, R. J., Chesterman, C. N. & Krilis, S. A. ( 1990;). Anti-phospholipid antibodies are directed against a complex antigen that includes a lipid-binding inhibitor of coagulation: beta 2-glycoprotein I (apolipoprotein H). Proc Natl Acad Sci U S A 87, 4120–4124.[CrossRef]
    [Google Scholar]
  36. McNeil, H. P., Chesterman, C. N. & Krilis, S. A. ( 1991;). Immunology and clinical importance of antiphospholipid antibodies. Adv Immunol 49, 193–280.
    [Google Scholar]
  37. Nimpf, J., Bevers, E. M., Bomans, P. H., Till, U., Wurm, H., Kostner, G. M. & Zwaal, R. F. ( 1986;). Prothrombinase activity of human platelets is inhibited by beta 2-glycoprotein I. Biochim Biophys Acta 884, 142–149.[CrossRef]
    [Google Scholar]
  38. Shi, T., Iverson, G. M., Qi, J. C., Cockerill, K. A., Linnik, M. D., Konecny, P. & Krilis, S. A. ( 2004;). β2-Glycoprotein I binds factor XI and inhibits its activation by thrombin and factor XIIa: loss of inhibition by clipped beta 2-glycoprotein I. Proc Natl Acad Sci U S A 101, 3939–3944.[CrossRef]
    [Google Scholar]
  39. Signäs, C., Raucci, G., Jönsson, K., Lindgren, P. E., Anantharamaiah, G. M., Höök, M. & Lindberg, M. ( 1989;). Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides. Proc Natl Acad Sci U S A 86, 699–703.[CrossRef]
    [Google Scholar]
  40. Smith, G. P. ( 1985;). Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228, 1315–1317.[CrossRef]
    [Google Scholar]
  41. Steinkasserer, A., Estaller, C., Weiss, E. H., Sim, R. B. & Day, A. J. ( 1991;). Complete nucleotide and deduced amino acid sequence of human beta 2-glycoprotein I. Biochem J 277, 387–391.
    [Google Scholar]
  42. Uhlen, M., Guss, B., Nilsson, B., Gatenbeck, S., Philipson, L. & Lindberg, M. ( 1984;). Complete sequence of the staphylococcal gene encoding protein A.A gene evolved through multiple duplications. J Biol Chem 259, 1695–1702.
    [Google Scholar]
  43. Vaudaux, P., Suzuki, R., Waldvogel, F. A., Morgenthaler, J. J. & Nydegger, U. E. ( 1984;). Foreign body infection: role of fibronectin as a ligand for the adherence of Staphylococcus aureus. J Infect Dis 150, 546–553.[CrossRef]
    [Google Scholar]
  44. von Eiff, C., Peters, G. & Heilmann, C. ( 2002;). Pathogenesis of infections due to coagulase-negative staphylococci. Lancet Infect Dis 2, 677–685.[CrossRef]
    [Google Scholar]
  45. Vroman, L., Adams, A. L., Fischer, G. C. & Munoz, P. C. ( 1980;). Interaction of high molecular weight kininogen, factor XII, and fibrinogen in plasma at interfaces. Blood 55, 156–159.
    [Google Scholar]
  46. Wang, S. X., Sun, Y. T. & Sui, S. F. ( 2000;). Membrane-induced conformational change in human apolipoprotein H. Biochem J 348, 103–106.[CrossRef]
    [Google Scholar]
  47. Wann, E. R., Gurusiddappa, S. & Höök, M. ( 2000;). The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen. J Biol Chem 275, 13863–13871.[CrossRef]
    [Google Scholar]
  48. Zhang, L., Jacobsson, K., Vasi, J., Lindberg, M. & Frykberg, L. ( 1998;). A second IgG-binding protein in Staphylococcus aureus strain 8325-4. Microbiology 144, 985–991.[CrossRef]
    [Google Scholar]
  49. Zhang, L., Jacobsson, K., Ström, K., Lindberg, M. & Frykberg, L. ( 1999;). Staphylococcus aureus expresses a cell surface protein that binds both IgG and β2-glycoprotein I. Microbiology 145, 177–183.[CrossRef]
    [Google Scholar]
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