β 1,4-N-acetylgalactosaminyltransferases from C. jejuni

Details β 1,4-N-acetylgalactosaminyltransferases from C. jejuni β 1,4-N-acetylgalactosaminyltransferases from C. jejuni

2007-01-30

2007-01-30

Swope, Sheridan (Department: 1656)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Transferase other than ribonuclease

C435S071100, C435S070100, C530S412000

Reexamination Certificate

active

10845408

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 in house Jul. 4, 2006. BLAST alignment of SEQ ID No. 23 with SEQ ID No. 17.
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.
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.
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 pathogenHelicobacter pylori. Jan. 1, 1998 Swiss-Prot Acc#A64547. Alignment with SEQ ID No. 17.
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 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 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 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 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. 66, 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 Sialytoligosaccharides 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).

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