Mutant forms of meningococcal ADP-ribosylating toxin

Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Amino acid sequence disclosed in whole or in part; or...

Reexamination Certificate

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C424S184100, C435S199000, C536S023200, C530S300000, C530S328000, C530S329000, C530S350000

Reexamination Certificate

active

07858096

ABSTRACT:
NMB1343 is an ADP-ribosylating toxin fromNeisseria meningitidis. The invention provides a mutant toxin having a substitution at one or more of amino Glu-109, Glu-111 or Glu-120. The mutations(s) is/are preferably Glu to Asp. The protein of the invention preferably has reduced or eliminated ADP-ribosyltransferase and/or NAD-glycohydrolase activity relative to the wild-type protein.

REFERENCES:
patent: 7115730 (2006-10-01), Pizza et al.
patent: 2006/0057155 (2006-03-01), Masignani et al.
patent: WO 95/17211 (1995-06-01), None
patent: WO 02/079242 (2002-10-01), None
Domenighini et al., Common features of the NAD-binding and catlytic site of ADP-ribosylating toxins. Mol. Microbiol., 1994, vol. 14 (1): 41-50.
Broun et al., Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids. Science, 1998, vol. 282: 1315-1317.
Kisselev L., Polypeptide release factors in prokaryotes and eukaryotes: same function, different structure. Structure, 2002, vol. 10: 8-9.
Seffernick et al., Melamine deaminase and Atrazine chlorohydrolase: 98 percent identical but functionally different. J. Bacteriol.,2001, vol. 183 (8): 2405-2410.
Wishart et al., A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase. J. Biol. Chem., 1995, vol. 270(45): 26782-26785.
Witkowski et al., Conversion of b-ketoacyl synthase to a Malonyl Decarboxylase by replacement of the active cysteine with glutamine. Biochemistry, 1999, vol. 38: 11643-11650.
Devos et al., Practical limits of function prediction. Proteins: Structure, Function, and Genetics. 2000, vol. 41: 98-107.
Whisstock et al., Prediction of protein function from protein sequence. Q. Rev. Biophysics., 2003, vol. 36 (3): 307-340.
Tettelin, H. et al. “Complete Genome Sequence ofNeisseria meningitidisSerogroup B Strain MC58,” Science, 287: 1809-1815 (2000).
Del Giudice, G. et al. “Genetically derived toxoids for use as vaccines and adjuvants,” Vaccine, 17, Suppl 2: S44-S52 (1999).
Allured et al. (1986). “Structure of exotoxin A ofPseudomonas aeruginosaat 3.0-Angstrom resolution,”Proc. Natl. Acad. Sci.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.
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,” Proc.Natl. Acad. Sci. 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.
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,”Proc. Natl. Acad. Sci., 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.
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 coliis 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.
Wilson et al. (1990). “Active-Site Mutations of Diphtheria Toxin: Effects of Replacing Glutamic Acid-148 with Aspartic Acid, Gitamine, or Serine,”Biochemistry29:8643-8651.
Ala'Aldeen, D. et al. (1996).“Cloning, Sequencing, Characterization and Implications for Vaccine Design of the Novel Dihydrolipoyl Acetyltransferase ofNeisseria meningitidis,” Journal of Medical Microbiology45:419-432.
Database Accession No. AX236858, last updated Sep. 26, 2001, located at <http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nuccore&id=15796444>, last visited on Jan. 26, 2009, 1 page.
Database EMBL Accession No. AE002482, last updated May 25, 2000, located at <http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nuccore&id=7226577>, last visited on Jan. 22, 2009, 8 pages.
Database EMBL Accession No. AX044032, last updated Nov. 24, 2000, located at <http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nuccore&id=11342916>, last visited on Jan. 23, 2009, 99 pages.
Database EMBL Accession No. CAA41592, last updated Sep. 23, 1991, located at <http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=protein&id=48421>, last visited on Jan. 23, 2009, 2 pages.
Database EMBL Accession No. X77920, last updated May 14, 1999, located at <http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nuccore&id=534954>, last visited on Jan. 22, 2009, pages.
Database EMBL Accession No. X82637, last updated Jan. 7, 1997, located at <http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nuccore&id=577781>, last visited on Jan. 22, 2009, 3 pages.
Database SWALL Accession No. Q9JZ10, last updated Oct. 31, 2006, located at <http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=protein&id=81784521>, last visited on Jan. 22, 2009, 2 pages.
Database EMBL Accession No. AAA81487 Database EMBL [Online] Dec. 4, 2000 Frazer, C.M. et al. (Apr. 20, 2000). “N. meningitidespartial DNA sequence gnm—35 SEQ ID No. 35” retrieved from EBI Database accession No. AAA81487 XP002239408 & WO 00 22430 A (Chiron Corp.).
Database EMBL Accession No. AAY96654 Database EMBL [Online] Mason, H. S. and Arntzen, C.J. (Jun. 29, 2000): “Plant-optimized mutant V.cholera toxin subunit K63” retrieved from EBI Database accession No. AAY96654 XP002239411.
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, 3 pages.
International Search Report mailed on Jul. 31, 2003, for PCT Application No. PCT/IB02/02080 filed on Mar. 28, 2002, 7 pages.
Krueger, K. et al. (1995). “The Family of Bacterial ADP-ribosylating Exotoxins,”Clinical Microbiology Reviews8:34-47.
Scharton-Kersten, T. et al. (2000). “Transcutaneous Immunization with Bacterial ADP-Ribosylating Exotoxins, Subunits, and Unrelated Adjuvants,”Infection and Immunity68(9): 5306-5313.
Seffernick, J. et al. (2001). “Melamine Deaminase and Atrazine Chlorohydrolase: 98 Percent Identical but Functionally Different,”Journal

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