Hyaluronan synthase gene and uses thereof

Details Hyaluronan synthase gene and uses thereof Hyaluronan synthase gene and uses thereof

2006-12-26

2006-12-26

Wax, Robert A. (Department: 1653)

Chemistry: molecular biology and microbiology

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

Transferase other than ribonuclease

C435S097000

Reexamination Certificate

active

07153677

ABSTRACT:
The present invention relates to a recombinantly produced, enzymatically active hyaluronan synthase, wherein the recombinantly produced, enzymatically active hyaluronan synthase is a single protein that is a dual-action catalyst that utilizes UDP-GlcA and UDP-GlcNAc to synthesize HA. The recombinantly produced, enzymatically active hyaluronan synthase may be produced from a hyaluronan synthase gene isolated from a microbial source, such as a streptococcal source.

REFERENCES:
patent: 4224179 (1980-09-01), Schneider
patent: 4235871 (1980-11-01), Papahadjopoulos et al.
patent: 4511478 (1985-04-01), Nowinski et al.
patent: 4517295 (1985-05-01), Bracke et al.
patent: 4708861 (1987-11-01), Popescu et al.
patent: 4780414 (1988-10-01), Nimrod et al.
patent: 4782046 (1988-11-01), Brown et al.
patent: 4784990 (1988-11-01), Nimrod et al.
patent: 4801539 (1989-01-01), Akasaka et al.
patent: 5015577 (1991-05-01), Weigel et al.
patent: 5023175 (1991-06-01), Hosoya et al.
patent: 5071751 (1991-12-01), Morita et al.
patent: RE37336 (2001-08-01), Weigel et al.
patent: 6423514 (2002-07-01), Briskin
patent: 0036776 (1988-05-01), None
patent: 0195303 (1989-11-01), None
patent: 0144019 (1990-06-01), None
patent: 0266578 (1993-07-01), None
patent: 0244757 (1994-11-01), None
patent: 2249315 (1992-05-01), None
patent: 60-060177 (1985-03-01), None
patent: 62032893 (1987-02-01), None
patent: 63094988 (1988-04-01), None
patent: 02193818 (1992-03-01), None
patent: 4-158796 (1992-06-01), None
patent: 91/03559 (1991-03-01), None
patent: 94/00463 (1994-01-01), None
patent: 95/24497 (1995-09-01), None
patent: 97/20061 (1997-06-01), None
“The Biosynthesis of Hyaluronic Acid byStreptococcus,” Stoolmiller, et al., Journal of Biological Chemistry, vol. 244, No. 2, pp. 236-246 (1969).
“Modern Genetics,” Ayala, et al., Benjamin/Cummings Publishing Col., Menlo Park CA, p. 45 (1980).
“Strains ofEscherichia coliCarrying the Structural Gene for Histidyl-tRNA Synthetase on a High Copy-Number Plasmid,” Eisenbeis, et al., Mol. Gen. Genet. 183:115-122 (1981).
“Synthesis of Hyaluronate in Differentiated Teratocarcinoma Cells,” Prehm, et al., J. Biochem, vol. 211, pp. 191-198 (1983).
“Isolation, Structure and Expression of Mammalian Genes for Histidyl-tRNA Synthetase,” Tsui, et al., Nucleic Acids Research, vol. 15, No. 8, pp. 3349-3367, (1997).
“Shuttle Vectors Containing a Multiple Cloning Site and a Lacza Gena for Conjugal Transfer of DNA FromEscherichia colito Gram-Positive Bacteria,” Trieu-Cout, et al., Gene, vol. 102, pp. 99-104, (1991).
“Analysis of teh Streptococcal Hyaluronic Acid Synthase Complex Using the photoaffinity Probe 5-Azido-UDP-Glucuronic Acid,” Van de Rijn, et al., J. Biol., Chem., vol. 267, No. 34, pp. 24302-24306, (1992).
“Molecular Characterization of a Locus Required for Hyaluronic Acid Capsule Production in Group AStreptococci,” Dougherty, et al., J. Exp. med., vol. 175, pp. 1291-1299, (1992).
“Hyaluronan,” Laurent, et al., FASEB Journal, vol. 6, pp. 2397-2404, (1992).
“Isolation of aStreptococcus pyogenesGene Locus That Directs Hyaluronan Biosynthesis in Acapsular Mutants and in Heterologous Bacteria,” DeAngelis, et al., J. Biol. Chem., vol. 268, No. 20, pp. 14568-14571, (1993).
“Hyaluronate Synthase: Cloning and Sequencing of the Gene FromStreptococcussp.,” Lansing, et al., J. Biochem., vol. 289, pp. 179-184, (1993).
“Molecular Characterization of HasB From an Operon Required for Hyaluronic Acid Synthesis in Group AStreptococci,” Dougherty, et al., J. Biol. Chem., vol. 268, No. 10, pp. 7118-7124, (1993).
“Molecular Cloning, Identification, and Sequence of the Hyaluronan Synthase Gene From Group AStreptococcus pyogenes,” DeAngelis, et al., J. Biol. Chem., vol. 268, No. 26, pp. 19181-19184, (1993).
“Molecular Characterization of HasA From an Operon Required for Hyaluronic Acid Synthesis in Group AStreptococci,” Dougherty, et al., J. Biol. Chem., vol. 269, No. 1, pp. 169-175, (1994).
“TheStreptococcus pyogenesHyaluronan Synthase: Sequence Comparison and Conservation Among Various Group A Strains,” DeAngelis, et al., Biochem. and Biophy. Res. Comm., vol. 1999, No. 1, pp. 1-10, (1994).
“The Production of Capsules, Hyaluronic Acid and Hyaluronidase by Group A and Group CStreptococci”, MacLennan, J. Gen. Microbiol., 14:134-142 (1956).
“The Isolation and Characterization of a Hyaluronidase Produced by a Capsulated Strain of Group CStreptococcus”, MacLennan, J. Gen. Microbiol., 14:143-152 (1956).
“The Biosynthesis of Hyaluronic Acid by Group AStreptococcus”, Markovitz et al., J. Biol. Chem., 234 (9):2343-2350 (1959).
“Biosynthesis of Hyaluronic Acid byStreptococcus”, Sugahara et al., J. Biol. Chem., 254:6252-6261 (1979).
“Streptococcal Hyaluronic Acid: Proposed Mechanisms of Degradation and Loss of Synthesis During Stationary Phase”, Van de Rijn, J. Bacteriol., 156(3):1059-1065 (1983).
“Solubilization of Hyaluronic Acid Synthetic Activity FromStreptococciand its Activation With Phospholipids”, Triscott et al., J. Biol. Chem., 261(13):6004-6009 (1986).
“Isolation of Streptococcal Hyaluronate Synthase”, Prehm et al., Biochem. J., 235:887-889 (1986).
“Homologs of the Xenopus Developmental Gene DG42 are Present in Zebrafish and Mouse and are Involved in the Synthesis of Nod-Like Chitin Oligosaccharides During Early Embryogenesis”, Semino et al., Proc. Natl. Acad. Sci. USA, 93:4548-4553 (1996).
“Enzymological Characterization of thePasteurella multocidaHyaluronic Acid Synthase”, DeAngelis, Biochemistry, 35 (30): 9768-9771 (1996).
“Molecular Cloning, Expression, and Characterization of the Authentic Hyaluronan Synthase From Group CStreptococcus equisimilis”, Kumari and Weigel, J. Biol. Chem., 272(51): 32539-32546 (1997).
“Hyaluronan Synthases”, Weigel et al., J. Biol. Chem., 272 (22): 13997-14000 (1997).
“Identification and Molecular Cloning of a Unique Hyaluronan Synthase FromPasteurella multocida”, DeAngelis et al., J. Biol. Chem., 273(14): 8454-8458 (1998).
Heldermon et al.; Site-directed mutation of conserved cysteine residues does not inactivate theStreptococcus pyogeneshyaluronan synthase. Glycobiology. 2001, vol. 11, No. 12, pp. 1017-1024, see entire document.
“The Production of Capsules, Hyaluronic Acid and Hyaluronidase by Group A and Group CStreptococci”, MacLennan, J. Gen. Microbiol., 14:134-142 (1956).
“The Isolation and Characterization of a Hyaluronidase Produced by a Capsulated Strain of Group CStreptococcus”, MacLennan, J. Gen. Microbiol., 14:143-152 (1956).
“The Biosynthesis of Hyaluronic Acid by Group AStreptococcus”, Markovitz et al., J. Biol. Chem., 234 (9):2343-2350 (1959).
“Biosynthesis of Hyaluronic Acid byStreptococcus”, Sugahara et al., J. Biol. Chem., 254:6252-6261 (1979).
“Streptococcal Hyaluronic Acid: Proposed Mechanisms of Degradation and Loss of Synthesis During Stationary Phase”, Van de Rijn, J. Bacteriol., 156(3):1059-1065 (1983).
“Solubilization of Hyaluronic Acid Synthetic Activity FromStreptococciand its Activation With Phospholipids”, Triscott et al., J. Biol. Chem., 261(13):6004-6009 (1986).
“Isolation of Streptococcal Hyaluronate Synthase”, Prehm et al., Biochem. J., 235:887-889 (1986).
Tan, SW et al.; “Hyaluronic Acid-A Versatile Biopolymer”; Australian J. of Biological Chem. vol. 4, No. 1:38-43 (1990).

Affiliated with

Also associated with

Rating

Hyaluronan synthase gene and uses thereof does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Hyaluronan synthase gene and uses thereof, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Hyaluronan synthase gene and uses thereof will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3717048