Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2011-04-19
2011-04-19
Robinson, Hope A (Department: 1652)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
C530S300000
Reexamination Certificate
active
07928192
ABSTRACT:
ADP-ribosylating toxins fromNeisseria meningitidis, Streptomyces coelicolor, Mycoplasma pneumoniae, Salmonella typhimurium, Salmonella paratyphi, andStreptococcus pyogenesare disclosed, together with mutant toxins and uses therefor. There is only a low level of sequence identity between these toxins and toxins such as cholera toxin andE. coliheat labile toxin.
REFERENCES:
patent: 7115730 (2006-10-01), Pizza et al.
patent: 2006/0269563 (2006-11-01), Pizza et al.
patent: WO 95/17211 (1995-06-01), None
patent: 00/71725 (2000-11-01), None
patent: WO-02/079242 (2002-10-01), None
Seffernick et al. (J. Bacteriology, vol. 183, pp. 2405-2410, 2001.
(Wells, Biochemistry, vol. 29, pp. 8509-8517, 1990).
Tettelin et al. (Science, vol. 287, pp. 1809-1815, 2000).
Database Accession No. AX236858, last updated Sep. 26, 2001, located at www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nuccore&id=15796444>, last visited on Jan. 26, 2009.
Devos et al., Practical limits of function prediction. Proteins: Structure, Function, and Genetics. 2000, vol. 41: 98-107.
Freytag, LC. et al. (1999). “Bacterial Toxins as Mucosal Adjuvants,”Current Topics in Microbiology and Immunology236:215-236.
Glenn, G. et al. (1999). “Advances in Vaccine Delivery: Transcutaenous Immunisation,”Expert Opinion on Investigational Drugs8(6):797-805.
International Search Report mailed on Jan. 12, 2004, for PCT Application No. PCT/IB03/04295 filed on Sep. 1, 2003.
International Search Report mailed on Jul. 31, 2003, for PCT Application No. PCT/IB02/02080 filed on Mar. 28, 2002.
Scharton-Kersten, T. et al. (2000). “Transcutaneous Immunization with Bacterial ADP-Ribosylating Exotoxins, Subunits, and Unrelated Adjuvants,”Infection and Immunity68(9):5306-5313.
United States Office Action mailed on May 5, 2010, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
Whisstock, J.C. et al. (Aug. 2003). “Prediction of Protein Function from Protein Sequence and Structure,”Quarterly Review of Biophysics36(3):307-340.
Allured et al. (1986). “Structure of exotoxin A ofPseudomonas aeruginosaat 3.0-Angstrom Resolution,”Proceedings of the National Academy of Sciences, USA, 83:1320-1324.
Antoine et al. (1993). “Evidence for a Catalytic Role of Glutamic Acid 129 in the NAD-glycohydrolase Activity of the Pertussis Toxin S1 Subunit,”The Journal of Biological Chemistry, 268(32):24149-24155.
Barbieri et al. (1989). “Photolabeling of Glu-29 of the S-1 Subunit of Pertussis Toxin with NAD,”Infection and Immunity, 57(11):3549-3554.
Broun et al. (1998). “Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids,”Science, 282:1315-1317.
Burnette et al. (1988). “Pertusssi Toxin S1 Mutant with Reduced Enzyme Activity and a Conserved Protective Epitope,”Science, 242(4875):72-74.
Carroll et al. (1984). “NAD Binding Site of Diphtheria Toxin: Identification of a Residue Within the Nicotinamide Subsite by Photochemical Modification With NAD,”Proceedings of the National Academy of Sciences, USA, 81;3307-3311.
Domenighini et al. (1994). “Common Features of the NAD-binding and Catalytic Site of ADP-ribosylating Toxins,”Molecular Microbiology, 14(1):41-50.
Douglas et al. (1987). “Exotoxin A ofPseudomonas aeruginosa: Substitution of Glutamic Acid 553 with Aspartic Acid Drastically Reduces Toxicity and Enzymatic Activity,”Journal of Bacteriology, 169(11):4967-4971.
Douglas et al. (1990). “Pseudomonas aeruginosaExotoxin A: Alterations of Biological and Biochemical Properties Resulting from Mutation of Glutamic Acid 553 to Aspartic Acid,”Biochemistry, 29(21):5043-5049.
Kisseley, L. (2002). “Polypeptide release factors in prokaryotes and eukaryotes: same function, different structure,”Structure10:8-9.
Lobet et al. (1991). “Effect of Site-Directed Mutagenic Alterations on ADP-Ribosyltransferase Activity of the A Subunit ofEscherichia coliHeat-Labile Enterotoxin,”Infection and Immunity, 59(9):2870-2879.
Pizza et al. (1988). “Subunit S1 of pertussis toxin: Mapping of the Regions Essential for ADP-ribosyltransferase Activity,”Proceedings of the National Academy of Sciences, USA, 85:7521-7525.
Rappuoli et al. (1991). “Structure and Evolutionary Aspects of ADP-ribosylating Toxins,” inBacterial Protein Toxins. Alouf, J.E., Freer, J.H. (eds., London: Academic Press. p. 12.
Response to United States Office Action mailed on Jan. 11, 2008, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
Response to United States Office Action mailed on May 24, 2007, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
Response to United States Office Action mailed on May 7, 2009, for U.S. Appl. 10/526,125, filed Sep. 1, 2003.
Response to United States Office Action mailed on Sep. 17, 2008, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
Seffernick et al. (2001). “Melamine deaminase and Atrazine chlorohydrolase: 98 percent identical but functionally different,”Journal of Bacteriology183(8):2405-2410.
Thanabalu et al. (1991). “Cloning, Sequencing, and Expression of a Gene Encoding a 100-Kilodalton Mosquitocidal Toxin fromBacillus sphaericusSSII-1,”Journal of Bacteriology, 173(9):2776-2785.
Tsuji et al. (1991). “Glutamic Acid-112 of the A Subunit of Heat-Labile Enterotoxin From EnterotoxigenicEscherichia coilis Important for ADP-ribosyltransferase Activity,”FEBS, 291 (2):319-321.
Tweten et al. (1985). “Diphtheria Toxin: Effect of Substituting Aspartic Acid for Glutamic Acid 148 on ADP-Ribosyltransferase Activity,”The Journal of Biological Chemistry, 260(19):10392-10394.
United States Office Action mailed on Aug. 4, 2009, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
United States Office Action mailed on Dec. 29, 2006, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
United States Office Action mailed on Jul. 11, 2007, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
United States Office Action mailed on Mar. 17, 2008, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
United States Office Action mailed on Nov. 7, 2008, for U.S. Appl. No. 10/526,125, filed Sep. 1, 2003.
Wilson et al. (1990). “Active-Site Mutations of Diphtheria Toxin: Effects of Replacing Glutamic Acid-148 with Aspartic Acid, Glutamine, or Serine,”Biochemistry29:8643-8651.
Wishart et al. (1995). “A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase,”Journal of Biological Chemistry270(45):26782-26785.
Witkowski et al. (1999). “Conversion of b-ketoacyl synthase to a Malonyl Decarboxylase by replacement of the active cysteine with glutamine,”Biochemistry38:11643-11650.
Ala'Aldeen et al., “Cloning, sequencing, characterization and implications for vaccine design of the novel dihydrolipoyl acetyltransferase of Neisseria Meningitidis,” J. Medical Microbiology 45:419-432, 1996.
Database EMBL accession No. AE002482, “N. meningitides serogrop B strain MC58 section 124 of 206 of the complete genome,” Mar. 15, 2000.
Database SWALL accession No. Q91Z10, “Hypothetical protein NMB 1343,” Oct. 15, 2000.
Database EMBL accession No. X82637, “N. meningitides pdh gene cluster,” Nov. 25, 1994.
Database EMBL accession No. X77920, “N. meningitides outer membrane protein P64K (pm-6) gene,” Mar. 8, 1994.
Database EMBL accession No. AAA81487, “N. meningitides partial DNA sequence gnm—35 SEQ ID No. 35,” Dec. 4, 2000.
Database EMBL accession No. AX044032, “Neisseria genomic sequences; sequence 111,” Nov. 24, 2000.
Database EMBL accession No. CAA41592, “Cholera toxin A protein (CTA),” Mar. 25, 1991.
Database EMBL accession No. AAY966654, “Plant-optimized mutant V. cholera toxin subunit K63”, Jun. 2000.
Giudice et al., “Genetically derived toxoids for use as vaccines and adjuvants,” Vac
Masignani Vega
Pizza Mariagrazia
Rappuoli Rino
Hessler Amy
Littlefield Otis
Novartis AG
Robinson Hope A
LandOfFree
ADP-ribosylating bacterial toxins does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with ADP-ribosylating bacterial toxins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and ADP-ribosylating bacterial toxins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2660630