Abstract

The binding of Streptococcus dysgalactiae to fibronectin involves fibronetcin-binding protein(s) present on the bacterial surface. Previously, we reported the cloning of two different genes coding for cell-wall-associated fibronectin-binding proteins from S. dysgalactiae strain S2 [Lindgren, P.-E., Speziale, R, McGavin, M. J., Monstein, H.-J., Hook, M., Visai, L., Kostiainen, T., Bozzini, S. & Lindberg, M. (1992) J. Biol. Chem. 267, 1924-1931]. The two genes, fnbA and fnbB, have now been sequenced and the primary amino acid sequences of the two fibronectin-binding proteins, FnBA and FnBB, have been deduced. The two proteins have predicted molecular masses of 117 kDa and 122 kDa, respectively, and are organized in a similar way. The fibronectin-binding activities are localized in repeated motifs, 32-37 amino acids long, in the COOH-terminal regions of the proteins. The two fibronectin-binding proteins have heterologous amino acid sequences, except for the COOH-terminal ends which include the fibronectin-binding repeats. The fibronectin-binding regions of the genes have been fused to IgG-binding domains of protein A, utilizing the IgG-binding capacity of the resulting fusion proteins, to facilitate isolation of the fibronectin-binding domains.

Published in

European Journal of Biochemistry
1993, Volume: 214, number: 3, pages: 819-827
Publisher: SPRINGER VERLAG

SLU Authors

• Guss, Bengt

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Immunology
Microbiology
Biochemistry and Molecular Biology


Publication identifier

DOI: https://doi.org/10.1111/j.1432-1033.1993.tb17985.x

Permanent link to this page (URI)

https://res.slu.se/id/publ/79294