Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Bacterium or component thereof or substance produced by said...
Reexamination Certificate
2008-09-30
2010-11-02
Mondesi, Robert B (Department: 1645)
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Bacterium or component thereof or substance produced by said...
C424S184100, C530S350000, C536S023100, C536S023700, C435S069100, C435S069300, C435S069700
Reexamination Certificate
active
07824692
ABSTRACT:
Novel genes encoding homologous immunoreactive thio-disulfide oxidoreductases, or disulfide bond formation (Dsb) proteins fromEhrlichia chaffeensisandEhrlichia canisare disclosed. While theE. chaffeensisandE. canisDsb proteins are at most only 31% or less homologous to other known Dsb proteins, theEhrlichiaDsbs contain a cysteine active site, Cys-Gly-Tyr-Cys, similar to those in known Dsb proteins. As predicted by 15-amino acid identical N-terminal signal peptides, the proteins are primarily localized in the periplasm ofE. chaffeensisandE. canis, possibly playing a role in antigenicity and pathogenesis. The present invention provides the nucleotide and amino acid sequences and expression vectors for theE. chaffeensisandE. canisdsb genes, antisera directed against the proteins, and kits to determine whether an individual or animal is infected with a given species ofEhrlichia.
REFERENCES:
patent: WO-98/16554 (1998-04-01), None
patent: WO-99/13720 (1999-03-01), None
patent: 00/65063 (2000-11-01), None
patent: WO-00/65063 (2000-11-01), None
patent: WO-02/066652 (2002-08-01), None
Doyle et al ; Journal of Molecular Diagnostics, vol. 7, No. 4, Oct. 2005.
Breitschwerdt et al 1998 (J. Clin. Microbiol1998 36: 2645-2651).
Petrovec et al 1997, J. Clin. Microbiol 35: 1556-1559.
Allsopp et al Journal of Clinical Microbiology, Nov. 2001,vol. 39, 4204-4207.
Vidotto MC, Infect Immun. Jul. 1994;62(7):2940-6.
Akiyama et al.; “In Vitro Catalysis of Oxidative Folding of Disulfide-bonded Proteins by theEscherichia colidsbA (ppfA) Gene Product”, The Journal of Biological Chemistry, Nov. 5, 1992, pp. 22440-22445, vol. 267(31).
Canadian Office Action, issued Mar. 2, 2010 (published Mar. 2, 2010) during the prosecution of the corresponding Canadian Patent Application No. 2,466,156.
Non-Final Office Action issued Dec. 1, 2004 during the prosecution of U.S. Appl. No. 10/286,516.
Non-Final Office Action issued Jun. 17, 2005 during the prosecution of U.S. Appl. No. 10/286,516.
Final Office Action issued Nov. 29, 2005 during the prosecution of U.S. Appl. No. 10/286,516.
Non-Final Office Action issued Dec. 31, 2007 during the prosecution of U.S. Appl. No. 10/286,516.
Notice of Allowance and Fee(s) Due issued Apr. 30, 2008 during the prosecution of U.S. Appl. No. 10/286,516.
Supplementary European Search Report dated Mar. 29, 2006 for European Patent Application No. 02789388.3.
Akiyama et al., “In vitro catalysis of oxidative folding of disulfide-bonded proteins by theEscherichia colidsbA (ppfA) gene product,”J. Biol. Chem., 267:22440-22445, 1992.
Bardwell et al., “Identification of a protein required for disulfide bond formation in vivo,”Cell, 67:581-589, 1991.
Isihara et al., “Cloning and characterization of the gene for a protein thiol-disulfide oxidoreductase inBacillus brevis,”J. Bacteriol., 177:745-749,1995.
Liu et al., “Disulfide-dependent folding and export ofEscherichia coliDsbC,”J. Biol. Chem., 276:1146-1151, 2001.
Miranda-Vizuete et al., “Cloning, expression, and characterization of a novelEscherichia colithioredoxin,”J. Biol. Chem., 272:30841-30847, 1997.
Missiakas et al., “TheEscherichia-colidsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation,”EMBO J., 13:2013-2020, 1994.
Ng et al., “Cloning and expression of the gene for a protein disulfide oxidoreductase fromAzotobacter vinelandii: complementation of anEscherichia colidsbA mutant strain,”Gene, 188:109-113, 1997.
Raina et al., “Making and breaking disulfide bonds,”Annu. Rev. Microbiol., 51:179-202, 1997.
Russel et al., “The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins,”J. Biol Chem., 261:14997-15005, 1986.
McBride Jere W.
Walker David H.
Baskar Padma V
Fulbright & Jaworski L.L.P.
Mondesi Robert B
Research Development Foundation
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