title: Two different genes coding for fibronectin-binding proteins from Streptococcus dysgalactiae. The complete nucleotide sequences and characterization of the binding domains.
abstract: The binding of Streptococcus dysgalactiae to fibronectin involves fibronectin-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, P., McGavin, M. J., Monstein, H.-J., Höök, 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.
authors.affiliation: Department of Microbiology, Swedish University of Agricultural Sciences, Uppsala.
authors.forename: P E
authors.initials: PE
authors.lastname: Lindgren
authors.forename: M J
authors.initials: MJ
authors.lastname: McGavin
authors.forename: C
authors.initials: C
authors.lastname: Signäs
authors.forename: B
authors.initials: B
authors.lastname: Guss
authors.forename: S
authors.initials: S
authors.lastname: Gurusiddappa
authors.forename: M
authors.initials: M
authors.lastname: Höök
authors.forename: M
authors.initials: M
authors.lastname: Lindberg
mesh_terms: D018829:Adhesins, Bacterial; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics*; D001426:Bacterial Proteins; D001483:Base Sequence; D002352:Carrier Proteins; D002473:Cell Wall / Q000737:chemistry; D003001:Cloning, Molecular; D005353:Fibronectins / Q000378:metabolism*; D005798:Genes, Bacterial / Q000235:genetics*; D008969:Molecular Sequence Data; D012091:Repetitive Sequences, Nucleic Acid; D015183:Restriction Mapping; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013291:Streptococcus / Q000235:genetics*; D013329:Structure-Activity Relationship
chemical_list: D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D005353:Fibronectins; C078635:fibronectin-binding proteins, bacterial