Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease
Reexamination Certificate
2006-10-11
2009-10-27
Swope, Sheridan (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Transferase other than ribonuclease
Reexamination Certificate
active
07608442
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 alignment GenBank AF130984 (from Gilbert et al, 2000; IDS) vs SEQ ID No. 40. Performed May 8, 2008.
USPTO in house alignment GenBank AF130984 (from Gilbert et al, 2000; IDS) vs SEQ ID No. 41. Performed May 8, 2008.
Linton et al, Biosynthesis of ganglioside mimics inCampylobacter jejuniOH4384. Identification of the glycosyltransferase genes, enzymatic synthesis of model compounds, and characterization of nanomole amounts by 600-mhz (1)h and (13)c NMR analysis. J Biol Chem. Feb. 11, 2000;275(6):3896-906.
Piesecki et al, Immobilization of B-galactosidase for application in organic chemistry using a chelating peptide. Biotech & Bioeng. Jun. 1993; 42(2): 178-184.
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).
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).
Ausubel et al.; “Protein Expression” In:Current Protocols in Molecular Biology; Wiley and Sons, Inc.; 1987; Chapter 16.
Belunis et al., “Biosynthesis of Endotoxin”J. Biol. Chem., 267: 9988-9997 (1992).
Guadino 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-Sialyltransferase 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 Biological 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. 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).
Tomb et al. ; “The complete genome sequence of the gastric pathogenHelicobacter pylon”; Swiss-Prot Accession No. A64547. Alignment with SEQ ID No. 17.
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).
Database; GenBank Accession No. AL111168;Campylobacter jejunisubsp.jejuniNCTC11168 complete genome; Jul. 18, 2002.
http://web.archive.org/web/*/http://www.sanger.ac.uk/Project/C—jejuni/ Search results for Jan. 1, 1996 through Apr. 7, 2004. “Campylobacter jejuni” Accessed on: Apr. 16, 2004.
Gilbert Michel
Wakarchuk Warren W.
National Research Council of Canada
Swope Sheridan
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