Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease
Reexamination Certificate
2004-04-08
2008-12-09
Swope, Sheridan (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Transferase other than ribonuclease
Reexamination Certificate
active
07462474
ABSTRACT:
This invention provides prokaryotic β1,4-N-acetylgalactosaminyl (GalNAc) transferases involved in synthesis of lipooligosaccharide (LOS). β1,4-GalNAc transferases are obtained from, for example,Campylobacterspecies, includingC. jejuni. In additional embodiments, the invention provides nucleic acids that encode the β1,4-GalNAc transferases, as well as expression vectors and host cells for expressing the β1,4-GalNAc transferases.
REFERENCES:
patent: 5352670 (1994-10-01), Venot et al.
patent: 5374541 (1994-12-01), Wong et al.
patent: 5545553 (1996-08-01), Gotschlich
patent: WO 92/16640 (1992-10-01), None
patent: WO 96/32491 (1996-10-01), None
patent: WO 99/49051 (1999-09-01), None
patent: WO 00/46379 (2000-08-01), None
patent: WO 0046379 (2000-08-01), None
Galye et al, Identification of regions in interleukin-1 alpha important for activity. J Biol Chem. Oct. 15, 1993;268(29):22105-11.
Whisstock et al, Prediction of protein function from sequence and structure. Q Rev Biophys. Aug. 2003;36(3):307-40. Review.
Blixt et al, Chemoenzymatic synthesis of 2-azidoethyl-ganglio-oligosaccharides GD3, GT3, GM2, GD2, GT2, GM1 and GD1a. Carbohydr Res. Sep. 5, 2005;340(12):1963-72.
Birkle et al, Role of tumor-associated gangliosides in cancer progression. Biochimie. Mar.-Apr. 2003;85(3-4):455-63. Review.
Livingston et al, Ganglioside vaccines with emphasis on GM2. Semin Oncol. Dec. 1998;25(6):636-45. Review.
Aspinall et al., “Lipopolysaccharides ofCampylobacter jejuniSerotype O:19: Structures of Core Oligosaccharide Regions from the Serostrain and Two Bacterial Isolates from Patients with the Guilliain-Barré Syndrome” Biochemistry, 33: 241-249 (1994b).
Aspinall et al., “Lipopolysaccharides ofCampylobacter jejuniSerotype O:19: Antigen Chains from the Serostrain and Two Bacterial Isolates from Patients with the Guillian-Barré Syndrome” Biochemistry, 33: 250-255 (1994c).
Aspinall, et al. “Chemical Structures of the Core Regions ofCampylobacter jejuniSerotypes O:1, 0:4. 0:23, and 0:36 Lipopolysaccharides,” European Journal of Biochemistry, vol. 213, No. 3, pp. 1017-1027. (May 1993).
Aspinall, et al. “Lipopolysaccharides fromCampylobacter jejuniAssociated with Guillian-Barré Syndrome Patients Mimic Human Gangliosides in Structure,” Infection and Immunity, vol. 62, No. 5, pp. 2122-2125, (May 1994).
Belunis et al., “Biosynthesis of Endotoxin” J. Biol. Chem., 267: 9988-9997 (1992).
Gaudino et al., “A Novel and Efficient Synthesis of Neolacto Series Gangliosides 3′-nLM1 anf 6′nLM1” J. Am. Chem. Soc., 116: 1149-1150 (1994).
Gilbert et al., “Cloning of the Lipooligosaccharide α-2, 3-Sialyltransferase from the Bacterial PathogensNeisseria mengingitidisandNeisseria gonorrhoeae,” Journal of Biological Chemistry, vol. 271, No. 45, pp. 28271-28276, The American Society for Biochemistry and Molecular Biology, Inc., USA, (Nov. 8, 1996).
Gilbert, et al., “Biosynthesis of Ganglioside Mimics inCampylobacter jejuniOH4384,” The Journal of Biolofical Chemistry, vol. 275, No. 6, pp. 3896-3906, The American Society for Biochemistry and Molecular Biology, Inc., USA, (Feb. 11, 2000).
Ito et al., “Synthesis of Bioactive Sialosides”Pure Appl. Chem., 65: 753 (1993).
Kuroki, “Campylobacter jejuniStrains from Patients with Guillain-Barré Syndrome Belong Mostly to Penner Serogroup 19 Contain β-N-Acetylglucosamine Residues” Ann. Neurol., 33:243-247 (1993).
Parkhill, et al. “The Genome Sequence of the Food-Borne PathogenCampylobacter jejuniReveals Hypervariable Sequences,” Nature, vol. 403, pp. 665-668, (Feb. 10, 2000).
Penner, et al., “Diversity of Lipopolysaccharide Structures inCampylobacter jejuni,” The Journal of Infectious Diseases, vol. 176, No. 2, pp. S135-S138, (Dec. 1997).
Prendergast, et al., “Lipopolysaccharides fromCampylobacter jejuniO:41 Strains Associated with Guillain- Barré Syndrome Exhibit Mimicry of GM1 Ganglioside,” Infection and Immunity, vol. 68, No. 8, pp. 3649-3677, (Aug. 1998).
Preston, et al., “The Lipooligosaccharides of Pathogenic Gram-Negative Bacteria,” Critical Reviews in Microbiology, vol. 22, No. 3, pp. 139-180, (1996).
Sabesan et al., “Combined Chemical and Enzymatic Synthesis of Sialyloligosaccharides and Characterization by 500-MHz 1H and C NMR Spectroscopy” J. Am. Chem. Soc., 108: 2068-2080 (1986).
Salloway, et al., “Miller-Fisher Syndrome Associated withCampylobacter jejuniBearing Lipopolysaccharide Molecules that Mimie Human Ganglioside GD3,” Infection and Immunity, vol. 64, No. 8, pp. 2945-2949, (Aug. 1996).
Wakarchuk et al., “Functional Relationships of the Genetic Locus Encoding the Glycosyltransferase Enzymes Involved in Expression of the Lacto-N-neotetraose Terminal Lipopolysaccharide Structure inNeisseria meningitidis” J. Biol. Chem.,. 271: 19166-19173 (1996).
Wood, et al., “Cloning, Mutation and Distribution of a Putative Lipopolysaccharide Biosynthesis Locus inCampylobacter jejuni,” Microbiology, vol. 145, No. 2, pp. 379-388, (Feb. 1999).
Aspinall et al., “Lipopolysaccharides ofCampylobacter jejuniSerotype O:19: Structures of Core Oligosaccharide Regions from the Serostrain and Two Bacterial Isolates from Patients with the Guillian-Barré Syndrome” Biochemistry, 33: 241-249 (1994b).
Aspinall et al., “Lipopolysaccharides ofCampylobacter jejuniSerotype O:19: Antigen Chains from the Serostrain and Two Bacterial Isolates from Patients with the Guillain-Barré Syndrome” Biochemistry, 33: 250-255 (1994c).
Aspinall, et al, “Chemical Structures of the Core Regions ofCampylobacter jejuniSerotypes 0:1, 0:4, 0:23, and 0:36 Lipopolysaccharides,”European Journal of Biochemistry, vol. 213, No. 3, pp. 1017-1027, (May 1993).
Aspinall, et al, “Lipopolysaccharides fromCampylobacter jejuniAssociated with Guillain-Barré Syndrome Patients Mimic Human Gangliosides In Structure,” Infection and Immunity, vol. 62, No. 5, pp. 2122-2125, (May 1994).
Ausuel et al., Protein Expression In: Current Protocols in Moecular Biology, Wiley and Sons, Inc. Chapter 18, (1987.
Belunis et al., “Biosynlhesis of Endotoxin” J. Biol. Chem., 267: 9988-9997 (1992).
Gaudino et al., “A Novel and Efficient Snythesis of Neolacto Series Gangliosides 3′-nLM1 and 6′-nLM1” J. Am. Chem. Soc., 116: 1149-1150 (1994).
Gilbert et al., “Cloning of the Lipooligosaccharide α-2,3-Sialyltransfarase from the Bacterial PathogensNeisseria meningitidisandNeisseria gonorrhoeae,” Journal of Biological Chemistry, vol. 271, No. 45, pp. 28271-28276, The American Society for Biochemistry and Molecular Biology, Inc. USA, (Nov. 8, 1996).
Gilbert, et al., “Biosynthesis of Ganglioside Mimics In,Campylobacter jejuniOH4384,” The Journal of Biolofical Chemistry, vol. 275, No. 6, pp. 3896-3906. The American Society for Biochemistry and Molecular Biology, Inc., USA, (Feb. 11, 2000).
Ito et al., “Synthesis of Bioactive Siatosides” Pure Appl. Chem., 65:753 (1993).
Kuroki, “Campylobacter jejuniStrains from Patients with Guillain-Barré Syndrome Belong Mostly to Penner Serogroup 19 Contain β-N-Acetylglucosamine Residues” Ann. Neurol., 33: 243-247 (1993).
Parkhill, et al, “The Genome Sequence of the Food-Borne PathogenCampylobacter jejuniReveals Hypervariable Sequences,” Nature, vol. 403, pp. 665-668. (Feb. 10, 2000).
Penner, et al., “Diversity of Upopolysaccharide Structures inCampylobacter jejuni,” The Journal of Infectious Diseases, vol. 176, No. 2, pp. S135-S138, (Dec. 1997).
Prendergast, et al., “Lipopolysaccharides fromCampylobacter jejuniO:41 Strains Associated with Guillian-Barré Syndrome Exhibit Mimicry of GM1 Ganglioside,” Infection and Immunity, vol. 66, No. 8, pp. 3649-3677, (Aug. 1998).
Preston, et al., “
Gilbert Michel
Wakarchuk Warren W.
National Research Council of Canada
Swope Sheridan
Townsend and Townsend / and Crew LLP
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