Production of lysosomal enzymes in plants by transient...

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

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C435S018000, C435S069100, C530S350000

Reexamination Certificate

active

06887696

ABSTRACT:
The invention relates to α-galactosidase truncated at the carboxy terminus and the production of enzymatically active recombinant human and animal lysosomal enzymes involving construction and expression of recombinant expression constructs comprising coding sequences of human or animal lysosomal enzymes in a plant expression system. The plant expression system provides for post-translational modification and processing to produce a recombinant gene product exhibiting enzymatic activity. The invention is demonstrated by working examples in which transgenic tobacco plants express recombinant expression constructs comprising human glucocerebrosidase nucleotide sequences. The invention is also demonstrated by working examples in which transfected tobacco plants express recombinant viral expression constructs comprising human α galactosidase nucleotide sequences. The recombinant lysosomal enzymes produced in accordance with the invention may be used for a variety of purposes, including but not limited to enzyme replacement therapy for the therapeutic treatment of human and animal lysosomal storage diseases.

REFERENCES:
patent: 5179023 (1993-01-01), Calhoun et al.
patent: 5401650 (1995-03-01), Desnick et al.
patent: 5580757 (1996-12-01), Desnick et al.
patent: 5589367 (1996-12-01), Donson et al.
patent: 5929304 (1999-07-01), Radin et al.
patent: 5977438 (1999-11-01), Turpen et al.
patent: 6210666 (2001-04-01), Miyamura
patent: 6232099 (2001-05-01), Chapman et al.
patent: WO 9612027 (1996-04-01), None
patent: WO 9710353 (1997-03-01), None
Chapman, et al., “Potato virus X as a vector for gene expression in plants,”The Plant Journal, 2(4):549-557 (1992).
Cramer,American Journal of Human Genetics, 57(4), 1995, Published for the American of Human Genetic by the University of Chicago Press.
Erickson, et al., “BioSynthesis of the Lysosomal Enzyme Glucocerebrosidase,”Journal of Biological Chemistry, 260(26):14319-14324 (1985).
Ferrari, et al., “Cloning and expression of a soluble sialidase from Chinese hamster ovary cells: sequence alignment similarities to bacterial sialidases,”Clycobiology, 4(3):367-373 (1994).
Furbish, et al., “Enzyme replacement therapy in Gaucher's disease: Large-scale purification of glucocerebrosidase suitable for human administration,”Proc. Natl. Acad. Sci., 71(8) 3560-3563 (1977).
Furbish, et al., “Uptake and Distribution of Placental Glucocerebrosidase in at Hepatic Cells and Effects of Sequential Deglycosylation,”Biochemica et Biophysica Acta. 673:425-434 (1981).
Frank, et al., “Automation of DNA Sequencing Reactions and Related Techniques: A Workstation for Micromanipulation of Liquids,”Biotechnology 6:1211 (1988).
Grace, et al., “Analyses of Catalytic Activity and Inhibitor Binding of Human Acid β-Glucosidase by Site-directed Mutagenesis,”The Journal Biological Chemistry, pp. 6827-6835 (1989).
Grace, et al., Analysis of Human Acid β-Glucosidase by Cite-Directed Mutagenesis and Heterologous Expression,The Journal of Biological Chemistry 269(3):2283-2291 (1994).
Grace and Grabowski, “Human Acid β-Glucosidase: Glycosylation is Required for Catalytic Activity,”Biochemical and Biophysical Research Communications 168(2):771-777 (1990).
Grabowski, et al., “Expression of Functional Human Acid β-Glucosidase in COS-1 andSpordoptera frugiperdaCells,”Enzyme 41:131-142 (1989).
Hopp, et al., “A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification,”Biotechnology 6:1204-1210 (1988).
Iiaskins, et al., Alpha-L-Iduronidase Deficiency in a Cat: A Model of Mucopolysaccharidosis I,Pediat. Res. 13:1294-1297 (1979).
Jonsson, et al., “Biosynthesis and naturation of glucocerebrosidase in Gaucher fibroblasts,”J. Biochem. 104:171-179 (1987).
Kaplan, et al., “Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts,”Proc. Natl. Acad. Sci. USA 74(5):2026-2030 (1977).
Kornfeld and Mellman, “The Biogenesis of Lysosomes,”Annu. Rev. Cell Biol. 5:483-525 (1989).
Miyamura, et al., “A Carboxy-terminal Truncation of Human α-Galactosidase A in a Heterozygous Female with Fabry Disease and Modification of the Enzymatic Activity by the Carboxy-terminal Domain,”J. Clin. Invest., 98(8):1809-1817 (1996).
Murray, “Lectin-Specific Targeting of Lysosomal Enzymes to Reticuloendothelial Cells,”Methods ni Enzymology, 149:25, 39, 41, 42 (1987).
Park, et al., “Structure and nucleotide sequence of tomato HMG2 encoding 3-hydroxy-3-methyl-glutaryl coenzyme A reductase,”Plant Molecular Biology 20:327-331 (1992).
Scott, et al., “Human α-L-iduronidase: cDNA isolation and expression,”Proc. Natl. Acad. Sci. USA, 88:9695-9699 (1991).
Scott, et al., Structure and Sequence of the Human α-L-Iduronidase GeneGenomics 13:1311-1313 (1992).
Schatzle, et al., Molecular Cloning and Characterization of the Structural Gene Coding for the Developmentally Regulated Lysosomal Enzyme, α-Mannosidase, inDictystelium discoideum, The Journal of Biological Chemistry 267(6):4000-4007 (1991).
Shull, et al., “Enzyme replacement in a canine model for Hurler syndrome,”Proc. Natl. Acad. Sci. USA, 91:12917-12941 (1994).
Coppola, et al., “Characterization of glycosylated and catalytically active recombinant human alpha-galactosidase A using a baculovirus vector”,Gene144(2):197-203, 1994.
Murray, et al., “Production of recombinant human glucocerebrosidase in plants”,FASEB J.10(6): A1126, 1996.
Brady, “Fabry Disease”,Peripheral Neropathym, 3rded., 1169-1178 (1993), W.B. Saunders.
Desnick, et al., “α -Galactosidase A Deficiency: Fabry Disease”,The Metabolic Bases of InheritedDiseases, Chapter 89, pp. 2741-2784 (1995), McGraw-Hill.

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