Prolyl tripeptidyl peptidases nucleic acid of Porphyromonas...

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C536S023200, C536S063000, C514S04400A, C435S004000, C435S006120, C435S069100, C435S198000, C530S350000

Reexamination Certificate

active

06875851

ABSTRACT:
The present invention provides isolated polypeptides, prolyl tripeptidyl-peptidases, and active analogs, active fragments or active modifications thereof, having amidolytic activity for cleavage of a peptide bond present in a target peptide having at least 30 amino acids. Isolated nucleic acid fragments encoding isolated prolyl tripeptidyl-peptidases are also provided, as are methods of reducing growth of a bacterium by inhibiting a prolyl tripeptidyl-peptidase.

REFERENCES:
patent: 4543329 (1985-09-01), Daum et al.
patent: 5223404 (1993-06-01), Suido et al.
patent: 5432055 (1995-07-01), Evans et al.
patent: 5475097 (1995-12-01), Travis et al.
patent: 5521081 (1996-05-01), Inaoka et al.
patent: 5523390 (1996-06-01), Travis et al.
patent: 5824791 (1998-10-01), Progulske-Fox et al.
patent: 5919690 (1999-07-01), Halkier et al.
patent: 5976854 (1999-11-01), Jones et al.
patent: 5981164 (1999-11-01), Wilstrom
patent: 6129917 (2000-10-01), Potempa et al.
patent: 6274718 (2001-08-01), Travis et al.
patent: 6284511 (2001-09-01), Inaoka et al.
patent: 6444799 (2002-09-01), Ross
patent: 255341 (1998-05-01), None
patent: 02-5580 (1990-01-01), None
patent: 9423022 (1994-10-01), None
patent: 974447 (1997-11-01), None
patent: WO 0052147 (2000-09-01), None
Martinsson et al, 1993, Genomics, vol. 17, pp. 493-495.*
Hillier et al (Genbank Accession number R11686, created date Apr. 21, 1995), (SEQ Algn. only).*
Kabashima, T et al, J. Biochemistry, vol. 120, pp. 1111-1117, 1996, Swiss-prot accession number P95782, xanthomonas maltophilia dipeptidyl peptidase IV, (sequence alignment abstract only).*
Diefenthal, T et al, Appl. Microbiol. Biotechnol. vol. 40, pp. 90-97, 1993, Cloning of proline-specific endopeptidase gene fromFlavobacterium meningosepticum:expression inEscherichia coliand purification of the heterologous protein.*
Kanatani, Akio et al, Journal of Biochemistry, vol. 113, pp. 790-796, 1993, Prolyl Endopeptidase fromAeromonas hydrophila: Cloning, sequencing, and expression of the enzyme gene and characterization of the expressed enzyme.*
Vanhoof, G et al, Gene, vol. 149, (1994),pp. 363-366, Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase.*
Abbott et al., “Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene”Immunogenetics(1994)40:331-338, accession No. U1378.
Andersen et al., “Presence and possible role of a renal brush-border Gly-Pro-X-releasing exopeptidase”,American Journal of Physiology, 253(4 Pt 2):F648-F655 (1987).
Binnie et al., “Isolation and Characterization of Two Genes Encoding Proteases Associated with the Mycelium ofStreptomyces lividans66”,Journal of Bacteriology, 177(21):6033-6040 (1995).
Renn et al., “Characterization and Cloning of Tripeptidyl Peptidase II from the Fruit Fly,Drosophila melanogaster”, The Journal of Biological Chemistry, 273(30):19173-19182 (1998).
Abiko et al., “Glycylprolyl Dipeptidylaminopeptidase fromBacteroides gingivalis,” J. Dent. Res., 64(2):106-111 (1985).
Altschul et al., “Gapped BLAST and PSI-BLAST: A New Generation of Protein Database Search Programs,”Nuc. Acids Res., 25(17):3389-3402 (1997).
Ausubel et al., eds.,Current Protocols in Molecular Biology, John Wiley & Sons, Inc., United States, title page, publication page and table of contents only, 12 pages (1994).
Banbula et al., “Unusual Processing of Proteins and Polypeptides During the Growth ofPorphyromonas gingivalis: Implications of a Primary Role for Prolyl Di- and Tripeptidyl-Peptidases,”J. Dent. Res., 78:466, Abstract No. 2888 (May, 1999).
Banbula et al., “Unusual Processing of Proteins and Polypeptides During the Growth ofPorphyromonas gingivalis: Implication of a Primary Role for Prolyl Di and Tripeptidyl-Peptidases,” poster presentation (6 pages) at Edward H. Hatton Awards Competition, Vancouver (B.C.), Canada (Mar. 9, 1999).
Banbula et al., “Prolyl Tripeptidyl Peptidase fromPorphyromonas gingivalis, A Novel Enzyme with Possible Pathological Implications for the Development of Periodontitis,”J. Biol. Chem., 274(14):9246-9252 (Apr. 2, 1999).
Banbula et al., “Emerging Family of Proline-Specific Peptidases ofPorphyromonas gingivalis: Purification and Characterization of Serine Dipeptidyl Peptidase, a Structural and Functional Homologue of Mammalian Prolyl Dipeptidyl Peptidase IV,”Infect. Immun., 68(3):1176-1182 (Mar., 2000).
Barua et al., “Purification of an 80,000-MrGlycylprolyl Peptidase fromBacteroides gingivalis,”Infect. Immun., 57(8):2522-2528 (1989).
Brosius et al., “Gene Organization and Primary Structure of a Ribosomal RNA Operon fromEscherichia coli, ”J. Mol. Biol., 148:107-127 (1981).
Chen et al., “Purification and Characterization of a 50-kDa Cysteine Proteinase (Gingipain) FromPorphromonas gingivalis,”J. Biol. Chem., 267(26):18896-18901 (1992).
Church et al., “Genomic Sequencing,”Proc. Natl. Acad. Sci. USA, 81(7)1991-1995 (1984).
Dashper et al., “Amino Acid and Peptide Uptake byPorphyromonas gingivalis,” J. Dent. Res., 77(5):1133, Abstract No. 36 (1998).
Fülöp et al., “Prolyl Oligopeptidase: An Unusual Beta-Propeller Domain Regulates Proteolysis,”Cell, 94(2):161-170 (1998).
Grenier et al., “Isolation of a Membrane-AssociatedBacteroides gingivalisGlycylprolyl Protease,”Infect. Immun., 55(12):3131-3136 (1987).
Hinode et al., “Purification and Characterization of Three Types of Proteases from Culture Supernatants ofPorphyromonas gingivalis,”Infect. Immun., 59(9):3060-3068 (1991).
Kabashima et al., “Cloning, Sequencing, and Expression of the Dipeptidyl Peptidase IV Gene formFlavobacterium meningosepticuminEscherichia coli,”Arch. Biochem. Biophys., 320(1):123-128 (1995), accession No. Q47900.
Kiyama et al., “Sequence Analysis of thePorphyromonas gingivalisDipeptidyl Peptidase IV Gene,”Biochim. Biophys. Acta, 1396, 39-46 (1998), Mar. 4.
Kornman, “Controlled-Release Local Delivery Antimicrobials in Periodontics: Prospects for the Future,”J. Periodontol., 64(8):782-791 (1993).
Matsudaira, “Sequence from Picomole Quantities of Proteins Electroblotted onto Polyvinylidene Difluoride Membranes,”J. Biol. Chem., 262(21):10035-10038 (1987).
“MS-Fit, A peptide-mass fingerprinting tool,” Ludwig Institute for Cancer Research & University College London, 2000.
Nakamura et al., “Cloning of the Gene Encoding a Glycylprolyl Aminopeptidase fromPorphyromonas gingivalis,”Arch. Oral Biol., 37(10):807-812 (1992).
“Open Reading Frame Finder,” National Center for Biotechnology Information (NCBI), (available on or before Mar. 3, 2000).
Potempa et al., “Host andPorphyromonas gingivalisProteinases in Periodontitis: A Biochemical Model of Infection and Tissue Destruction,”Perspect. Drug Discovery Design, 2:445-458 (1995).
Rawlings et al., “A New Family of Serine-type Peptidase Related to Prolyl Oligopeptidase,”Biochem. J., 279(Pt. 3):907-908 (1991).
Sambrook et al.,Molecular Cloning, a Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, title page, publication page and table of contents only, 30 pgs. (1989).
Schägger et al., “Tricine-Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis for the Separation of Proteins in the Range from 1 to 100 kDa,”Anal. Biochem., 166:368-379 (1987).
Slots et al., “The Occurrence ofActinobacillus actinomycetemcomitans, Bacteroides gingivalisandBacteroides intermediusin Destructive Periodontal Disease in Adults,”J. Clin. Periodontol., 13:570-577 (1986).
Stenfors et al., “Characterization of Endogenous Neuropeptide Y in Rat Hippocampus and its Metabolism by Nanospray Mass Spectrometry,”J. Biol. Chem., 272(9):5747-5751 (1997).
“TIGR,” The Institute for Genomic Research, (available on or

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Prolyl tripeptidyl peptidases nucleic acid of Porphyromonas... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Prolyl tripeptidyl peptidases nucleic acid of Porphyromonas..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Prolyl tripeptidyl peptidases nucleic acid of Porphyromonas... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3411663

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.