O'Farrell, In re
| Decision Date | 10 August 1988 |
| Docket Number | No. 87-1486,87-1486 |
| Parties | , 7 U.S.P.Q.2d 1673 In re Patrick H. O'FARRELL, Barry A. Polisky and David H. Gelfand. |
| Court | U.S. Court of Appeals — Federal Circuit |
J. Bruce McCubbrey, Fitch, Even, Tabin & Flannery, of San Francisco, Cal., argued for appellant. Virginia H. Meyer, Fitch, Even, Tabin & Flannery, of San Francisco, Cal., was on the brief for appellant.
Harris A. Pitlick, Associate Sol., of Arlington, Va., argued for appellee. With him on the brief were Joseph F. Nakamura, Sol. and Fred E. McKelvey, Deputy Sol.
Before MARKEY, Chief Judge, and RICH and NIES, Circuit Judges.
This appeal is from the decision of the United States Patent and Trademark Office Board of Patent Appeals and Interferences (board) affirming the patent examiner's final rejection of patent application Serial No. 180,424, entitled "Method and Hybrid Vector for Regulating Translation of Heterologous DNA in Bacteria." The application was rejected under 35 U.S.C. Sec. 103 on the ground that the claimed invention would have been obvious at the time the invention was made in view of a published paper by two of the three coinventors, and a publication by Bahl, Marians & Wu, 1 Gene 81 (1976) (Bahl). We affirm.
The claimed invention is from the developing new field of genetic engineering. A broad claim on appeal reads:
Claim 1. A method for producing a predetermined protein in a stable form in a transformed host species of bacteria comprising, providing a cloning vector which includes at least a substantial portion of a gene which is indigenous to the host species of bacteria and is functionally transcribed and translated in that species, said substantial portion of said indigenous gene further including the regulatory DNA sequences for RNA synthesis and protein synthesis but lacking the normal gene termination signal, and linking a natural or synthetic heterologous gene encoding said predetermined protein to said indigenous gene portion at its distal end, said heterologous gene being in proper orientation and having codons arranged in the same reading frame as the codons of said indigenous gene portion so that readthrough can occur from said indigenous gene portion into said heterologous gene in the same reading frame, said heterologous gene portion further containing sufficient DNA sequences to result in expression of a fused protein having sufficient size so as to confer stability on said predetermined protein when said vector is used to transform said host species of bacteria.
Illustrative embodiments are defined in more specific claims. For example:
Claim 2. A method for producing a predetermined protein in a stable form in a transformed host species of bacteria, comprising, providing an E. coli plasmid having an operator, a promoter, a site for the initiation of translation, and at least a substantial portion of the beta-galactosidase gene of the E. coli lactose operon, said substantial portion of said beta-galactosidase gene being under the control of said operator, promoter and site for initiation of translation, said substantial portion of said beta-galactosidase gene lacking the normal gene termination signal, and linking a heterologous gene encoding said predetermined protein to said beta-galactosidase gene portion at its distal end, said heterologous gene being in proper orientation and having codons arranged in the same reading frame as the codons of the said beta-galactosidase gene portion so that readthrough can occur from said beta-galactosidase gene portion into said heterologous gene in the same reading frame, said heterologous gene portion further containing sufficient DNA sequences to result in expression of a fused protein having sufficient size so as to confer stability on said predetermined protein when said vector is used to transform said host species of bacteria.
Claim 3. The method of Claim 2 wherein said E. coli plasmid comprises the plasmid designated pBGP120.
Although the terms in these claims would be familiar to those of ordinary skill in genetic engineering, they employ a bewildering vocabulary new to those who are not versed in molecular biology. An understanding of the science and technology on which these claims are based is essential before one can analyze and explain whether the claimed invention would have been obvious in light of the prior art.
Proteins are biological molecules of enormous importance. Proteins include enzymes that catalyze biochemical reactions, major structural materials of the animal body, and many hormones. Numerous patents and applications for patents in the field of biotechnology involve specific proteins or methods for making and using proteins. Many valuable proteins occur in nature only in minute quantities, or are difficult to purify from natural sources. Therefore, a goal of many biotechnology projects, including appellants' claimed invention, is to devise methods to synthesize useful quantities of specific proteins by controlling the mechanism by which living cells make proteins.
The basic organization of all proteins is the same. Proteins are large polymeric molecules consisting of chains of smaller building blocks, called amino acids, that are linked together covalently. 2 The chemical bonds linking amino acids together are called peptide bonds, so proteins are also called polypeptides. 3 It is the exact sequence in which the amino acids are strung together in a polypeptide chain that determines the identity of a protein and its chemical characteristics. 4 Although there are only 20 amino acids, they are strung together in different orders to produce the hundreds of thousands of proteins found in nature.
To make a protein molecule, a cell needs information about the sequence in which the amino acids must be assembled. The cell uses a long polymeric molecule, DNA (deoxyriboneucleic acid), to store this information. The subunits of the DNA chain are called nucleotides. A nucleotide consists of a nitrogen-containing ring compound (called a base ) linked to a 5-carbon sugar that has a phosphate group attached. 5 DNA is composed of only four nucleotides. They differ from each other in the base region of the molecule. The four bases of these subunits are adenine, guanine, cytosine, and thymine (abbreviated respectively as A, G, C and T). The sequence of these bases along the DNA molecule specifies which amino acids will be inserted in sequence into the polypeptide chain of a protein.
DNA molecules do not participate directly in the synthesis of proteins. DNA acts as a permanent "blueprint" of all of the genetic information in the cell, and exists mainly in extremely long strands (called chromosomes ) containing information coding for the sequences of many proteins, most of which are not being synthesized at any particular moment. The region of DNA on the chromosome that codes for the sequence of a single polypeptide is called a gene. 6 In order to express a gene (the process whereby the information in a gene is used to synthesize new protein), a copy of the gene is first made as a molecule of RNA (ribonucleic acid).
RNA is a molecule that closely resembles DNA. It differs, however, in that it contains a different sugar (ribose instead of deoxyribose) and the base thymine (T) of DNA is replaced in RNA by the structurally similar base, uracil (U). Making an RNA copy of DNA is called transcription. The transcribed RNA copy contains sequences of A, U, C, and G that carry the same information as the sequence of A, T, C, and G in the DNA. That RNA molecule, called messenger RNA, then moves to a location in the cell where proteins are synthesized.
The code whereby a sequence of nucleotides along an RNA molecule is translated into a sequence of amino acids in a protein (i.e., the "genetic code") is based on serially reading groups of three adjacent nucleotides. Each combination of three adjacent nucleotides, called a codon, specifies a particular amino acid. For example, the codon U-G-G in a messenger RNA molecule specifies that there will be a tryptophan molecule in the corresponding location in the corresponding polypeptide. The four bases A, G, C and U can be combined as triplets in 64 different ways, but there are only 20 amino acids to be coded. Thus, most amino acids are coded for by more than one codon. For example, both U-A-U and U-A-C code for tyrosine, and there are six different codons that code for leucine. There are also three codons that do not code for any amino acid (namely, U-A-A, U-G-A, and U-A-G). Like periods at the end of a sentence, these sequences signal the end of the polypeptide chain, and they are therefore called stop codons.
The cellular machinery involved in synthesizing proteins is quite complicated, and centers around large structures called ribosomes that bind to the messenger RNA. The ribosomes and associated molecules "read" the information in the messenger RNA molecule, literally shifting along the strand of RNA three nucleotides at a time, adding the amino acid specified by that codon to a growing polypeptide chain that is also attached to the ribosome. When a stop codon is reached, the polypeptide chain is complete and detaches from the ribosome.
The conversion of the information from a sequence of codons in an RNA molecule into the sequence of amino acids in a newly synthesized polypeptide is called translation. A messenger RNA molecule is typically reused to make many copies of the same protein. Synthesis of a protein is usually terminated by destroying the messenger RNA. (The information for making more of that protein remains stored in DNA in the chromosomes.)
The translation of messenger RNA begins at a specific sequence of nucleotides that bind the RNA to the ribosome and specify which is the first codon that is to be translated. Translation then proceeds by reading nucleotides, three at a time, until a stop codon is reached. If some error...
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