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. 1985 Oct;50(1):77–81. doi: 10.1128/iai.50.1.77-81.1985

Attachment of staphylococci and streptococci on fibronectin, fibronectin fragments, and fibrinogen bound to a solid phase.

P Kuusela, T Vartio, M Vuento, E B Myhre
PMCID: PMC262138  PMID: 3899940

Abstract

The attachment of Staphylococcus aureus (Cowan I) and two strains of group A and G streptococci on glass cover slips coated with fibronectin, fibronectin fragments, or fibrinogen was studied. The attachment was quantitated by counting the attached bacteria on glass surfaces coated with a similar molarity of the proteins. Fibronectin was a more effective attachment factor than fibrinogen for staphylococci, while group G streptococci attached better on fibrinogen- than on fibronectin-coated cover slips. In this system, group A streptococci bound almost exclusively to substrate-bound fibrinogen. Attachment experiments involving the use of staphylococci pretreated with soluble fibronectin or fibrinogen revealed that bacterium-bound fibronectin and fibrinogen were able to enhance the adherence on cover slips coated with fibronectin. The 30-kilodalton NH2-terminal and the 120- to 140-kilodalton COOH-terminal fragments of fibronectin, both of which contain bacterial binding sites, mediated the staphylococcal attachment, suggesting that both parts of the molecule are involved in the attachment mediated by fibronectin.

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Selected References

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  1. Abraham S. N., Beachey E. H., Simpson W. A. Adherence of streptococcus pyogenes, Escherichia coli, and Pseudomonas aeruginosa to fibronectin-coated and uncoated epithelial cells. Infect Immun. 1983 Sep;41(3):1261–1268. doi: 10.1128/iai.41.3.1261-1268.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chen A. B., Mosesson M. W., Solish G. I. Identification of the cold-insoluble globulin of plasma in amniotic fluid. Am J Obstet Gynecol. 1976 Aug 1;125(7):958–961. doi: 10.1016/0002-9378(76)90495-6. [DOI] [PubMed] [Google Scholar]
  3. Engvall E., Ruoslahti E. Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int J Cancer. 1977 Jul 15;20(1):1–5. doi: 10.1002/ijc.2910200102. [DOI] [PubMed] [Google Scholar]
  4. Forsgren A., Sjöquist J. "Protein A" from S. aureus. I. Pseudo-immune reaction with human gamma-globulin. J Immunol. 1966 Dec;97(6):822–827. [PubMed] [Google Scholar]
  5. GREENWOOD F. C., HUNTER W. M., GLOVER J. S. THE PREPARATION OF I-131-LABELLED HUMAN GROWTH HORMONE OF HIGH SPECIFIC RADIOACTIVITY. Biochem J. 1963 Oct;89:114–123. doi: 10.1042/bj0890114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Grinnell F., Feld M. K. Fibronectin adsorption on hydrophilic and hydrophobic surfaces detected by antibody binding and analyzed during cell adhesion in serum-containing medium. J Biol Chem. 1982 May 10;257(9):4888–4893. [PubMed] [Google Scholar]
  7. Kronvall G. A surface component in group A, C, and G streptococci with non-immune reactivity for immunoglobulin G. J Immunol. 1973 Nov;111(5):1401–1406. [PubMed] [Google Scholar]
  8. Kronvall G., Myhre E. B., Björck L., Berggård I. Binding of aggregated human beta2-microglobulin to surface protein structure in group A, C, and G streptococci. Infect Immun. 1978 Oct;22(1):136–142. doi: 10.1128/iai.22.1.136-142.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kronvall G., Schönbeck C., Myhre E. Fibrinogen binding structures in beta-hemolytic streptococci group A, C, and G. Comparisons with receptors for IgG and aggregated beta 2-microglobulin. Acta Pathol Microbiol Scand B. 1979 Oct;87(5):303–310. [PubMed] [Google Scholar]
  10. Kronvall G., Simmons A., Myhre E. B., Jonsson S. Specific absorption of human serum albumin, immunoglobulin A, and immunoglobulin G with selected strains of group A and G streptococci. Infect Immun. 1979 Jul;25(1):1–10. doi: 10.1128/iai.25.1.1-10.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kurkinen M., Vartio T., Vaheri A. Polypeptides of human plasma fibronectin are similar but not identical. Biochim Biophys Acta. 1980 Aug 21;624(2):490–498. doi: 10.1016/0005-2795(80)90090-2. [DOI] [PubMed] [Google Scholar]
  12. Kuusela P. Fibronectin binds to Staphylococcus aureus. Nature. 1978 Dec 14;276(5689):718–720. doi: 10.1038/276718a0. [DOI] [PubMed] [Google Scholar]
  13. Kuusela P., Vaheri A., Palo J., Ruoslahti E. Demonstration of fibronectin in human cerebrospinal fluid. J Lab Clin Med. 1978 Oct;92(4):595–601. [PubMed] [Google Scholar]
  14. Kuusela P., Vartio T., Vuento M., Myhre E. B. Binding sites for streptococci and staphylococci in fibronectin. Infect Immun. 1984 Aug;45(2):433–436. doi: 10.1128/iai.45.2.433-436.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Mosesson M. W., Chen A. B., Huseby R. M. The cold-insoluble globulin of human plasma: studies of its essential structural features. Biochim Biophys Acta. 1975 Apr 29;386(2):509–524. doi: 10.1016/0005-2795(75)90294-9. [DOI] [PubMed] [Google Scholar]
  16. Mosesson M. W., Umfleet R. A. The cold-insoluble globulin of human plasma. I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components. J Biol Chem. 1970 Nov 10;245(21):5728–5736. [PubMed] [Google Scholar]
  17. Mosher D. F., Furcht L. T. Fibronectin: review of its structure and possible functions. J Invest Dermatol. 1981 Aug;77(2):175–180. doi: 10.1111/1523-1747.ep12479791. [DOI] [PubMed] [Google Scholar]
  18. Mosher D. F., Proctor R. A. Binding and factor XIIIa-mediated cross-linking of a 27-kilodalton fragment of fibronectin to Staphylococcus aureus. Science. 1980 Aug 22;209(4459):927–929. doi: 10.1126/science.7403857. [DOI] [PubMed] [Google Scholar]
  19. Myhre E. B., Kronvall G. Demonstration of specific binding sites for human serum albumin in group C and G streptococci. Infect Immun. 1980 Jan;27(1):6–14. doi: 10.1128/iai.27.1.6-14.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Myhre E. B., Kuusela P. Binding of human fibronectin to group A, C, and G streptococci. Infect Immun. 1983 Apr;40(1):29–34. doi: 10.1128/iai.40.1.29-34.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Runehagen A., Schönbeck C., Hedner U., Hessel B., Kronvall G. Binding of fibrinogen degradation products to S. aureus and to beta-hemolytic streptococci group A, C and G. Acta Pathol Microbiol Scand B. 1981 Apr;89(2):49–55. doi: 10.1111/j.1699-0463.1981.tb00151_89b.x. [DOI] [PubMed] [Google Scholar]
  22. Ruoslahti E., Engvall E., Hayman E. G. Fibronectin: current concepts of its structure and functions. Coll Relat Res. 1981;1(1):95–128. doi: 10.1016/s0174-173x(80)80011-2. [DOI] [PubMed] [Google Scholar]
  23. Ruoslahti E., Vaheri A. Interaction of soluble fibroblast surface antigen with fribrinogen and fibrin. J Exp Med. 1975 Feb 1;141(2):497–501. doi: 10.1084/jem.141.2.497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Simpson W. A., Beachey E. H. Adherence of group A streptococci to fibronectin on oral epithelial cells. Infect Immun. 1983 Jan;39(1):275–279. doi: 10.1128/iai.39.1.275-279.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Stanislawski L., Simpson W. A., Hasty D., Sharon N., Beachey E. H., Ofek I. Role of fibronectin in attachment of Streptococcus pyogenes and Escherichia coli to human cell lines and isolated oral epithelial cells. Infect Immun. 1985 Apr;48(1):257–259. doi: 10.1128/iai.48.1.257-259.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Switalski L. M., Ljungh A., Rydén C., Rubin K., Hök M., Wadström T. Binding of fibronectin to the surface of group A, C, and G streptococci isolated from human infections. Eur J Clin Microbiol. 1982 Dec;1(6):381–387. doi: 10.1007/BF02019939. [DOI] [PubMed] [Google Scholar]
  27. Toy P. T., Lai L. W., Drake T. A., Sande M. A. Effect of fibronectin on adherence of Staphylococcus aureus to fibrin thrombi in vitro. Infect Immun. 1985 Apr;48(1):83–86. doi: 10.1128/iai.48.1.83-86.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Vartio T. Characterization of the binding domains in the fragments cleaved by cathepsin G from human plasma fibronectin. Eur J Biochem. 1982 Apr 1;123(2):223–233. doi: 10.1111/j.1432-1033.1982.tb19757.x. [DOI] [PubMed] [Google Scholar]
  29. Vartio T., Salonen E. M., De Petro G., Barlati S., Miggiano V., Stähli C., Virgallita G., Takács B., Vaheri A. Monoclonal antibody against the N-terminal end of human plasma fibronectin. Biochem J. 1983 Oct 1;215(1):147–151. doi: 10.1042/bj2150147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Vartio T., Vaheri A., Von Essen R., Isomäki H., Stenman S. Fibronectin in synovial fluid and tissue in rheumatoid arthritis. Eur J Clin Invest. 1981 Jun;11(3):207–212. doi: 10.1111/j.1365-2362.1981.tb01842.x. [DOI] [PubMed] [Google Scholar]
  31. Vaudaux P. E., Waldvogel F. A., Morgenthaler J. J., Nydegger U. E. Adsorption of fibronectin onto polymethylmethacrylate and promotion of Staphylococcus aureus adherence. Infect Immun. 1984 Sep;45(3):768–774. doi: 10.1128/iai.45.3.768-774.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Vaudaux P., Suzuki R., Waldvogel F. A., Morgenthaler J. J., Nydegger U. E. Foreign body infection: role of fibronectin as a ligand for the adherence of Staphylococcus aureus. J Infect Dis. 1984 Oct;150(4):546–553. doi: 10.1093/infdis/150.4.546. [DOI] [PubMed] [Google Scholar]
  33. Vuento M., Salonen E., Koskimies A., Stenman U. H. High concentrations of fibronectin-like antigens in human seminal plasma. Hoppe Seylers Z Physiol Chem. 1980 Sep;361(9):1453–1456. [PubMed] [Google Scholar]
  34. Vuento M., Vaheri A. Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions. Biochem J. 1979 Nov 1;183(2):331–337. doi: 10.1042/bj1830331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Vuento M., Vartio T., Saraste M., von Bonsdorff C. H., Vaheri A. Spontaneous and polyamine-induced formation of filamentous polymers from soluble fibronectin. Eur J Biochem. 1980 Mar;105(1):33–42. doi: 10.1111/j.1432-1033.1980.tb04471.x. [DOI] [PubMed] [Google Scholar]
  36. Wagner D. D., Hynes R. O. Domain structure of fibronectin and its relation to function. Disulfides and sulfhydryl groups. J Biol Chem. 1979 Jul 25;254(14):6746–6754. [PubMed] [Google Scholar]
  37. Woods D. E., Straus D. C., Johanson W. G., Jr, Bass J. A. Role of fibronectin in the prevention of adherence of Pseudomonas aeruginosa to buccal cells. J Infect Dis. 1981 Jun;143(6):784–790. doi: 10.1093/infdis/143.6.784. [DOI] [PubMed] [Google Scholar]

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