Patent 6924365 Issued on August 2, 2005. Estimated Expiration Date: September 28, 2019. Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.
536/23.1, DNA or RNA fragments or modified forms thereof (e.g., genes, etc.)435/69.1, Recombinant DNA technique included in method of making a protein or polypeptide435/320.1, VECTOR, PER SE (E.G., PLASMID, HYBRID PLASMID, COSMID, VIRAL VECTOR, BACTERIOPHAGE VECTOR, ETC.) BACTERIOPHAGE VECTOR, ETC.)435/325, ANIMAL CELL, PER SE (E.G., CELL LINES, ETC.); COMPOSITION THEREOF; PROCESS OF PROPAGATING, MAINTAINING OR PRESERVING AN ANIMAL CELL OR COMPOSITION THEREOF; PROCESS OF ISOLATING OR SEPARATING AN ANIMAL CELL OR COMPOSITION THEREOF; PROCESS OF PREPARING A COMPOSITION CONTAINING AN ANIMAL CELL; CULTURE MEDIA THEREFORE530/350, PROTEINS, I.E., MORE THAN 100 AMINO ACID RESIDUES530/381, Blood coagulation factors and fibrin, e.g., thromboplastin, etc.435/69.6, Blood proteins536/23.5, Encodes an animal polypeptide514/44Polynucleotide (e.g., RNA, DNA, etc.)
The present invention is directed to a synthetic nucleic acid sequence which encodes a protein wherein at least one non-common codon or less-common codon is replaced by a common codon. The synthetic nucleic acid sequence can include a continuous stretch of at least 90 codons all of which are common codons.
Other References
Grantham et al., Nucleic Acid Research vol. 9, No. 1,(1981) r43-r74.
Peter Lind et al.. “Novel forms of B-domain-deleted recombinant factor VIII molecules Construction and biochemical characterization”, European Journal of Biochemistry, vol. 232, No. 1, pp. 19-27 (Aug. 15, 1995).
Carmel M. Lynch et al, “Sequences in the Coding Region of Clotting Factor VIII Act as Dominant Inhibitors of RNA Accumulation and Protein Production”, Human Gene Therapy, vol. 4, No. 3, pp. 259-272 (Jun. 1, 1993).
Louise C. Wasley et al., “PACE Furin Can Process the Vitamin K-dependent Pro-factor IX Precursor within the Secretory Pathway”, Journal of Biological Chemistry, vol. 268, No. 12, pp. 8458-8465 (Apr. 25, 1993).
Chiu et al., “Engineered GFP as a vital reporter in plants”, Current Biology, vol. 6, No. 3, pp 325-330 (1996).
D'Onofrio et al., “Correlations between the Compositional Properties of Human Genes, Codon Usage, and Amino Acid Composition of Proteins”, Journal of Molecular Evolution, vol. 32, No. 6, pp 504-510 (1991).
Eyre-Walker, “An Analysis of Codon Usage in Mammals: Selection or Mutation Bias?”, Journal of Molecular Evolution, vol. 33, No. 5, pp 442-449 (1991).
Haas et al., “Codon usage limitation in the expression of HIV-1 envelope glycoprotein”, Current Biology, vol. 6, No. 3, pp 315-324 (1996).
Hannig et al., “Strategies for optimizing heterologous protein expression in Escherichia coli”; TIBTECH, vol. 16, pp 54-60 (1998).
Herrick et al., “Identification and Comparison of Stable and Unstable MRNAs in Saccharomyces cerevisiae”, Molecular and Cellular Biology, vol. 10, No. 5, pp 2269-2284 (1990).
Herrick et al., “The Half-Life of c-myc mRNA in Growing and Serum-Stimulated Cells: Influence of the Coding and 3' Untranslated Regions and Role of Ribosome Translocation”, Molecular and Cellular Biology, vol. 14, No. 3, pp 2119-2128 (1994).
Hoekema et al., “Codon Replacement in the PGKI Gene of Saccharomyces cerevisiae: Experimental Approach To Study the Role of Biased Codon Usage in Gene Expression”, Molecular and Cellular Biology, vol. 7, No. 8, pp 2914-2924 (1987).
Hubatsch et al., “Human glutathione transferase A4-4: an Alpha class Enzyme with high catalytic efficiency in the conjunction of 4-hydroxynonenal and other genotoxic products of lipid peroxidation”; Biochem. J., 330, pp 175-179 (1998).
Kim et al., “Codon optimization for high-level expression of human erythropoietin (EPO) in mammalian cells”; GENE, pp 293-301 (1997).
Mehta et al., “Optimization Gene Synthesis, High Level Expression, Isotopic Enrichment, and Refolding of Human Interleukin-5”; Protein Expression and Purification, 11, pp 86-94 (1997).
Parker et al., “Translation and a 42-nucleotide segment within the coding region of the mRNA encoded by the MATα1 gene are involved in promoting rapid mRNA decay in yeast”, Proc. Natl. Acad. Sci. vol. 87, No. 7, pp 2780-2784 (1990).
Solomovici et al., “Does Escherichia coli Optimize the Economics of the Translation Process?”; J. theor. Biol., 185, pp 511-521 (1997).
Wright, “The ‘Effective number of codons’ used in a gene”, Gene, vol. 87, No. 1, pp 23-29 (1990).
Yang et al., “Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein”, Nucleic Acids Research, vol. 24, No. 22, pp 4592-4593 (1996).
Zhang et al., “An Enhanced Green Fluorescent Protein Allows Sensitive Detection of Gene Transfer in Mammalian Cells”, Biochemical and Biophysical Research Communications, vol. 227, No. 3, pp 707-711 (1996).
Zhang et al., “Graphic Analysis of Codon Usage Strategy in 1490 Human Proteins”, Journal of Protein Chemistry, vol. 12, No. 3, pp 329-335 (1993).
Andre et al., “Increased Immune Response Elicited by DNA Vaccination with a Synthetic gp120 Sequence with Optimized Codon Usage”; Journal of Virology, vol. 72, No. 2, pp 1497-1503 (1998).
Berg et al., “Growth Rate-optimized tRNA Abundance and Codon Usage”; J. Mol. Biol., pp 544-550 (1997).
Billinton, et al., “Development of a green fluorescent protein reporter for a yeast genotoxicity biosensor”; Biosensors& Bioelectronics 13 pp 831-838 (1998).