DETAILED ACTION
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 .
Applicant’s amendment, filed on 6/28/2023, is acknowledged.
Claims 1-20 are currently pending.
Claim 1 is the only independent claim.
Election/Restrictions
Applicant’s election: 1) of the anti-survivin antibody with the HCDR1-3 and LCDR1-3 of SEQ ID NO: 7, 8, 9, 10, 11, 12, respectively and a VH and VL of SEQ ID NO: 19 and 20, respectively 2) a human antibody; 3) IgG2b subtype; 4) Myasthenia Gravis, respectively in the reply filed on 4/16/2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
After consideration, the search and examination has been extended to cover all of the antibody types recited in instant claim 5.
Claims 10 (unelected VH/VL), 12-17 (unelected diseases), and 20 (unelected VH/VL) are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions.
Claims 1-9, 11, 18, and 19 are under examination as reading on a method of treating a survivin-positive autoimmune disease comprising administration of an anti-survivin antibody with the HCDR1-3 and LCDR1-3 of SEQ ID NO: 7, 8, 9, 10, 11, 12, respectively.
Priority
Applicant’s claim for the benefit of a prior-filed U.S. provisional patent application no.
63/132,964, filed December 31, 2020, is acknowledged.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 6/28/2026 and 11/26/2024 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner in their entireties.
Specification
The use of the terms:
Vacutainer™ (¶[0115]);
Leucosep™ (¶[0115]);
Nunc-immuno™ (¶[0128]);
Microwell™ (¶[0128];
Varioskan™ (¶[0128]);
SUPERFROST® (¶[0130]); and
Fluoromount-G™ (¶[0130])
which are trade names or marks used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Claim Objections
Claims 1 is objected to because the claim recites “[a] method of treating survivin-positive autoimmune disease…” and should most likely recite “..method of treating a surviving-positive autoimmune disease…” to correct a minor typographical error.
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.
Claim 1-7 and 11 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 methods of treating survivin-positive autoimmune diseases comprising administration of the anti-survivin antibody structures of the clones 2C2E7 and 30H3D2, does not reasonably provide enablement for methods of treating survivin-positive autoimmune diseases comprising administration of a broad genus of antibody structures with no recited structure and the function “specific for survivin”. 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 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.
Breadth of claims and nature of invention:
Claims 1-7 and 11-17 encompass a broad genus of methods of treating surviving-positive autoimmune diseases comprising administration of an anti-survivin antibody with no recited structure with the function of “specific for survivin” (claims 1, 4-7, and 11-17), or that has been generated in response to the sequences in either claims 2 or 3 with the function of “specific for surviving”.
The specification discloses the use of anti-survivin antibodies for the treatment of Myasthenia gravis (Example 1).
Amount of direction and existence of working examples:
Two examples of anti-survivin antibody structures are disclosed, which are the anti-survivin monoclonal antibody clones 2C2E7 and 30H3D2 (¶[0110]).
The specification further discloses PBMCs isolated from patients with MG had a higher surface expression of survivin compared to healthy donors (¶[0135] and Fig. 1). Treatment with 2C2E7 protected mice from experimental autoimmune MG, as the mice maintained grip strength and had lower disease scores when compared to vehicle treated controls (¶[0136], Fig. 2), and reduced survivin expression in B cells during EAMG (¶[0137]-[0141], Fig. 3).
Level of predictability, state of prior art, and quantity of experimentation needed:
The claims are directed to methods of treating survivin-positive autoimmune diseases comprising administration of a broad class of antibodies with no recited structure, all with the function of “specific for survivin”, which includes broad genera of millions to billions of different antibody structures with the recited function.
However, the specification did not give the skilled in the art enough information to choose candidate antigen binding structures from the vast number of options of millions of candidates, and therefore required scientists to engage in a great deal of experimentation and failure. “That is not enablement”—it is a “hunting license.”
The specification discloses two different anti-survivin antibodies, 2C2E7 and 30H3D2. These two antibody clones have specific structures defined by their amino acid sequences, especially in the CDR regions that are critical for antigen binding.
In Amgen Inc. et al. v. Sanofi et al., 598 U.S. 594, 2023 USPQ2d 602 (2023), the Supreme Court held that claims drawn to a genus of monoclonal antibodies, which were functionally claimed by their ability to bind to a specific protein, PCSK9, were invalid due to lack of enablement. The claims at issue were functional, in that they defined the genus by its function (the ability to bind to specific residues of PCSK9) as opposed to reciting a specific structure (the amino acid sequence of the antibodies in the genus). The Supreme Court concluded that the patents at issue failed to adequately enable the full scope of the genus of antibodies that performed the function of binding to specific amino acid residues on PCSK9 and blocking the binding of PCSK9 to a particular cholesterol receptor, LDLR. This decision reaffirmed the prior decision made by the Federal District Court in Amgen Inc. v. Sanofi, Aventisub LLC., 987 F.3d 1080 (Fed. Cir. 2021).
The Court clarified that the specification does not always need to "describe with particularity how to make and use every single embodiment within a claimed class." Id. at 610-11. However, "[i]f a patent claims an entire class of processes, machines, manufactures, or compositions of matter, the patent’s specification must enable a person skilled in the art to make and use the entire class….The more one claims, the more one must enable." Id.
The specification may require a reasonable amount of experimentation to make and use the invention and what is reasonable will depend on the nature of the invention and the underlying art. For example, "it may suffice to give an example (or a few examples) if the specification also discloses some general quality … running through the class that gives it a peculiar fitness for the particular purpose" and "disclosing that general quality may reliably enable a person skilled in the art to make and use all of what is claimed, not merely a subset." Id. at 611 (internal quotations omitted). However, the Supreme Court found that Amgen failed to enable all that it claimed, even if allowing for a reasonable degree of experimentation. Id. at 613; see also Baxalta Inc. v Genentech, Inc., 81 F.4th 1362, 1367, 2023 USPQ2d 1103 (Fed. Cir. 2023) ("[t]he facts of this case are more analogous to—and are, in fact, indistinguishable from—those in Amgen. We do not interpret Amgen to have disturbed our prior enablement case law, including Wands and its factors."). Moreover, "[w]e see no meaningful difference between Wands' ‘undue experimentation’ and Amgen's ‘[un]reasonable experimentation’ standards. Id. at footnote 4. See also Guidelines for Assessing Enablement in Utility Applications and Patents in View of the Supreme Court Decision in Amgen Inc. et al. v. Sanofi et al., 89 FR 1563 (January 10, 2024), which explains that regardless of the technology the Wands factors should be used when assessing enablement.
However, while the specification in Amgen identified 26 exemplary antibodies that performed the claimed function by their amino acid sequences, the claims at issue were directed to a class which included "a ‘vast’ number of additional antibodies" that Amgen had not described by their amino acid sequences. Id. at 613. The Court found that Amgen sought to monopolize an entire class by their function, even though that class was much broader than the 26 exemplary antibodies disclosed by their amino acid structure. Id. at 613.
In Amgen Inc. v. Sanofi, Aventisub LLC, 987 F.3d 1080 (Fed. Cir. 2021), which the Supreme Court affirmed, the Federal Circuit explicitly applied the Wands factors to assess whether the specification of Amgen’s patent provided sufficient enablement, for purposes of 35 U.S.C. 112(a), to make and use the full scope of the claimed invention. The court relied on evidence showing that the scope of the claims encompassed millions of antibodies and that it was necessary to screen each candidate antibody in order to determine whether it met the functional limitations of the claim. Id. at 1088. Consequently, the Federal Circuit concluded that there was a lack of enablement. See also the following cases across various technology areas: McRO, Inc. v. Bandai Namco Games Am. Inc., 959 F.3d 1091, 2020 USPQ2d 10550 (Fed. Cir. 2020); Wyeth & Cordis Corp. v. Abbott Laboratories, 720 F.3d 1380, 107 USPQ2d 1273 (Fed. Cir. 2013); Enzo Life Sciences, Inc. v. Roche Molecular Systems, Inc., 928 F.3d 1340 (Fed. Cir. 2019); and Idenix Pharmaceuticals LLC v. Gilead Sciences Inc., 941 F.3d 1149, 2019 USPQ2d 415844 (Fed. Cir. 2019).
Amgen attempted to claim an entire class of compounds by their function, namely antibodies that bind to the “sweet spot” of PCSK9 thereby inhibiting it from binding to LDL, while only describing 26 amino acid sequences in its specification. The two processes, the “roadmap” and “conservative substitution” did not save Amgen. According to the Court, these amounted to “little more than two research assignments” which forced scientists to conduct “painstaking experimentation” to see what worked. (citing Incandescent Lamp). The Court therefore held that Amgen’s specification did not enable the claims.
This case is akin to the issue in Amgen Inc. v. Sanofi, Aventisub LLC, in which the court relied on evidence showing that the scope of the claims encompassed millions of antibodies and that it was necessary to screen each candidate antibody in order to determine whether it met the functional limitations of the claim. Sanofi-Aventisub at 1088. Consequently, the Federal Circuit concluded that there was a lack of enablement. While the specification in Amgen identified 26 exemplary antibodies that performed the claimed function by their amino acid sequences, the claims at issue were directed to a class that included “a ‘vast' number of additional antibodies” that Amgen had not described by their amino acid sequences. Id. at 1256. The Supreme Court found that Amgen sought to monopolize an entire class of antibodies by their function, which was much broader than the 26 exemplary antibodies disclosed by their amino acid structure.
In the instant case, the claims are directed to a broad class of antibodies that are functionally claimed to bind to survivin (claims 1, 4-7, and 11-17), or specific amino acid sequences on the survivin protein (claims 2 and 3) with no recited structure.
The instant claims are directed to classes of polypeptides that include “a ‘vast’ number” of additional antibody structures (i.e., amino acid sequences of all of the CDR regions that are necessary for antigen binding) in which the instant specification fails to describe. It would be necessary to first generate and then screen each candidate agent to determine whether or not it met the function limitations of “specific for survivin”. The Federal Circuit concluded that there was a lack of enablement, which was affirmed by the Supreme Court in Amgen.
The instant specification does not disclose any common structural feature delineating which other polypeptide structures would have the function of “specific for survivin”. The only structure-function relationship guidance the specification provides is to disclose individual examples of anti-survivin antibody structures with these functions.
The instant claims simply direct skilled artisans to engage in the same iterative, trial-and-error process the inventors followed to discover the antibody structures they elected to disclose and that “[u]nder Amgen, such random trial-and-error discovery, without more, constitutes unreasonable experimentation that falls outside the bounds required by § 112(a).” Id. at *8, *10.
Applicant is relying upon certain biological activities such as inhibitory antibodies to surviving and a limited number of species with defined structures (e.g. amino acid sequences) to support an entire genus of diverse and structurally unrelated inhibitory antibody structures. Yet the instant specification does not provide sufficient guidance and directions as to the structural features of the polypeptide structures and the correlation between the structure and the desired antigen binding and inhibitory function.
The Supreme Court’s 2023 decision in Amgen v. Sanofi, which mainly involves the enablement requirement, states that “where a patentee purports to invent an entire genus, it must enable the entire genus”; “disclosing how to produce some antibodies that perform a specified function is not equivalent to disclosing how to produce all such antibodies – and it is the latter that petitioners claim as their invention”; S. Ct.
Additionally, in its recent decision in Baxalta Inc. v. Genentech, Inc., No. 2022-1461, 2023 WL 6135930 (Fed. Cir. Sept. 20, 2023) the Federal Circuit found the facts of this case to be "materially indistinguishable from those in Amgen." Baxalta, 2023 WL 6135930, at *4. According to the Federal Circuit, claim 1 covers "millions of potential candidate antibodies" (id.) that bind to Factor IX/IXa and increase the procoagulant activity of Factor IXa. The court, however, noted that the specification discloses the amino acid sequence of just 11 of those antibodies. And like the roadmap in the patents at issue in Amgen, "the '590 patent's roadmap simply directs skilled artisans to engage in the same iterative, trial-and-error process the inventors followed to discover the [11] antibodies they elected to disclose." (Id.) Missing from the specification, according to the Federal Circuit, was "'a quality common to every functional embodiment' ... that would allow a skilled artisan to predict which antibodies will perform the claimed functions" (id.; quoting Amgen Inc. v. Sanofi., 598 U.S. 594, 614 (2023)), such as a common structural or other feature that would allow the antibodies to perform the claimed functions, or an explanation as to why the 11 antibodies do so and others do not. (Baxalta, 2023 WL 6135930, at *4). And the Federal Circuit was not persuaded by Baxalta's argument that its disclosed hybridoma-and screening process "predictably and reliably generates new claimed antibodies every time it is performed" (id.), because "it is undisputed that to practice the full scope of the claimed invention, skilled artisans must make candidate antibodies and screen them to determine which ones perform the claimed functions." (Id.).
The specification does not reasonably provide enablement to make and use the invention of instant claims 1-7 and 11-17. The specification does enable one with ordinary skill to make the antibody clone discussed supra.
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.
To resolve this issue, it is recommended to amend claim 1 to recite specific anti-survivin antibody structures, defined by their amino acid sequences (for example, the CDR sequences recited in claim 8).
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1 and 11 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Zhang et al. ("Survivin Promotes Autoreactive Immune Cells in Myasthenia Gravis: An Animal Model and Human Study." George Washington Research Days 2019 poster).
Zhang et al. teaches that autoimmune cells from a mouse model of MG has elevated surviving expression (Abstract): “[t]he EAMG mouse model demonstrated survivin expression in CD3- CD19+ splenic B cells, but less in CD3+ CD19- splenic T cells…” Zhang et al. additionally teaches that anti-survivin antibody treatment successfully treats this mouse model of MG (Abstract): “…treatment with anti-survivin effectively reduced survivin in splenic B cells in a dose dependent manner, and corresponded to reduced levels of AChR-Specific IgG subtype production.”
Thus, Zhang et al. teaches a method of treating the survivin-positive autoimmune disease myasthenia gravis comprising administration of an anti-survivin antibody, anticipating the limitations of instant claims 1 and 11.
The reference teaching anticipates the instantly claimed invention.
Claims 1-4, 6-9, 11, 18, and 19 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Zhang et al. 2020 (J Immunol. 2020 Oct 1;205(7):1743-1751. doi: 10.4049/jimmunol.2000482), as evidenced by Fenstermaker et al. (U.S. PGPub 20170066837).
Zhang et al. 2020 teaches that survivin-positive autoimmune cells are elevated in Myasthenia Gravis in humans and a mouse model of experimental MG (Introduction): “…we found an increased percentage of survivin-expressing B cells among MG patients but a near absence in controls. Furthermore, we found the hyperplastic thymus, which is considered to be the site of disease induction in MG, to contain survivin+ cells. In our animal experiments, we determined that rodents with experimental autoimmune MG (EAMG) also had survivin+ lymphocytes.”
Zhang et al. 2020 further teaches treatment with an anti-survivin monoclonal antibody 2C2, which is the IgG2A isotype, to treat mouse experimental MG (pg. 1744): “[t]o test the therapeutic potential, we used a hybridoma IgG2a Ab to the modified peptide SVN53-63/M57 (Ab 2C2)…”
Zhang et al. 2020 teaches the 2C2 antibody successfully treats mouse experimental MG (Fig. 2).
Therefore, Zhang et al. 2020 teaches a method of treating surviving-positive MG comprising administration of a composition comprising the anti-survivin monoclonal IgG2b antibody clone 2C2, anticipating claims 1, 4, 6, 7, and 11.
Fenstermaker et al. is provided as an evidentiary reference to demonstrate the sequence of the 2C2 antibody taught by Zhang et al. Fenstermaker et al. teaches (¶[0072]): “…[a] modified survivin peptide of SEQ ID NO: 4 was used to generate hybridomas…[s]everal hybridoma lines were generated which produced antibodies that were reactive against peptide of SEQ ID NO:4 and a survivin peptide DLAQCFFCFKELEGW (SEQ ID NO:27) in which the sequence is identical to a portion of human surviving…[t]hese are termed as 2C2 and the 30H3. From these hybridomas, one clone each was further characterized. These are termed as 2C2E7…[c]onsensus amino acid sequence for the heavy and light chain variable regions from the mAb 2C2E7 are provided in SEQ ID NOs:19 and 20 respectively.”
Therefore, the prior art demonstrates that the 2C2 antibody clone has the VH and VL of SEQ ID NO: 19 and 20 of Fenstermaker et al., and was raised against SEQ ID NO: 4 of Fenstermaker et al. SEQ ID NO: 19 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 19:
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SEQ ID NO: 20 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 20:
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SEQ ID NO: 4 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 4:
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Therefore, the 2C2 antibody taught by Zhang et al. 2020 has identical VH and VL sequences as the anti-survivin sequences recited in instant claim 9, and was generated in response to the peptide claimed in instant claim 3, meeting the limitations of instant claims 2, 3, 8, 9, 18, and 19.
The reference teachings anticipates the instant invention encompassed by claims 1-4, 6-9, 11, 18, and 19.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-9, 11, 18, and 19 are rejected under 35 U.S.C. 103 as being unpatentable over Zhang et al. (supra) in view of Fenstermaker et al. (supra).
Zhang et al. teaches (Abstract): “[m]yasthenia gravis (MG) is a T cell dependent, B cell mediated disorder which targets the neuromuscular junction…[o]ur objectives are to reduce survivin in an experimental autoimmune MG (EAMG) mouse model and to demonstrate surviving as a potential target in human B cells…”
Zhang et al. further teaches that autoimmune cells from a mouse model of MG has elevated surviving expression (Abstract): “[t]he EAMG mouse model demonstrated survivin expression in CD3- CD19+ splenic B cells, but less in CD3+ CD19- splenic T cells…” Zhang et al. additionally teaches that anti-survivin antibody treatment successfully treats this mouse model of MG (Abstract): “…treatment with anti-survivin effectively reduced survivin in splenic B cells in a dose dependent manner, and corresponded to reduced levels of AChR-Specific IgG subtype production.”
Zhang et al. additionally teaches that PBMCs from patients with MG have elevated surviving expression, and suggests that anti-survivin antibodies to treat MG in humans (Abstract): “[i]n the human study, survivin was expressed in CD4- CD20+ human B cells, whereas, CD4-CD20+ survivin+ lymphocytes of MG patients are significantly higher than HCs.” Zhang et al. concludes: “[t]he animal study demonstrates that survivin does have a pathological role to promote autoreactive B cells and expression of autoantibodies. The expression of the survivin in Human B cells suggest that survivin could be used as a potential therapeutic target.”
Zhang et al. does not teach the specific antibody structure recited in claims 8 and 9.
Fenstermaker et al., in the same field of endeavor, teaches generation of the 2C2 antibody clone raised against a modified human survivin peptide (¶[0072]): “…[a] modified survivin peptide of SEQ ID NO: 4 was used to generate hybridomas…[s]everal hybridoma lines were generated which produced antibodies that were reactive against peptide of SEQ ID NO:4 and a survivin peptide DLAQCFFCFKELEGW (SEQ ID NO:27) in which the sequence is identical to a portion of human surviving…[t]hese are termed as 2C2 and the 30H3. From these hybridomas, one clone each was further characterized. These are termed as 2C2E7…[c]onsensus amino acid sequence for the heavy and light chain variable regions from the mAb 2C2E7 are provided in SEQ ID NOs:19 and 20 respectively.”
SEQ ID NO: 19 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 19 (supra), SEQ ID NO: 20 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 20 (supra), and SEQ ID NO: 4 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 4 (supra).
Fenstermaker et al. further teaches that the 2C2 antibody successfully binds to human surviving (¶[0124]): “…2C2E7 was sufficient to bind the modified survivin peptide of SEQ ID NO:4 at an OD of 1.019 and wild type survivin peptide of SEQ ID NO:27 at an OD of 0.891…”
It would have been obvious to one with ordinary skill in the art, before the effective filing date of the instant application, to have modified the teachings of Zhang et al. in view of Fenstermaker et al. to have used the 2C2 anti-survivin antibody clone in a method of treating surviving-positive MG in a patient (i.e., the limitations of instant claims 1 and 11) with a reasonable expectation of success, as Fenstermaker et al. teaches the 2C2 anti-survivin antibody structure successfully binds to human survivin that can be used in the method of treating MG taught by Zhang et al. One would have been motivated to make this change for the purposes of treating MG. One with ordinary skill in the art would appreciate that the 2C2 can replace the antibody in the method of treating MG taught by Zhang et al., or the antibody can be combined to treat MG with two different anti-survivin antibodies.
Regarding claims 2 and 3, the 2C2 antibody taught by Fenstermaker et al. was generated in response to instant SEQ ID NO: 4 (supra), meeting the claim limitations.
Regarding claim 5, Fenstermaker et al. teaches that anti-survivin antibodies can be chimeric, human, humanized, a single-chain antibody, or a multispecific antibody (claim 5), meeting the claim limitations.
Regarding claims 4, 6-9, 18, and 19, the 2C2 antibody taught by Fenstermaker et al. is a IgG2 monoclonal antibody that has identical VH and VL sequences to instant SEQ ID NO: 19 and 20, respectively, meeting the claim limitations.
Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the references, especially in the absence of evidence to the contrary.
Claims 1-9, 11, 18, and 19 are rejected under 35 U.S.C. 103 as being unpatentable over Zhang et al. 2020 (supra) in view of Safdari et al. (Biotechnol Genet Eng Rev. 2013;29:175-86. doi: 10.1080/02648725.2013.801235), as evidenced by Fenstermaker et al. (supra).
The teachings of Zhang et al. 2020, as evidenced by Fenstermaker et al., has been discussed in the 35 U.S.C. § 102 rejection supra. Zhang et al. 2020, as evidenced by Fenstermaker et al., does not teach methods of treating MG with a humanized antibody (i.e., the limitations of instant claim 5).
Safdari et al. in the same field of endeavor, teaches than the human immune response neutralizes administered non-human antibodies in patients, which limits the application of such antibodies in the treatment of human diseases (Introduction). Safdari et al. teaches that there are multiple known techniques to “humanize” antibodies to overcome this limitation, such as CDR grafting onto human frameworks and germline humanization (pages 175-177).
It would have been obvious to one of ordinary skill in the art, before the effective filing date of the invention, to have modified the combined teachings of Zhang et al. 2020, as evidenced by Fenstermaker et al., in view of Safdari et al. to humanize the 2C2 anti-survivin antibody clone to reduce the antibody’s immunogenicity in humans with a reasonable expectation of success, as Safdari et al. teaches multiple methods of antibody humanization. One would have been motivated to make this change for the purposes of reducing the immunogenicity of the 2C2 antibody taught by Zhang et al. 2020 when it is administered into humans.
Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the references, especially in the absence of evidence to the contrary.
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.
Claim 1-9, 11, 18, and 19 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 10,167,340 (Pat ‘340) in view of Zhang et al. ("Survivin Promotes Autoreactive Immune Cells in Myasthenia Gravis: An Animal Model and Human Study." George Washington Research Days 2019 poster, supra), as evidenced by Fenstermaker et al. (U.S. PGPub 20190066837, supra) Although the claims at issue are not identical, they are not patentably distinct from each other.
Pat ‘340 claims anti-survivin monoclonal antibodies comprising the VH and VL of SEQ ID NO: 19 and 20, respectively (claims 1, and 2). SEQ ID NO: 19 of Pat ‘340 is 100% identical to instant SEQ ID NO: 19:
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SEQ ID NO: 20 of Pat ‘340 is 100% identical to instant SEQ ID NO: 20:
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Pat ‘340 does not claim methods of treating surviving-positive autoimmune diseases such as MG with the antibody (i.e., the limitations of instant claim 1).
Zhang et al., in the same field of endeavor, teaches (Abstract): “[m]yasthenia gravis (MG) is a T cell dependent, B cell mediated disorder which targets the neuromuscular junction…[o]ur objectives are to reduce survivin in an experimental autoimmune MG (EAMG) mouse model and to demonstrate surviving as a potential target in human B cells…”
Zhang et al. further teaches that autoimmune cells from a mouse model of MG has elevated surviving expression (Abstract): “[t]he EAMG mouse model demonstrated survivin expression in CD3- CD19+ splenic B cells, but less in CD3+ CD19- splenic T cells…” Zhang et al. additionally teaches that anti-survivin antibody treatment successfully treats this mouse model of MG (Abstract): “…treatment with anti-survivin effectively reduced survivin in splenic B cells in a dose dependent manner, and corresponded to reduced levels of AChR-Specific IgG subtype production.”
Zhang et al. additionally teaches that PBMCs from patients with MG have elevated surviving expression, and suggests that anti-survivin antibodies to treat MG in humans (Abstract): “[i]n the human study, survivin was expressed in CD4- CD20+ human B cells, whereas, CD4-CD20+ survivin+ lymphocytes of MG patients are significantly higher than HCs.” Zhang et al. concludes: “[t]he animal study demonstrates that survivin does have a pathological role to promote autoreactive B cells and expression of autoantibodies. The expression of the survivin in Human B cells suggest that survivin could be used as a potential therapeutic target.”
It would have been obvious to one with ordinary skill in the art to have used the antibody claimed by Pat ‘340 in view of Zhang et al. in a method of treating surviving positive MG (i.e., the limitations of instant claims 1, 8, 9, 11, 18, and 19) with a reasonable expectation of success as Zhang et al. teaches methods of treating MG with anti-survivin antibodies that the antibody claimed by Pat ‘340 could be used in. One would have been motivated to make this change for the purposes of treating MG. One with ordinary skill in the art would appreciate that the 2C2 can replace the antibody in the method of treating MG taught by Zhang et al., or the antibody can be combined to treat MG with two different anti-survivin antibodies.
Regarding claims 4-7, Pat ‘340 claims humanized monoclonal antibodies (claims 1 and 4) and IgG2b isotypes (claim 6), meeting the claim limitations.
Regarding claims 2 and 3, Fenstermaker et al. is provided as an evidentiary reference to demonstrate the antibody claimed by Pat ‘340 has identical VH and VL sequences to the 2C2 antibody taught by Fenstermaker et al.
Fenstermaker et al. teaches (¶[0072]): “…[a] modified survivin peptide of SEQ ID NO: 4 was used to generate hybridomas…[s]everal hybridoma lines were generated which produced antibodies that were reactive against peptide of SEQ ID NO:4 and a survivin peptide DLAQCFFCFKELEGW (SEQ ID NO:27) in which the sequence is identical to a portion of human surviving…[t]hese are termed as 2C2 and the 30H3. From these hybridomas, one clone each was further characterized. These are termed as 2C2E7…[c]onsensus amino acid sequence for the heavy and light chain variable regions from the mAb 2C2E7 are provided in SEQ ID NOs:19 and 20 respectively.”
SEQ ID NO: 19 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 19 and SEQ ID NO: 19 of Pat ‘340:
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SEQ ID NO: 20 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 20 and SEQ ID NO: 20 of Pat ‘340:
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SEQ ID NO: 4 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 4:
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Therefore, one with ordinary skill in the art would appreciate that the 2C2 antibody, as well as the antibody structure claimed by Pat ‘340, inherently has the properties recited in instant claim 2 and 3, meeting the claim limitations.
The invention encompassed by the instant claims is a prima facie obvious variant of the invention claimed by Pat ‘340 in view of Zhang et al., as evidenced by Fenstermaker et al., especially in absence of evidence to the contrary.
Claim 1, 4, 5, 8, 11, and 18 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4 of U.S. Patent No. 11,773,181 (Pat ‘181) in view of Zhang et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other.
Pat ‘181 claims anti-survivin monoclonal antibodies comprising the HCDR1-3 of SEQ ID NO: 7-9, respectively, and the LCDR1-3 of SEQ ID NO: 10-12, respectively (claim 1). The HCDR1-3 claimed by Pat ‘181 are identical to the HCDR1-3 of the antibody recited in instant claim 8(a):
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The LCDR1-3 claimed by Pat ‘181 are identical to the LCDR1-3 of the antibody recited in instant claim 8(a):
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Pat ‘181 does not claim methods of treating surviving-positive autoimmune diseases such as MG with the antibody (i.e., the limitations of instant claims 1 and 11).
The invention encompassed by the instant claims is a prima facie obvious variant of the invention claimed by Pat ‘181 in view of Zhang et al. for the same reasons discussed for Pat ‘340 supra.
Regarding claims 4 and 5, Pat ‘181 claims monoclonal antibodies (claim 1), as well as scFv formats (i.e., “single chain antibody”; Pat ‘181 claim 5), meeting the claims limitations.
Regarding claims 8 and 18, Pat ‘181 claims monoclonal antibodies with identical CDRs (supra), meeting the claim limitations.
Therefore, the invention encompassed by the instant claims is a prima facie obvious variant of the invention claimed by Pat ‘181 in view of Zhang et al., especially in absence of evidence to the contrary.
Claims 2, 3, 6, 7, 9, and 19 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4 of U.S. Patent No. 11,773,181 (Pat ‘181, supra) in view of Zhang et al. (supra), as applied to claims 1, 4, 5, 8, 11, and 18 above, and further in view of Fenstermaker et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other.
The invention encompassed by Pat ‘181 in view of Zhang et al. has been discussed supra. The combined references do not teach an anti-survivin antibody raised against instant SEQ ID NO: 4 with the VH and VL of SEQ ID NO: 19 and 20, respectively.
Fenstermaker et al., in the same field of endeavor, teaches (¶[0072]): “…[a] modified survivin peptide of SEQ ID NO: 4 was used to generate hybridomas…[s]everal hybridoma lines were generated which produced antibodies that were reactive against peptide of SEQ ID NO:4 and a survivin peptide DLAQCFFCFKELEGW (SEQ ID NO:27) in which the sequence is identical to a portion of human surviving…[t]hese are termed as 2C2 and the 30H3. From these hybridomas, one clone each was further characterized. These are termed as 2C2E7…[c]onsensus amino acid sequence for the heavy and light chain variable regions from the mAb 2C2E7 are provided in SEQ ID NOs:19 and 20 respectively.”
SEQ ID NO: 19 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 19 (supra), SEQ ID NO: 20 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 20 (supra), and SEQ ID NO: 4 of Fenstermaker et al. is 100% identical to instant SEQ ID NO: 4 (supra).
Fenstermaker et al. additionally teaches that the anti-survivin antibodies can be the IgG2b isotype (claim 7) and human or humanized antibodies (claim 5).
It would have been obvious to one with ordinary skill in the art to have modified the invention claimed by Pat ‘181 in view of Zhang et al., further in view of Fenstermaker et al. to use the 2C2 anti-survivin antibody clone taught by Fenstermaker et al. in the method of treating MG taught by Pat ‘181 in view of Zhang et al. (i.e., the limitations of instant claims 1-9, 11, 18, and 19) with a reasonable expectation of success, as the 2C2 antibody has identical CDRs to the antibody claimed by Pat ‘181, leading one with ordinary skill in the art to expect that this antibody could work in a method of treating MG as well. One would have been motivated to make this change for the purposes of generating full-size antibodies that contain the CDRs claimed by Pat ‘181 to treat MG, such as the 2C2 antibody taught by Fenstermaker et al.
Therefore, the invention encompassed by the instant claims is a prima facie obvious variant of the invention claimed by Pat ‘181 in view of Zhang et al., and further in view of Fenstermaker et al., especially in absence of evidence to the contrary.
Claim 1, 4, 5, 8, 11, and 18 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 of U.S. Patent No. 10,738,129 (Pat ‘129) in view of Zhang et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other.
Pat ‘129 claims compositions comprising anti-survivin monoclonal antibodies comprising the HCDR1-3 of SEQ ID NO: 7-9, respectively, and the LCDR1-3 of SEQ ID NO: 10-12, respectively (claim 1). The HCDR1-3 claimed by Pat ‘181 are identical to the HCDR1-3 of the antibody recited in instant claim 8(a):
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The LCDR1-3 claimed by Pat ‘181 are identical to the LCDR1-3 of the antibody recited in instant claim 8(a):
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Pat ‘181 does not claim methods of treating surviving-positive autoimmune diseases such as MG with the antibody (i.e., the limitations of instant claims 1 and 11).
The invention encompassed by the instant claims is a prima facie obvious variant of the invention claimed by Pat ‘181 in view of Zhang et al. for the same reasons discussed for Pat ‘340 supra.
Regarding claims 4 and 5, Pat ‘129 claims monoclonal antibodies (claim 1), as well as scFv formats (i.e., “single chain antibody”; Pat ‘129 claim 2), meeting the claims limitations.
Regarding claims 8 and 18, Pat ‘129 claims monoclonal antibodies with identical CDRs (supra), meeting the claim limitations.
Therefore, the invention encompassed by the instant claims is a prima facie obvious variant of the invention claimed by Pat ‘181 in view of Zhang et al., especially in absence of evidence to the contrary.
Claims 2, 3, 6, 7, 9, and 19 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 of U.S. Patent No. 10,738,129 (Pat ‘129, supra) in view of Zhang et al. (supra), as applied to claims 1, 4, 5, 8, 11, and 18 above, and further in view of Fenstermaker et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other.
The invention encompassed by the instant claims is a prima facie obvious variant of the invention claimed by Pat ‘129 in view of Zhang et al., and further in view of Fenstermaker et al. for the same reasons discussed for Pat ‘181 supra.
Claims 1-4 and 11 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 8,580,269 (Pat ‘269) in view of Trier et al. (Methods. 2012 Feb;56(2):136-44. doi: 10.1016/j.ymeth.2011.12.001) and Zhang et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other.
Pat ‘269 claims survivin peptides used in methods of stimulating immune responses against survivin expressing cells (claim 1), wherein the peptide consists of SEQ ID NO: 6 (claim 5). SEQ ID NO: 6 of Pat ‘269 is 100% identical to instant SEQ ID NO: 4:
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Pat ‘269 does not claim producing antibodies against the peptides, or methods of treating survivin-positive MG with the antibodies.
However, once the antigen of interest is selected, the use of that antigen in the known method of Kohler and Milstein will result in the expected hybrid cell lines and the specific monoclonal antibodies. Ex parte Erlich, 3 USPQ2d 1011, 1015 (BPAI 1986).
Trier et al., in the same field of endeavor, teaches methods of synthesizing antibodies from short peptides of 8-20 amino acids in length (entire document), which would include SEQ ID NO: 6 of Pat ‘269, which is 15 residues in length. These antibodies are useful for a variety of purposes, including purification, diagnostic tests, therapeutics, and research techniques (“Applications of peptide antibodies” section). Trier et al. further teaches a method of producing the antibodies comprising culturing hybridomas expressing the antibodies (i.e., host cells comprising a nucleic acid encoding the antibody) and isolating/purifying the monoclonal antibody from the supernatant of the cultured hybridoma (“Immunization” and “Purification of peptide antibodies” sections).
Zhang et al., in the same field of endeavor, teaches (Abstract): “[m]yasthenia gravis (MG) is a T cell dependent, B cell mediated disorder which targets the neuromuscular junction…[o]ur objectives are to reduce survivin in an experimental autoimmune MG (EAMG) mouse model and to demonstrate surviving as a potential target in human B cells…”
Zhang et al. further teaches that autoimmune cells from a mouse model of MG has elevated surviving expression (Abstract): “[t]he EAMG mouse model demonstrated survivin expression in CD3- CD19+ splenic B cells, but less in CD3+ CD19- splenic T cells…” Zhang et al. additionally teaches that anti-survivin antibody treatment successfully treats this mouse model of MG (Abstract): “…treatment with anti-survivin effectively reduced survivin in splenic B cells in a dose dependent manner, and corresponded to reduced levels of AChR-Specific IgG subtype production.”
Zhang et al. additionally teaches that PBMCs from patients with MG have elevated surviving expression, and suggests that anti-survivin antibodies to treat MG in humans (Abstract): “[i]n the human study, survivin was expressed in CD4- CD20+ human B cells, whereas, CD4-CD20+ survivin+ lymphocytes of MG patients are significantly higher than HCs.” Zhang et al. concludes: “[t]he animal study demonstrates that survivin does have a pathological role to promote autoreactive B cells and expression of autoantibodies. The expression of the survivin in Human B cells suggest that survivin could be used as a potential therapeutic target.”
It would have been obvious to one of ordinary skill in the art, before the effective date of the invention, to modify the invention claimed by Pat ‘269 in view of Trier et al. and Zhang et al. to make a monoclonal antibody that specifically binds to SEQ ID NO: 6 of Pat ‘269 using the methods of Trier et al. (i.e., hybridoma technology), and use the antibody in a method of treating survivin-positive MG with a reasonable expectation of success (i.e., the limitations of instant claim 1 and 11), as Trier et al. teaches methods of generating antibodies that bind to short peptides such as the one claimed by Pat ‘269 (entire document), and Zhang et al. teaches such monoclonal antibodies can be used to treat MG. One would have been motivated to do so for the purposes of generating monoclonal anti-survivin antibodies that specifically bind to SEQ ID NO: 6 of Pat ‘269 for use in the method of treating survivin-positive MG such as the one taught by Zhang et al.
Regarding claims 2-4, the monoclonal antibody generated by the combined references would be generated in response to instant SEQ ID NO: 4, meeting the claim limitations.
Therefore, the invention encompassed by the instant claim is a prima facie obvious variant of the invention claimed by Pat ‘269 in view of Trier et al. and Zhang et al., especially in absence of evidence to the contrary.
Claims 5-7 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 of U.S. Patent No. 8,580,269 (Pat ‘269, supra) in view of Trier (supra) and Zhang et al. (supra), as applied to claims 1-4 and 11 above, and further in view of Fenstermaker et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other.
The invention claimed by Pat ‘269 in view of Trier et al. and Zhang et al. has been discussed supra. The combined teachings do not teach humanized anti-survivin antibodies, or monoclonal IgG2 antibodies (i.e., the limitations of instant claims 5-7).
Fenstermaker et al., in the same field of endeavor, teaches that anti-survivin monoclonal antibodies can be humanized (claim 5) and the IgG2b isotype (claim 7). Fenstermaker et al. teaches an example of an IgG2 anti-survivin antibody (¶[0115]): “…2C2E7 was found to have the isotype IgG2b…”
It would have been obvious to one with ordinary skill in the art to have modified the combined teachings of Pat ‘269 in view of Trier et al. and Zhang et al. further in view of Fenstermaker et al. to make a method of treating survivin-positive MG with a humanized IgG2 antibody directed to the survivin epitope comprising instant SEQ ID NO: 4 with a reasonable expectation of success, as Fenstermaker et al. teaches that such monoclonal antibodies can be made and are functional. One would have been motivated to make this change for the purposes of generating a humanized IgG2b monoclonal antibody against instant SEQ ID NO: 4 to treat survivin-positive MG.
Therefore, the invention encompassed by the instant claim is a prima facie obvious variant of the invention claimed by Pat ‘269 in view of Trier et al. and Zhang et al., and further in view of Fenstermaker et al., especially in absence of evidence to the contrary.
Conclusion
No claim is allowed.
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/ALEC JON PETERS/Examiner, Art Unit 1641
/MISOOK YU/Supervisory Patent Examiner, Art Unit 1641
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