Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Bacterium or component thereof or substance produced by said...
Reexamination Certificate
2005-09-06
2005-09-06
Swartz, Rodney P. (Department: 1645)
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Bacterium or component thereof or substance produced by said...
C424S009100, C424S009200, C424S184100, C424S185100, C424S192100, C424S200100, C424S234100, C530S300000, C530S350000, C536S023700
Reexamination Certificate
active
06939548
ABSTRACT:
The present invention relates to the field of medical immunology and further to pharmaceutical compositions, methods of making and methods of use of vaccines. More specifically this invention relates to recombinant proteins derived from the genes encodingClostridium difficiletoxin A and toxin B, and their use in an active vaccine againstC. difficile.
REFERENCES:
patent: 4530833 (1985-07-01), Wilkins et al.
patent: 4533630 (1985-08-01), Wilkins et al.
patent: 4863852 (1989-09-01), Wilkins et al.
patent: 4879218 (1989-11-01), Wilkins et al.
patent: 5098826 (1992-03-01), Wilkins et al.
patent: 5736139 (1998-04-01), Kink et al.
patent: 5919463 (1999-07-01), Thomas et al.
patent: WO 96/12802 (1996-05-01), None
patent: WO 97/02836 (1997-01-01), None
Barroso et al. “Nucleotide Sequence ofClostridum difficileToxin B Gene” Nucl. Acids Res. 18:4004 (1990).
Dove et al. “Molecular Characterization of theClostridum difficileToxin A Gene” Infect. Immun. 58:480-488 (1990).
Eichel-Streiber et al. “Clostridum difficileToxin A Carries a C-Terminal Repetitive Structure Homologous to the Carbohydrate Binding Region of Streptococcal Glycosyltransferases” Gene 96:107-113 (1992).
Faust et al. “The Enzymatic Domain ofClostridium difficileToxin A is Located within Its N-Terminal Region” Biochem. Biophys. Res. Commun. 251:100-105 (1998).
Hofmann et al. “Localization of the Glucosyltransferase Activity ofClostridium difficileToxin B to the N-Terminal Part of the Holotoxin” J. Biol. Chem. 272:11074-11078 (1997).
Just et al. “Glucosylation of Rho Proteins byClostridium difficileToxin B” Nature 375:500-503 (1995).
Just et al. “The Enterotoxin fromClostridium difficile(ToxA) Monoglucosylates the Rho Proteins” J. Biol. Chem. 270:13932-13939 (1995).
Krivan et al. “Cell Surface Binding Site forClostridium difficileEnterotoxin: Evidence for a Glycoconjugate Containing the Sequence . . . ” Infect. Immun. 53:573-581 (1986).
Lyerly et al.Infections of the Gastrointestinal TractChapter 5, pp. 867-891 (1995).
Lyerly et al. “Vaccination Against LethalClostridium difficileEnterocolitis with a Nontoxic Recombinant Peptide of Toxin A” Current Microbiology 21:29-32 (1990).
Makoff et al. “Expression of Tetanus Toxin Fragment C inE. coli: Its Purification and Potential Use as a Vaccine” Bio/Technology 7:1043-1046 (1989).
Makoff et al. “Expression of Tetanus Toxin Fragment C inE. coli: High Level Expression by Removing Rare Codons” Nucleic Acids Res. 17:10191-10202 (1989).
Moncrief et al. “Positive Regulation ofClostridium difficileToxins” Infect. Immun. 65:1105-1108 (1997).
Tucker et al. “Toxin A ofClostridium difficileBinds to the Human Carbohydrate Antigens I, X and Y” Infect, Immun. 59:73-78 (1991).
Lyerly David M.
Moncrief J. Scott
Phelps Carol
Wilkins Tracy D.
Zheng Limin
Swartz Rodney P.
Techlab, Inc.
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