Chemistry: molecular biology and microbiology – Vector – per se
Reexamination Certificate
1999-06-08
2002-03-12
Navarro, Mark (Department: 1645)
Chemistry: molecular biology and microbiology
Vector, per se
C536S023700
Reexamination Certificate
active
06355477
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
This invention relates to a novel fibrinogen and fibronectin binding protein from group A streptococci, and the DNA encoding the protein. The protein and its DNA are useful in the preparation of compositions for the diagnosis, treatment, and prevention of streptococcal infection.
2. Description of the Related Art
Among surface proteins of gram-positive bacteria, the fibronectin-binding (Fn-binding) proteins are responsible for adhesion to host epithelial cells (11, 12). Accordingly, Fn-binding proteins may provide the bacterial cell with the means to initiate the infection process (11, 12, 13, 14). Fn-binding proteins have been identified in
Staphylococcus aureus
(3, 11, 16), class I (SOF
−
)
S. pyogenes
(10, 12, 15) and
Streptococcus dysgalactiae
(6,14). Sequence analysis of these proteins revealed that they are large cell surface proteins, with a predicted size range of 73-122 kDa. The domain architecture of these molecules is similar: a divergent N-terminal portion which constitutes up to 80% of their sequence, followed by three to five homologous tandem Fn-binding repeats of from 32 to 43 residues each (3, 6, 12, 15, 16). In at least two cases, protein F from
S. pyogenes
class I and FnBPB from
S. aureus
, a region of approximately 50 residues N terminal to the tandem repeats has also been implicated as essential for maximal Fn-binding activity (3, 15). A putative cell wall-spanning segment is located C terminally to the repeats, followed by a typical gram-positive cell attachment motif.
Group A Streptococci (
Streptococcus pyogenes
) is the etiologic agent for different suppurative infections (e.g., pharyngitis, impetigo, and necrotizing fasciitis) as well as systemic diseases (e.g., scarlet fever, toxic shock-like syndrome), some of which may lead to serious sequelae, such as rheumatic fever and glomerulonephritis. The ability to bind fibronectin has proven to be one of the mechanisms
Streptococcus pyogenes
use for attachment to host cells (5, 8, 10). Since this glycoprotein is present in body fluids, extracellular matrices, and on the surface of mammalian cells, the identification and characterization of new fibronectin-binding proteins is likely to have pathogenic significance.
SUMMARY OF THE INVENTION
Accordingly, a major object of the present invention is to provide a new streptococcal fibronectin and fibrinogen binding protein. The present invention also provides compositions of matter, including pharmaceutical compositions, comprising the fibronectin and fibrinogen binding protein of the present invention. The present invention further provides antibodies to the fibronectin and fibrinogen binding protein of the present invention and methods for assaying the proteins of the present invention in biological samples using those antibodies.
A further object of the present invention is to provide the DNA encoding the fibronectin and fibrinogen binding protein of the present invention. The present invention also provides vectors, including plasmids and viral vectors comprising the DNA of the present invention, methods of transforming cells with the vectors of the present invention, and transformed cells.
With the foregoing and other objects, advantages and features of the invention that will become hereinafter apparent, the nature of the invention may be more clearly understood by reference to the following detailed description of the preferred embodiments of the invention and to the appended claims.
REFERENCES:
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patent: 5416021 (1995-05-01), Hook et al.
patent: 5910441 (1999-06-01), Rocha et al.
Hoeoek, M., et al. “Fibronectin Binding Protein” Accession No. A12915 (1994) Abstract.
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Jonsson, K. et al., “Two Different Genes Encode Fibronectin Binding Proteins inStaphylococcus aureus”,Eur. J. Biochem. (1991) 202:1041-1048.
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Flock, J-I et al. “Cloning and Expression of the Gene for a Fibronectin-Binding Protein fromStaphylococcus aureus”, EMBO J. (1987) 6:2351-2357.
Hanski, E. et al. “Protein F, a Fibronectin-binding Protein, is an Adhesin of the group A StreptococcusStreptococcus pyogenes”, Proc. Natl. Acad. Sci. USA(1992) 89:6172-6176.
Hanski, E. et al., “Expression of Protein F, the Fibronectin-Binding Protein ofStreptococcus pyogenesJRS4, in Heterologous Streptococcal and Enterococcal Strains Promotes Their Adherence to Respiratory Epithelial Cells”,Infect. Immun. (1992) 60:5119-5125.
Lindgren, P. et al., “Cloning and Expression of Two Different Genes fromStreptococcus dysgalactiaeEncoding Fibronectin Receptors”,J. Biol. Chem. (1992) 267:1924-1931.
Sela, S. et al. “Protein F: an adhesin ofStreptococcus pyogenesBinds Fibronectin via Two Distinct Domains”,Mol. Microbiol. (1993) 10:1049-1055.
Signas, C., et al. “Nucleotide Sequence of the Gene for a Fibronectin-binding Protein fromStaphylococcus aureus: Use of this Peptide Sequence in the Synthesis of Biologically Active Peptides”,Proc. Natl. Acad. Sci. USA(1989) 86:699-703.
Jaffe et al. “Protein F2, a Novel Fibronectin-Binding Protein FromStreptococcus Pyogenus, Possesses Two Binding Domains”Molecular Biologyvol. 21, No. 2, pp. 373-384 (Jul. 1996).
Courtney et al “DNA Sequence of the Serum Opacity Factor of Group A Streptococci: Identification of a Fibronectin-Binding Repeat Domain”Infection and Immunityvol. 62, No. 9, pp. 3937-3946 (Sep. 1994).
Fischetti Vincent A.
Rocha Claudia
Burns Doane Swecker & Mathis L.L.P.
Navarro Mark
The Rockefeller University
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