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Abstract

  1. Top of page
  2. Abstract
  3. REFERENCES

A gene encoding a fibronectin binding protein (FnBP) has recently been isolated and sequenced from Staphylococcus aureus strain 8325–4. In the same bacterial strain, 682 bp downstream to the stop codon of this gene (fnbA), a second gene termed fnbB has now been discovered, encoding another FnBP (FnBPB). The two genes show in large parts striking sequence homologies. The complete amino acid sequence encoded by fnbB has been deduced and compared to that deduced from fnbA. In FnBPB a stretch of 66 amino acids downstream to the signal peptide has 75% identity with the corresponding region in FnBPA. At the C-terminal site another 394 amino acid stretch is almost identical in both gene products. This stretch contains the 38 amino acid long D repeats, the wall spanning Wr repeats and the hydrophobic membrane spanning domain. In FnBPA each of the three D repeats has been identified as a fibronectin binding structure. These structures are highly conserved in FnBPB and most likely represent the major Fn-binding domain of this protein. However, a subclone of gene fnbB lacking the coding region for the D repeats also clearly expresses fibronectin binding activity. This additional binding site is so far unique for FnBPB and interacts like the D domains with the N-terminal 24–31-kDa fragment of fibronectin. The purified recombinant FnBP fragment (not containing the D repeats) completely inhibits the binding of fibronectin to whole cells of S. aureus.

Abbreviations
Fn

fibronectin

FnBP

Fn binding protein

FnBPA

FnBP encoded by fnbA

FnBPB

FnBP encoded by fnbB

Enzymes
 

Thermolysin (EC 3.4.24.4)

 

lysozyme (EC 3.2.1.17)

REFERENCES

  1. Top of page
  2. Abstract
  3. REFERENCES
  • 1
    Hynes, R. O. (1985) Annu. Rev. Cell Biol. 1, 6790.
  • 2
    Yamada, K. M. (1983) Annu. Rev. Biochem. 52, 761799.
  • 3
    Hynes, R. O. (1986) Sci. Am. 254, 4251.
  • 4
    Ruoslahti, E. & Pierschbacher, M. D. (1986) Cell 44, 517518.
  • 5
    Woods, A., Couchman, J. R., Johansson, S. & Höök, M. (1986) EMBO J. 5, 665670.
  • 6
    Kuusela, P. (1978) Nature 276, 718720.
  • 7
    Höök, M., Switalski, L. M., Wadström, T. & Lindberg, M. (1989) in Fibronectin (Mosher, D. F., ed.) pp. 295308, Academic Press, Inc., San Diego , CA .
  • 8
    Pierschbacher, M. D., Hayman, E. G. & Ruoslahti, E. (1981) Cell 26, 259267.
  • 9
    Fröman, G., Switalski, L. M., Faris, A., Wadström, T. & Höök, M. (1984) J. Biol. Chem. 259, 1489914905.
  • 10
    Mosher, D. F. & Proctor, R. A. (1980) Science 209, 927929.
  • 11
    Kuusela, P., Vartio, T., Vuento, M. & Myhre, E. B. (1985) Infect. Immun. 48, 318323.
  • 12
    Speziale, P., Höök, M., Switalski, L. M. & Wadström, T. (1984) J. Bacteriol. 157, 420436.
  • 13
    Espersen, F. & Clemmensen, I. (1982) Infect. Immun. 37, 526531.
  • 14
    Fröman, G., Switalski, L. M., Speizale, P. & Höök, M. (1987) J. Biol. Chem. 262, 65646571.
  • 15
    Flock, J.-I., Fröman, G., Jönsson, K., Guss, B., Signäs, C., Nilsson, B., Raucci, G., Höök, M., Wadström, T. & Lindberg, M. (1987) EMBO J. 6, 23512357.
  • 16
    Signäs, C., Raucci, G., Jönsson, K., Lindgren, P.-E., Anantharamaiah, G. M., Höök, M. & Lindberg, M. (1989) Proc. Natl Acad. Sci. USA 86, 699703.
  • 17
    Carter, P., Bedouelle, H. & Winter, G. (1985) Nucleic Acids Res. 12, 44314443.
  • 18
    Hanahan, D. (1983) J. Mol. Biol. 166, 557580.
  • 19
    Bolivar, F., Rodriques, R. L., Green, P. J., Betlach, M. C., Heynecker, H. L., Boyer, H. W., Crosa, J. H. & Falkow, S. (1977) Gene 2, 95113.
  • 20
    Norrander, J., Kempe, T. & Messing, J. (1983) Gene 26, 101106.
  • 21
    Löfdahl, S., Guss, B., Uhlén, M., Philipson, L. & Lindberg, M. (1983) Proc. Natl Acad. Sci. USA 80, 697701.
  • 22
    Wikner, N. E. & Clark, R. A. F. (1988) Methods Enzymol. 162, 214222.
  • 23
    Hunter, W. M. & In Wier, K. M. (1978) Handbook of experimental immunology, pp. 14.114.40, Blackwell, London .
  • 24
    Monstein, H.-J. & Geijer, T. (1986) Biochem. Int. 12, 889896.
  • 25
    Sambrook, J., Fritch, E. F. & Maniatis, T. (1989) Molecular cloning: a laboratory manual, 2nd end, Cold Spring Harbor Lab Press, Cold Spring Harbor , New York .
  • 26
    Sanger, F., Nicklen, S. & Coulson, A. R. (1977) Proc. Natl Acad. Sci. USA 74, 54635467.
  • 27
    Devereux, J., Haeberli, P. & Smithies, O. (1984) Nucleic Acids Res. 12, 387395.
  • 28
    Towbin, H., Staehelin, T. & Gordon, J. (1979) Proc. Natl Acad. Sci. USA 76, 43504354.
  • 29
    Nilsson, B., Moks, T., Jansson, B., Abramsén, L., Elmblad, A., Holmgren, E., Henrichson, C., Jones, T. A. & Uhlén, M. (1987) Prot. Eng. 1, 107113.
  • 30
    McGavin, M. J., Raucci, G., Gurusiddappa, S. & Höök, M. (1991) J. Biol. Chem. 266, 83438347.
  • 31
    Lindgren, P.-E., Speziale, P., McGavin, M., Mostein, H. J., Höök, M., Visai, L., Kostiainen, T., Bozzini, S. & Lindberg, M. (1992) J. Biol. Chem., in the press.
  • 32
    Kuypers, J. M. & Proctor, R. A. (1989) Infect. Immun. 57, 23062312.