B1,4-N-acetylglucosaminyl (GALNAC) transferase polypeptides

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease

Reexamination Certificate

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Reexamination Certificate

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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.

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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).
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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., “

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