Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Applicant’s amendment filed on 12/18/2023 is acknowledged.
3. Claims 134-153 are pending and under consideration.
4. Applicant’s IDS documents filed on 12/18/2023 and 05/13/2025 have been considered.
5. The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
6. Claims 134-153 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 134-135 recites “a variable heavy chain polypeptide comprising the VH CDR1, VH CDR2 and VH CDR3 of the VH set forth in” and “a variable light chain polypeptide comprising the VL CDR1, VL CDR2 and VL CDR3 of the VL set forth in” and these recitations are indefinite. The claims must recite the CDR sequences themselves.
As evidenced by the art of Dondelinger et al. (PTO-892; Reference U) which teaches that the use of different amino acid numbering schemes currently available in the literature is confusing and might lead to aberrant identification of framework and CDR residues. Therefore, it is of crucial importance to understand the different numbering schemes and, consequently, being able to compare them. There are Kabat, Chothia, Martin, Gelfand, IMGT and Honneger’s numbering schemes as detailed on pages 3-7. Figure 6 teaches the alignment of residue positions of the CDRs within the light and heavy chain variable domains showing the disparity in the CDR definition according to the different numbering schemes.
As such, the residues that constitute the different CDRs can vary depending on which numbering scheme is used. Therefore, one of ordinary skill in the art could not define the metes and bounds of the instant claims and what constitutes infringement because the answer varies depending on which numbering scheme is used. Claims 134-135 are rejected for indefiniteness. Dependent claims 136-153 are included in this rejection as these claims depend from claims 134 and 135.
Correction is required.
7. The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
8. Claims 134-153 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for: the antibodies of SEQ ID NOs 1 and 5; 9 and 13; 17 and 21; 25 and 29; 33 and 37; 41 and 45; 49 and 53; 57 and 61; 65 and 69; 73 and 77; 81 and 85; 89 and 93; 97 and 101; 105 and 109; 113 and 117; 121 and 125; 129 and 133; 137 and 141; 145 and 149; 153 and 157; 161 and 165; 169 and 173; 177 and 181; 185 and 189; 193 and 197; 201 and 205; 209 and 213; 217 and 221; 225 and 229; 233 and 237; 241 and 245; 249 and 253; 257 and 261; 265 and 269; 273 and 277; 281 and 285; 289 and 293; 297 and 301; 305 and 309; 313 and 317; 321 and 325; 329 and 333; 337 and 341; 345 and 349; 353 and 357; 361 and 365; 369 and 373; 377 and 381; 385 and 389; 393 and 397; 401 and 405; 409 and 413; 417 and 421; 425 and 429; 433 and 437; 441 and 445; 449 and 453; 457 and 461 and 465 and 469; and fusion proteins, conjugates pharmaceutical compositions and kits thereof; methods of administering the antibodies; nucleic acids encoding the antibodies, cells comprising the nucleic acids encoding the antibodies, and methods of production of the antibodies, the specification does not reasonably provide enablement for:
A. antibodies competing for binding to the SARS-VCoV-2 antigen with the antibodies of SEQ ID NOs 1 and 5; 9 and 13; 17 and 21; 25 and 29; 33 and 37; 41 and 45; 49 and 53; 57 and 61; 65 and 69; 73 and 77; 81 and 85; 89 and 93; 97 and 101; 105 and 109; 113 and 117; 121 and 125; 129 and 133; 137 and 141; 145 and 149; 153 and 157; 161 and 165; 169 and 173; 177 and 181; 185 and 189; 193 and 197; 201 and 205; 209 and 213; 217 and 221; 225 and 229; 233 and 237; 241 and 245; 249 and 253; 257 and 261; 265 and 269; 273 and 277; 281 and 285; 289 and 293; 297 and 301; 305 and 309; 313 and 317; 321 and 325; 329 and 333; 337 and 341; 345 and 349; 353 and 357; 361 and 365; 369 and 373; 377 and 381; 385 and 389; 393 and 397; 401 and 405; 409 and 413; 417 and 421; 425 and 429; 433 and 437; 441 and 445; 449 and 453; 457 and 461 and 465 and 469; and fusion proteins, conjugates pharmaceutical compositions and kits thereof; methods of administering the antibodies; nucleic acids encoding the antibodies, cells comprising the nucleic acids encoding the antibodies, and methods of production of the antibodies;
B. antibodies competing for binding to the SARS-VCoV-2 antigen with antibodies comprising the CDRs of SEQ ID NOs 1 and 5; 9 and 13; 17 and 21; 25 and 29; 33 and 37; 41 and 45; 49 and 53; 57 and 61; 65 and 69; 73 and 77; 81 and 85; 89 and 93; 97 and 101; 105 and 109; 113 and 117; 121 and 125; 129 and 133; 137 and 141; 145 and 149; 153 and 157; 161 and 165; 169 and 173; 177 and 181; 185 and 189; 193 and 197; 201 and 205; 209 and 213; 217 and 221; 225 and 229; 233 and 237; 241 and 245; 249 and 253; 257 and 261; 265 and 269; 273 and 277; 281 and 285; 289 and 293; 297 and 301; 305 and 309; 313 and 317; 321 and 325; 329 and 333; 337 and 341; 345 and 349; 353 and 357; 361 and 365; 369 and 373; 377 and 381; 385 and 389; 393 and 397; 401 and 405; 409 and 413; 417 and 421; 425 and 429; 433 and 437; 441 and 445; 449 and 453; 457 and 461 and 465 and 469; and fusion proteins, conjugates pharmaceutical compositions and kits thereof; methods of administering the antibodies; nucleic acids encoding the antibodies, cells comprising the nucleic acids encoding the antibodies, and methods of production of the antibodies.
The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and or use the invention commensurate in scope with the claims. The specification disclosure does not enable one skilled in the art to practice the invention without an undue amount of experimentation.
Factors to be considered in determining whether undue experimentation is required to practice the claimed invention are summarized In re Wands (858 F2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)). The factors most relevant to this rejection are the scope of the claim, the amount of direction or guidance provided, the lack of sufficient working examples, the unpredictability in the art and the amount of experimentation required to enable one of skill in the art to practice the claimed invention.
The specification discloses the antibodies of SEQ ID NOs 1 and 5; 9 and 13; 17 and 21; 25 and 29; 33 and 37; 41 and 45; 49 and 53; 57 and 61; 65 and 69; 73 and 77; 81 and 85; 89 and 93; 97 and 101; 105 and 109; 113 and 117; 121 and 125; 129 and 133; 137 and 141; 145 and 149; 153 and 157; 161 and 165; 169 and 173; 177 and 181; 185 and 189; 193 and 197; 201 and 205; 209 and 213; 217 and 221; 225 and 229; 233 and 237; 241 and 245; 249 and 253; 257 and 261; 265 and 269; 273 and 277; 281 and 285; 289 and 293; 297 and 301; 305 and 309; 313 and 317; 321 and 325; 329 and 333; 337 and 341; 345 and 349; 353 and 357; 361 and 365; 369 and 373; 377 and 381; 385 and 389; 393 and 397; 401 and 405; 409 and 413; 417 and 421; 425 and 429; 433 and 437; 441 and 445; 449 and 453; 457 and 461 and 465 and 469; and fusion proteins, conjugates pharmaceutical compositions and kits thereof; methods of administering the antibodies; nucleic acids encoding the antibodies, cells comprising the nucleic acids encoding the antibodies, and methods of production of the antibodies for use in the claimed invention.
The specification is not enabled for making and using an antibody that specifically binds to SARS-COV-2 antigen, wherein the antibody competes for binding to the SARS-COV-2 antigen with an antibody comprising the recited sequences or antibodies comprising the CDRs of the recited sequences.
The specification has not adequately disclosed the genus of these molecules which can be made and used commensurate in scope with the specification including for use in a method of administration to be therapeutically effective in neutralizing the SARS-CoV-2 infection.
The breadth of the instant claims encompasses antibodies with fewer than all six CDRs found in the heavy plus light chain binding region. The specification does not adequately disclose how the skilled artisan would make and use the various antibodies recited in the instant claims.
It is well established in the art that it is highly unpredictable which changes in amino acid sequence can be made in complementarity determining regions (CDRs) of a parental antibody such that the derived antibody retains the binding specificity and affinity of the parent antibody. The art of Mariuzza et al. (PTO-892; Reference V) reviews the structural basis of antigen-antibody recognition and teaches that a naturally occurring antibody comprises light and heavy chains. The antigen-combining site of an antibody is a three-dimensional structure, which fully comprises six "complementarity-determining regions" (CDRs), three each from the light and heavy chains. The amino acid sequences of the CDRs are hypervariable, as the amino acid residues contained within the CDRs determine much of antibody's antigen-binding specificity. Of the amino acid residues of the antibody contacting the antigen, six are within the light chain, nine are within the heavy chain, and two are within the constant or nearly constant "framework" regions (In particular, whole document). As such, one of skill in the art would not be able to make and use the genus of recited antibodies which would retain antigen binding function, because it is the 6 CDRs together which determine the antibody's antigen-binding specificity.
It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function.
Rudikoff et al. (PTO-892; Reference W) teaches that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function (In particular, page 1979, whole document). Rader et al. (PTO-892; Reference X) teaches in vitro selection and evolution of antibodies derived from phage display libraries by pairing either heavy or light chain of the rodent antibody with human polypeptide library for antibody humanization is unpredictable, and certain antibodies cannot be humanized using this approach; and in addition, antibodies consisting of the same heavy chain paired with light chains that differ in light chain CDR3 and elsewhere in VL can obtain undesired feature of binding different epitopes of the same antigen (In particular, discussion on pages 8914-8915, whole document). Accordingly, since it is known in the art that antibodies can comprise the same CDR3 amino acid sequences but not share antigen-binding specificity, it is apparent that one of skill in the art could not be able to make and use the genus of recited antibodies which would retain binding specificity and function. For these reasons, one of skill in the art would not recognize that the specification is not enabled for the use of the genus of the recited antibodies.
The specification provides insufficient direction or guidance regarding how to produce antibodies as broadly defined by the claims other than the recited VH and VL pairs of antibodies. One of ordinary skill in the art would be required to practice undue experimentation to practice the invention commensurate in scope with the claimed.
In view of the quantity of experimentation necessary, the limited working examples, the unpredictability of the art, the lack of sufficient guidance in the specification, and the breadth of the claims, it would take undue trials and errors to make and use the claimed antibodies with less than six CDRs.
The specification does not adequately teach how to effectively treat or reach any therapeutic endpoint in animals by administrating the recited compositions as encompassed by the instant claims. The specification does not teach how to extrapolate data obtained from the disclosed studies to the development of effective in vivo animal therapeutic treatment, commensurate in scope with the claimed invention.
It is not enough to rely on the disclosed studies where, as here, a person having ordinary skill in the art has no basis for perceiving those studies as constituting recognized screening procedures with clear relevance to efficacy in humans or animals (emphasis added). Ex parte Maas, 9 USPQ2d 1746
In view of the absence of a specific and detailed description in Applicant's specification of how to effectively use the genus of methods claimed, absence of working examples providing evidence which is reasonably predictive that the genus of methods that are effective for in vivo treatment of disease, and the lack of predictability in the art at the time the invention was made, an undue amount of experimentation would be required to practice the claimed methods with a reasonable expectation of success.
Substantiating evidence may be in the form of animal tests, which constitute recognizedscreening procedures with clear relevance to efficacy in humans. See Ex parte Krepelka, 231USPQ 746 (Board of Patent Appeals and Interferences 1986) and cases cited therein. Ex parteMaas, 9 USPQ2d 1746.
Reasonable correlation must exist between the scope of the claims and scope of the enablement set forth. In view on the quantity of experimentation necessary the limited working examples, the nature of the invention, the state of the prior art, the unpredictability of the art and the breadth of the claims, it would take undue trials and errors to practice the claimed invention.
9. Claims 134-153 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Applicant is in possession of: the antibodies of SEQ ID NOs 1 and 5; 9 and 13; 17 and 21; 25 and 29; 33 and 37; 41 and 45; 49 and 53; 57 and 61; 65 and 69; 73 and 77; 81 and 85; 89 and 93; 97 and 101; 105 and 109; 113 and 117; 121 and 125; 129 and 133; 137 and 141; 145 and 149; 153 and 157; 161 and 165; 169 and 173; 177 and 181; 185 and 189; 193 and 197; 201 and 205; 209 and 213; 217 and 221; 225 and 229; 233 and 237; 241 and 245; 249 and 253; 257 and 261; 265 and 269; 273 and 277; 281 and 285; 289 and 293; 297 and 301; 305 and 309; 313 and 317; 321 and 325; 329 and 333; 337 and 341; 345 and 349; 353 and 357; 361 and 365; 369 and 373; 377 and 381; 385 and 389; 393 and 397; 401 and 405; 409 and 413; 417 and 421; 425 and 429; 433 and 437; 441 and 445; 449 and 453; 457 and 461 and 465 and 469; and fusion proteins, conjugates pharmaceutical compositions and kits thereof; methods of administering the antibodies; nucleic acids encoding the antibodies, cells comprising the nucleic acids encoding the antibodies, and methods of production of the antibodies
Applicant is not in possession of:
A. antibodies competing for binding to the SARS-VCoV-2 antigen with the antibodies of SEQ ID NOs 1 and 5; 9 and 13; 17 and 21; 25 and 29; 33 and 37; 41 and 45; 49 and 53; 57 and 61; 65 and 69; 73 and 77; 81 and 85; 89 and 93; 97 and 101; 105 and 109; 113 and 117; 121 and 125; 129 and 133; 137 and 141; 145 and 149; 153 and 157; 161 and 165; 169 and 173; 177 and 181; 185 and 189; 193 and 197; 201 and 205; 209 and 213; 217 and 221; 225 and 229; 233 and 237; 241 and 245; 249 and 253; 257 and 261; 265 and 269; 273 and 277; 281 and 285; 289 and 293; 297 and 301; 305 and 309; 313 and 317; 321 and 325; 329 and 333; 337 and 341; 345 and 349; 353 and 357; 361 and 365; 369 and 373; 377 and 381; 385 and 389; 393 and 397; 401 and 405; 409 and 413; 417 and 421; 425 and 429; 433 and 437; 441 and 445; 449 and 453; 457 and 461 and 465 and 469; and fusion proteins, conjugates pharmaceutical compositions and kits thereof; methods of administering the antibodies; nucleic acids encoding the antibodies, cells comprising the nucleic acids encoding the antibodies, and methods of production of the antibodies;
B. antibodies competing for binding to the SARS-VCoV-2 antigen with antibodies comprising the CDRs of SEQ ID NOs 1 and 5; 9 and 13; 17 and 21; 25 and 29; 33 and 37; 41 and 45; 49 and 53; 57 and 61; 65 and 69; 73 and 77; 81 and 85; 89 and 93; 97 and 101; 105 and 109; 113 and 117; 121 and 125; 129 and 133; 137 and 141; 145 and 149; 153 and 157; 161 and 165; 169 and 173; 177 and 181; 185 and 189; 193 and 197; 201 and 205; 209 and 213; 217 and 221; 225 and 229; 233 and 237; 241 and 245; 249 and 253; 257 and 261; 265 and 269; 273 and 277; 281 and 285; 289 and 293; 297 and 301; 305 and 309; 313 and 317; 321 and 325; 329 and 333; 337 and 341; 345 and 349; 353 and 357; 361 and 365; 369 and 373; 377 and 381; 385 and 389; 393 and 397; 401 and 405; 409 and 413; 417 and 421; 425 and 429; 433 and 437; 441 and 445; 449 and 453; 457 and 461 and 465 and 469; and fusion proteins, conjugates pharmaceutical compositions and kits thereof; methods of administering the antibodies; nucleic acids encoding the antibodies, cells comprising the nucleic acids encoding the antibodies, and methods of production of the antibodies.
The specification discloses discloses the antibodies of SEQ ID NOs 1 and 5; 9 and 13; 17 and 21; 25 and 29; 33 and 37; 41 and 45; 49 and 53; 57 and 61; 65 and 69; 73 and 77; 81 and 85; 89 and 93; 97 and 101; 105 and 109; 113 and 117; 121 and 125; 129 and 133; 137 and 141; 145 and 149; 153 and 157; 161 and 165; 169 and 173; 177 and 181; 185 and 189; 193 and 197; 201 and 205; 209 and 213; 217 and 221; 225 and 229; 233 and 237; 241 and 245; 249 and 253; 257 and 261; 265 and 269; 273 and 277; 281 and 285; 289 and 293; 297 and 301; 305 and 309; 313 and 317; 321 and 325; 329 and 333; 337 and 341; 345 and 349; 353 and 357; 361 and 365; 369 and 373; 377 and 381; 385 and 389; 393 and 397; 401 and 405; 409 and 413; 417 and 421; 425 and 429; 433 and 437; 441 and 445; 449 and 453; 457 and 461 and 465 and 469; and fusion proteins, conjugates pharmaceutical compositions and kits thereof; methods of administering the antibodies; nucleic acids encoding the antibodies, cells comprising the nucleic acids encoding the antibodies, and methods of production of the antibodies for use in the claimed invention.
The specification has not adequately described antibodies which compete for binding with the recited antibodies wherein there is no structure for the competing antibodies themselves recited.
Therefore, the skilled artisan cannot envision all the antibody and method possibilities recited in the instant claims.
Consequently, conception cannot be achieved until a representative description of the structural and functional properties of the claimed invention has occurred, regardless of the complexity or simplicity of the method.
As evidenced by the art of Goel et al. (PTO-892; Page 2; Reference U), Khan et al. (PTO-892; Page 2; Reference V) and Poosarla et al. (PTO-892; Page 2; Reference W), antibody specificity for a particular antigen does not correlate with any particular structure for the antibodies themselves. It was well known to those skilled in the art at the time the invention was made that minor structural differences among structurally related antibodies or compositions thereof could result in substantially different binding activities. Given the lack of guidance in the specification, it is unpredictable which antibodies with which structures would bind to the recited sequences. The specification does not disclose a correlation between the structure of the antibodies themselves and their function of binding to the recited sequences and competing for binding with the recited antibodies such that a skilled artisan would have known what antibody structures possess the claimed functions.
U.S. Court of Appeals for the Federal Circuit recently decided Amgen v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017) which concerned adequate written description for claims drawn to antibodies. The Federal Circuit explained in Amgen that when an antibody is claimed,
35 U.S.C. § 112(a) requires adequate written description of the antibody itself. Amgen, 872 F.3d at 1378-79. The Amgen court expressly stated that the so-called "newly characterized antigen" test, which had been based on an example in USPTO-issued training materials and was noted in dicta in several earlier Federal Circuit decisions, should not be used in determining whether there is adequate written description under 35 U.S.C. § 112(a) for a claim drawn to an antibody. Citing its decision in Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co. , the court also stressed that the "newly characterized antigen" test could not stand because it contradicted the quid pro quo of the patent system whereby one must describe an invention in order to obtain a patent. Amgen, 872
F.3d at 1378-79, quoting Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1345
(Fed. Cir. 2010). In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional. Id.
The specification does not provide adequate written description of the claimed invention.
The legal standard for sufficiency of a patent's (or a specification's) written description is
whether that description "reasonably conveys to the artisan that the inventor had possession at
that time of the. . .claimed subject matter", Vas-Cath, Inc. V. Mahurkar, 19 U.S.P.Q.2d 1111
(Fed. Cir. 1991). In the instant case, the specification does not convey to the artisan that the
applicant had possession at the time of invention of the claimed inventions.
The claims encompass antibodies without any structure and numerous functions. The claims are not limited to the antibodies that were actually produced in the examples in the specification which actually bind to SARS-CoV-2 antigen .
It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in
order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites.
MacCallum, et al. (PTO-892; Page 2; Reference X) analyzed many different antibodies for interactions with antigen and state that although CDR3 of the heavy and light chain dominate, a number of residues outside the standard CDR definitions make antigen contacts (see page 733, right column) and non-contacting residues within the CDRs coincide with residues as important in defining canonical backbone conformations (see page 735, left column). De Pascalis, et al. (PTO-892; Page 3; Reference U) demonstrates that grafting of the CDRs into a human framework was performed by grafting CDR residues and maintaining framework residues that were deemed essential for preserving the structural integrity of the antigen binding site (see page 3079, right column). Although abbreviated CDR residues were used in the constructs, some residues in all 6 CDRs were used for the constructs (see page 3080, left column). Thus it is unpredictable as to what antibodies other than the original antibodies disclosed in the specification wherein the antibodies would still function. Thus, the skilled artisan cannot envision the detailed structure of the encompassed invention and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation.
Adequate written description requires more than a mere statement that it is part of the invention and a reference to a potential method of isolating it. In the instant application, the amino acid sequence itself or isolated protein is required. See Fiers v. Revel, 25 USPQ 2d 1601 at 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Lts., 18 USPQ2d 1016. In view of the aforementioned problems regarding description of the claimed invention, the specification does not provide an adequate written description of the invention claimed herein.
See The Regents of the University of California v. Eli Lilly and Company, 43 USPQ2d 1398,
1404-7 (Fed. Cir. 1997). In University of California v. Eli Lilly and Co., 39 U.S.P.Q.2d 1225
(Fed. Cir. 1995) the inventors claimed a genus of DNA species encoding insulin in different vertebrates or mammals, but had only described a single species of cDNA which encoded rat insulin. The court held that only the nucleic acids species described in the specification (i.e. nucleic acids encoding rat insulin) met the description requirement and that the inventors were not entitled to a claim encompassing a genus of nucleic acids encoding insulin from other vertebrates, mammals or humans, id. at 1240. The Federal Circuit has held that if an inventor is "unable to envision the detailed constitution of a gene so as to distinguish it from other materials.
. .conception has not been achieved until reduction to practice has occurred", Amgen, Inc. v.
Chugai Pharmaceutical Co, Ltd., 18 U.S.P.Q.2d 016 (Fed. Cir. 1991). Attention is also directed
to the decision of The Regents of the University of California v. Eli Lilly and Company (CAFC,
July 1997) wherein is stated: "The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 222 USPQ 369, 372-373 (Fed. Cir. 1984) (affirming rejection because the specification does "little more than outlin[e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate.").
Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material. Thus, as we have previously held, a cDNA is not defined or described by the mere name "cDNA," even if accompanied by the name of the protein that it encodes, but requires a kind of specificity usually achieved by means of the recitation of the sequence of nucleotides that make up the cDNA." See Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606.
As such, there is insufficient written description of the required kind of structure identifying information about the corresponding makeup of the claimed antagonists and antibodies to demonstrate possession.
10. No claim is allowed.
11. Any inquiry concerning this communication or earlier communications from the examiner should be directed to NORA MAUREEN ROONEY whose telephone number is (571)272-9937. The examiner can normally be reached on M-F from 8:00am to 4:30pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner' s supervisor, Misook Yu, can be reached at telephone number (571) 272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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November 15, 2025
/Nora M Rooney/
Primary Examiner, Art Unit 1641