Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease
Reexamination Certificate
2007-07-03
2007-07-03
Swope, Sheridan (Department: 1656)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Transferase other than ribonuclease
C435S069700, C435S252330
Reexamination Certificate
active
10962235
ABSTRACT:
This invention provides prokaryotic glycosyltransferases, including a bifunctional sialyltransferase that has both an α2,3- and an α2,8-activity. A β1,4-GalNAc transferase and a β1,3-galactosyltransferase are also provided by the invention, as are other glycosyltransferases and enzymes involved in synthesis of lipooligosaccharide (LOS). The glycosyltransferases can be obtained from, for example,Campylobacterspecies, includingC. jejuni. In additional embodiments, the invention provides nucleic acids that encode the glycosyltransferases, as well as expression vectors and host cells for expressing the glycosyltransferases.
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
USPTO STIC in house alignment SEQ ID No. 17 with SEQ ID No. 21 of U.S. Appl. No. 09/962,235 performed Aug. 25, 2006.
Gilbert et al, The genetic bases for the variation in the lipo-oligosaccharide of the mucosal pathogen,Campylobacter jejuni. Biosynthesis of sialylated ganglioside mimics in the core oligosaccharide. J Biol Chem. Jan. 4, 2002;277(1):327-37. Epub Oct. 31, 2001.
Livingston, Ganglioside vaccines with emphasis on GM2. Semin Oncol. Dec. 1998;25(6):636-45. Review.
Parkhill, J., et al., “The genome sequence of the food-borne pathogenCampylobacter jejunireveals hypervariable sequences,” Nature, Feb. 10, 2000, 403:665-668.
http://web.archive.org/web/*/http://www.sanger.ac.uk/Projects/C—jejuni/ Search Results for Jan. 1, 1996-Apr. 7, 2004.
Aspinall et al., “Lipopolysaccharides ofCampylobacter jejuniSerotype O:19: Structures of Core Oligosaccharide Regions from the Serostrain and Two Bacterial Isolates from Patients with the Guillain-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).
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 and 6'-nLM1” J. Am. Chem. Soc., 116: 1149-1150 (1994).
Gilbert et al., “Cloning of the Lipooligosaccharide α-2,3-Sialyttransferase from the Bacterial Pathogens Neisseria Meningitidis and Neisseria 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 formCampylobacter jejuniO:41 Strains Associated with Guillain-Barré Syndrome Exhibit Mimicry of GM1 Ganglioside,” Infection and Immunity, vol. 66, No. 6, 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 Moiecules 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 in Neisseria 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).
Ausubel et al Protein Expression In: Current Protocols in Molecular Biology Wiley and Sons, Inc. 1987 Chapter 16.
Tomb et al The complete genome sequence of the gastric pathogen Helicobacter pylori. Swiss-Prot Acc#A64547. Alignment with SEQ ID No. 17.
Gilbert Michel
Wakarchuk Warren W.
National Research Council of Canada
Swope Sheridan
Townsend and Townsend / and Crew LLP
LandOfFree
β 1,4-N-acetylgalactosaminyl transferases from C. jejuni does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with β 1,4-N-acetylgalactosaminyl transferases from C. jejuni, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and β 1,4-N-acetylgalactosaminyl transferases from C. jejuni will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3809970