DETAILED ACTION
NOTE: The examiner for this application has changed. The new examiner is Sean Aeder.
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 .
Election/Restriction
The response filed on 2/4/26 to the restriction requirement of 12/3/25 has been received. Applicant has elected Group I, and the following species:
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Because Applicant did not distinctly and specifically point out any errors in the restriction requirement, the election has been treated as an election without traverse (MPEP 818.03(a)).
Claims 1-8, 10-12, 15, 17, 19, 22-25, 27, 31, 32, and 36 are pending.
Claims 6 and 8 are withdrawn from further consideration by the examiner under 37 CFR 1.142(b) as being drawn to a non-elected invention.
Groups II-III have been rejoined with elected group I.
Claims 1-5, 7, 10-12, 17, 19, 22-25, 27, 31, 32, and 36 are currently under consideration.
Claim Rejections - 35 USC § 112
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.
Claims 4, 5, and 7 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 4, 5, and 7 are rejected because claim 4 recites “…constant regions (Ig Fc e.g., Ig CH2-CH3)….” The metes-and-bounds of the claims are unclear because it is unclear how, or if, “”(Ig Fc e.g., Ig CH2-CH3)” limits the claims.
Claim Rejections - 35 USC § 112
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.
Claims 1-5, 7, 10-12, 17, 19, 22-25, 27, 31, 32, and 36 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. In the instant case, the claims are inclusive of a genus of reversibly masked MODs comprising (i) a TGF-b polypeptide sequence and (ii) a TGF-b receptor polypeptide sequence that reversibly binds and masks the TGF-b polypeptide sequence. However, the written description in this case only sets forth reversibly masked MODs encompassed by the claims comprising (1) a reversibly masked MOD comprising (i) a TGF-b2 polypeptide comprising SEQ ID NO:103 except for a substitution at one or more of Lys 25, Ile 92, and/or Lys 94 and (ii) a TbRII polypeptide comprising SEQ ID NO: 108; (2) a reversibly masked MOD comprising (i) a TGF-b1 polypeptide comprising SEQ ID NO:102 except for a substitution at one or more of Arg 25, Val 92, and/or Arg 94 and (ii) a TbRI polypeptide comprising SEQ ID NO: 107; and (3) a reversibly masked MOD comprising (i) a TGF-b3 polypeptide comprising SEQ ID NO:106 except for a substitution at one or more of Arg 25, Val 92, and/or Arg 94 and (ii) a TbRIII polypeptide comprising SEQ ID NO: 218 or 219 ([0224] on page 56 to [0238] on page 61, in particular). The specification does not disclose, and the art does not teach, the genus as broadly encompassed in the claims.
The written description only reasonably conveys the following reversibly masked MODs comprising (i) a TGF-b polypeptide sequence and (ii) a TGF-b receptor polypeptide sequence that reversibly binds and masks the TGF-b polypeptide sequence wherein the reversibly masked MODs comprise:
(1) a reversibly masked MOD comprising (i) a TGF-b2 polypeptide comprising SEQ ID NO:103 except for a substitution at one or more of Lys 25, Ile 92, and/or Lys 94 and (ii) a TbRII polypeptide comprising SEQ ID NO: 108;
(2) a reversibly masked MOD comprising (i) a TGF-b1 polypeptide comprising SEQ ID NO:102 except for a substitution at one or more of Arg 25, Val 92, and/or Arg 94 and (ii) a TbRI polypeptide comprising SEQ ID NO: 107; and/or
(3) a reversibly masked MOD comprising (i) a TGF-b3 polypeptide comprising SEQ ID NO:106 except for a substitution at one or more of Arg 25, Val 92, and/or Arg 94 and (ii) a TbRIII polypeptide comprising SEQ ID NO: 218 or 219 ([0224] on page 56 to [0238] on page 61, in particular).
While one could screen for possible other members of the genus of MODs comprising (i) a TGF-b polypeptide sequence and (ii) a TGF-b receptor polypeptide sequence that reversibly binds and masks the TGF-b polypeptide sequence, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. MODs encompassed by the claims could possibly have mutations in the TGF-b polypeptide sequences and/or TGF-b receptor polypeptide sequences other than those mentioned above. However, other than the residues mentioned above, it is unclear which possible mutations of the polypeptide sequences would (or would not) result in reversibly masked MODs. Those of skill in the art recognize that protein chemistry is probably one of the most unpredictable areas of biotechnology. For example, Burgess et al. (J. Cell Biol. 111:2129-2138, 1990) shows that a conservative replacement of a single “lysine” residue at position 118 of acidic fibroblast growth factor by “glutamic acid” led to a substantial loss of heparin binding, receptor binding and biological activity of the protein. Similarly, Lazar et al. ( Mol. Cell Biol. 8:1247-1252, 1998) teach that in transforming growth factor alpha, replacement of aspartic acid at position 47 alone with alanine or asparagines did not affect biological activity while replacement with serine or glutamic acid sharply reduced the biological activity of the mitogen. These references demonstrate that even a single amino acid substitution or what appears to be an inconsequential chemical modification will often dramatically affect the biological activity and characteristics of a protein.
A description of a genus may be achieved by means of a recitation of a representative number of species falling within the scope of the genus or by describing structural features common to that genus that “constitute a substantial portion of the genus.” See University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568, 43 USPQ2d 1398, 1406 (Fed. Cir. 1997): “A description of a genus of cDNAs may be achieved by means of a recitation of a representative number of cDNA, defined by nucleotide sequence, falling within the scope of the genus or of a recitation of structural features common to the members of the genus, which features constitute a substantial portion of the genus.”
The inventions at issue in Lilly were DNA constructs per se, the holdings of that case is also applicable to claims such as those at issue here. In regards to claims to a product defined by function, without a correlation between structure and function, the claim does little more than define the claimed invention by function. That is not sufficient to satisfy the written description requirement. See Eli Lilly, 119 at1568 USPQ2d at 1406 (“definition by function…does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is”).
The instant specification fails to provide sufficient descriptive information, such as definitive structural features that are common to the genus. That is, the specification provides neither a representative number of MODs that encompass the genus nor does it provide a description of structural features that are common to the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus. “[A] sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Ariad, 598 F.3d at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). A “representative number of species” means that those species that are adequately described are representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (“The ’128 and ’485 patents, however, only describe species of structurally similar antibodies that were derived from Joe-9. Although the number of the described species appears high quantitatively, the described species are all of the similar type and do not qualitatively represent other types of antibodies encompassed by the genus.”). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species.
The functional requirement of the claimed MODs is the sort of wish list of properties which fails to satisfy the written description requirement because MODs those properties have not been adequately described. See Centocor, 636 F.3d at 1352. The “claims merely recite a description of the problem to be solved while claiming all solutions to it and . . . cover any compound later actually invented and determined to fall within the claim’s functional boundaries— leaving it to the pharmaceutical industry to complete an unfinished invention.”Ariad Pharmaceuticals, Inc. v. EliLilly and Co.,598 F.3d 1336, 1353 (Fed. Cir. 2010).
Since the disclosure fails to describe common attributes or characteristics that adequately identify members of the genus, and because the genus is highly variant, the disclosure is insufficient to describe the genus. Thus, one of skill in the art would reasonably conclude that the disclosure fails to provide a representative number of species to describe the genus as broadly claimed.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116). As discussed above, even though Applicant may propose methods of screening for possible members of the genus, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus, 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 reference to a potential method of isolation. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. See Ariad, 94 USPQ2d at 1161; Centocor at 1876 (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”)
One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483. In Fiddes, claims directed to mammalian FGF’s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115).
Claim Rejections - 35 USC § 112
Claims 1-5, 7, 10-12, 17, 19, 22-25, 27, 31, 32, and 36 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 making, therapeutically administering, and contacting cells with TMAPP-epitope conjugates encompassed by the claims wherein the reversibly masked MODs of the conjugates comprise (1) a reversibly masked MOD comprising (i) a TGF-b2 polypeptide comprising SEQ ID NO:103 except for a substitution at one or more of Lys 25, Ile 92, and/or Lys 94 and (ii) a TbRII polypeptide comprising SEQ ID NO: 108; (2) a reversibly masked MOD comprising (i) a TGF-b1 polypeptide comprising SEQ ID NO:102 except for a substitution at one or more of Arg 25, Val 92, and/or Arg 94 and (ii) a TbRI polypeptide comprising SEQ ID NO: 107; and/or (3) a reversibly masked MOD comprising (i) a TGF-b3 polypeptide comprising SEQ ID NO:106 except for a substitution at one or more of Arg 25, Val 92, and/or Arg 94 and (ii) a TbRIII polypeptide comprising SEQ ID NO: 218 or 219 (see [0224] on page 56 to [0238] on page 61, in particular), does not reasonably provide enablement for making, therapeutically or prophylactically administering, and contacting cells with TMAPP-epitope conjugates encompassed by the claims wherein the reversibly masked MODs of the conjugates comprise just any reversibly masked TGF-b MOD comprising (i) a TGF-b polypeptide sequence and (ii) a TGF-b receptor polypeptide sequence that reversibly binds and masks the TGF-b polypeptide sequence. 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 use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are summarized in Ex parte Forman, 230 USPQ 546 (BPAI 1986). They include the nature of the invention, the state of the prior art, the relative skill of those in the art, the amount of direction or guidance disclosed in the specification, the presence or absence of working examples, the predictability or unpredictability of the art, the breadth of the claims, and the quantity of experimentation which would be required in order to practice the invention as claimed.
The instant claims are drawn to TMAPP-epitope conjugates, method of therapeutically or prophylactically administering the TMSAPP-epitope conjugates, and methods of contacting cells with the TMAPP-epitope conjugates, wherein the TMAPP-epitope conjugates comprise reversibly masked MODs comprising (i) a TGF-b polypeptide sequence and (ii) a TGF-b receptor polypeptide sequence that reversibly binds and masks the TGF-b polypeptide sequence. This includes (a) a genus of reversibly masked MODs that are not adequately described and (b) a highly-unpredictable prophylactic treatment method that has not been demonstrated.
This invention is in a class of invention which the CAFC has characterized as "the unpredictable arts such as chemistry and biology". Mycogen Plant Sci., Inc. v. Monsanto Co., 243 F.3d 1316, 1330 (Fed. Cir. 2001).
The specification discloses TMAPP-epitope conjugates encompassed by the claims wherein the reversibly masked MODs of the conjugates comprise (1) a reversibly masked MOD comprising (i) a TGF-b2 polypeptide comprising SEQ ID NO:103 except for a substitution at one or more of Lys 25, Ile 92, and/or Lys 94 and (ii) a TbRII polypeptide comprising SEQ ID NO: 108; (2) a reversibly masked MOD comprising (i) a TGF-b1 polypeptide comprising SEQ ID NO:102 except for a substitution at one or more of Arg 25, Val 92, and/or Arg 94 and (ii) a TbRI polypeptide comprising SEQ ID NO: 107; and/or (3) a reversibly masked MOD comprising (i) a TGF-b3 polypeptide comprising SEQ ID NO:106 except for a substitution at one or more of Arg 25, Val 92, and/or Arg 94 and (ii) a TbRIII polypeptide comprising SEQ ID NO: 218 or 219 (see [0224] on page 56 to [0238] on page 61, in particular). One of skill in the art could readily envision therapeutically administering and/or contacting cells with such conjugates. However, the specification in view of the art does not adequately describe the reversibly masked MODs encompassed by the claims. Further, the specification does not demonstrate the highly unpredictable prophylactic methods recited by claim 32.
Reasonable guidance with respect to preventing any disorder relies on quantitative analysis from defined populations which have been successfully pre-screened and are predisposed to the disorder. This type of data might be derived from widespread genetic analysis, cancer clusters, or family histories. The essential element towards the validation of a preventive therapeutic is the ability to test the drug on subjects monitored in advance of clinical disease and link those results with subsequent histological confirmation of the presence or absence of disease. This irrefutable link between antecedent drug and subsequent knowledge of the prevention of the disease is the essence of a valid preventive agent.
One cannot extrapolate the teachings of the specification to the scope of the claims because the claims are broadly drawn to TMAPP-epitope conjugates, method of therapeutically or prophylactically administering the TMSAPP-epitope conjugates, and methods of contacting cells with the TMAPP-epitope conjugates, wherein the TMAPP-epitope conjugates comprise reversibly masked MODs comprising (i) a TGF-b polypeptide sequence and (ii) a TGF-b receptor polypeptide sequence that reversibly binds and masks the TGF-b polypeptide sequence, and Applicant has not enabled the claims because (i) undue and unreasonable experimentation would be required to identify the genus of MODs of the TMAPP-epitope conjugates encompassed by the claims and (ii) undue and unreasonable experimentation would be require to determine which, if any, TMAPP-epitope conjugates encompassed by the claims give rise to prophylaxis.
Further, similar to claims at issue in Amgen Inc. v Sanofi, the instant specification does not enable the full scope of the claims. The instant specification, in view of the prior art, does not teach one of skill the recited genus of MODs of the TMAPP-epitope conjugates encompassed by the claims.
In view of the teachings above and the lack of guidance, workable examples and or exemplification in the specification, it would require undue experimentation by one of skill in the art to determine with any predictability, that the method would function as claimed.
Prior art of Interest
The closest prior art to the instant claims is Seidel et al (WO 2017/151818 A2; 9/8/17; 5/16/25 IDS). Seidel et al teaches T-cell modulatory multimeric polypeptides for modulating the activity of T-cells upon contacting the T-cells ([0003],in particular). Seidel et al further teaches a multimeric polypeptide comprising a) a first polypeptide comprising, from N’ to C’: i) an epitope; ii) a presenting complex sequence comprising a first MHC polypeptide; and b) a second polypeptide comprising, from N’ to C’: i) a presenting complex sequence comprising a second MHC polypeptide; and ii) optionally an Ig Fc polypeptide or a non-Ig scaffold, wherein the multimeric polypeptide comprises one or more immunostimulatory domains at the N-terminus and/or C-terminus of the first and/or second polypeptides ([0005], in particular). Seidel et al further teaches the multimeric polypeptide wherein the first and second MHC polypeptides are linked via disulfide linkage ([0006], in particular). Seidel et al further teaches the multimeric polypeptide wherein the epitope is a T cell epitope (line 5 on page 4, in particular), which renders the multimeric polypeptide a T-cell modulatory antigen-presenting polypeptide (TMAPP). Seidel et al further teaches the epitope can be attached to the presenting sequence of the first polypeptide via a linker ([00116], in particular) and that a linker in the first polypeptide can include a cysteine residue that forms a disulfide bond (“chemical conjugation”) with a cysteine residue present in a second polypeptide ([00119], in particular). Seidel et al further teaches the multimeric polypeptide wherein one of the MHC polypeptides is an MHC class II alpha (note: MHC class II alpha polypeptides comprise a1 and a2 domains) polypeptide and the other MHC polypeptide is an MHC class II beta (note: MHC class II beta polypeptides comprise b1 and b2 domains) polypeptide (lines 3-5 on page 4, in particular). Seidel et al further teaches the one or more immunostimulatory domains of the multimeric polypeptide is a T cell modulatory domain (MOD) that can be a cytokine, PD-L1, and/or 4-1BBL ([00187]-[00188], in particular). Seidel et al further teaches the multimeric polypeptide as part of a duplex where a first multimeric polypeptide and a second multimeric polypeptide can form a duplex comprising a homo-dimer or a hetero-dimer by linking Fc domains ([00114], in particular). However, Seidel et al does not specifically teach the multimeric polypeptide comprising both (i) an immunostimulatory domain that is a TGF-b sequence that reversibly masked by a TGF-b receptor sequence and (ii) an epitope of the multimeric polypeptide of Seidel et al that is a Type 1 Diabetes (T1D)-associated epitope. Further, the prior art does not adequately describe immunostimulatory domains that are TGF-b sequences that are reversibly masked by TGF-b receptor sequences (see above rejections under 35 U.S.C. 112(a)).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-5, 7, 10-12, 17, 19, 22-25, 31, 32, and 36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 and 19 of copending Application No. 18/287754 in view of Seidel et al (WO 2017/151818 A2; 9/8/17; 5/16/25 IDS). The patent claims differ from the instant claims in that the patent claims specify that the T1D peptide epitope is chemically conjugated to the multimeric antigen-presenting polypeptide. However, it would have been obvious to chemically conjugate the T1D peptide epitope of the copending claims to the MHC sequences of the multimeric antigen-presenting polypeptide of the copending claims by because Seidel et al teaches a peptide epitope can be attached to an MHC presenting sequence of a multimeric antigen-presenting polypeptide via a linker ([00116], in particular) and that the linker can include a cysteine residue that forms a disulfide bond (“chemical conjugation”) with a cysteine residue present in a second polypeptide ([00119], in particular) – which can be the T1D peptide epitope, and chemically conjugating the T1D peptide epitope to the MHC sequences of the multimeric antigen-presenting polypeptide of the copending claims would maintain association of the peptide antigen with the multimeric antigen-presenting polypeptide for in vivo administration.
This is a provisional nonstatutory double patenting rejection.
Conclusion
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/SEAN E AEDER/ Primary Examiner, Art Unit 1642
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