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 .
DETAILED ACTION
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-12 and 14 and species: Fab fragment in the reply filed 07/28/2025 is acknowledged.
Claims 13 and 15-20 are withdrawn from consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions and species, there being no allowable generic or linking claims. Election was made in the reply filed 07/28/2025.
Claims 1-7, 9, 11-12 and 14 are now under consideration in the instant Office Action.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. The hyperlinks can be found on pages 11 and 96, where there are three instances of its use. Applicant is advised to review the entire specification for any additional embedded hyperlinks and/or other form of browser-executable code.
Claim Objections
Claim 1 is objected to because of the following informalities: it recites “…wherein the antibody comprises the antibody comprises a heavy chain complementarity…”. The language of the claim is repetitive and should be revised to remove the redundancy. Appropriate correction is required.
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 4 is 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Instant claim 4 recites an antibody that binds to human transferrin receptor (TfR), wherein the antibody comprises “… a (VH or VL) comprising an amino acid sequence at least 80% identical to SEQ ID NO: (respective number)…”. The claims encompass a genus of heavy and/or light chain variable regions comprising variability (e.g., 80% identical) in both the heavy and/or light chain variable regions which are claimed as having the function of specifically binding to TfR. This means that the variability in sequence identity can also occur in the CDRs, the domains that are critical for the antibody binding to its target, which one of ordinary skill in the art would understand to result in unpredictable binding characteristics with no reasonable expectation of maintaining antigen binding. Additionally, the instant disclosure does not provide an adequate number of species of the claimed genus nor does the disclosure provide a structure-function correlation that would allow for a person of ordinary skill in the art to envision what variation can occur to the light and heavy chains, particularly in the CDR regions, such that the obtained structure would result in the claimed functions.
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The antibodies or antigen binding fragments thereof in Applicant disclosure Table 1 (see selected Ab 6-D3 (entire table not copied) above) with 100% sequence identity in the CDR regions of the heavy and light chain variable regions represents the antibodies and antigen binding fragments thereof that the applicant was in possession of at the time of filing. It is noted that there would be support for 100% identity of the full complement of the six CDRs together with some percentages of identity in the framework region that would have been predictable.
At the time of filing, antibody functionality was known to depend on the entire structure, particularly a full complement of six CDRs. At the time of filing, no evidence of mutations in the six CDRs (e.g., 6-D3 antibody SEQ ID NOs: 49-51 (HCDR1-3); 52, 29, 53 (LCDR1-3)) of the instant claimed anti-human-TfR antibody (within Applicant’s claimed range of variability) which retain antigen (e.g., Transferrin Receptor) binding were taught in the prior art. It is understood by one of ordinary skill in the art that that mutation to CDRs is unpredictable and that each construct requires function testing.
Sela-Culang et al. (Fron. Immuno., Vol. 4, Article 302, Oct. 2013, in instant PTO-892), hereinafter “Sela-Culang”, reviews the structural basis of antibody-antigen recognition in the state of the art. Naturally occurring antibodies typically consists of four polypeptide chains with two identical heavy (H) and two identical light (L) chains, with H and L chains liked to form a Y-shaped structure known as a Fab [e.g., pg. 4, Figure 2A-B]. The Fab has two variable (V) domains (VH and VL) that dimerize to form the Fv fragment which comprises the antigen-binding site of the antibody via six hypervariable loops (3 Heavy, 3 light) [e.g., pg. 3, “The Role of CDRs and their Definition”]. The six hypervariable loops are commonly termed complementary determining regions (CDRs) and are widely assumed to be responsible for antigen recognition [e.g., pg. 1, abstract] and the three-dimensional configuration of these CDRs form the antigen-recognition complex termed a paratope [e.g., pg. 3, “The Role of CDRs and their Definition”]. Despite the integrated effect of CDRs, antibodies can also be considered a modular system , composed of different elements (e.g., Fab, VH, VL) which may bind to an antigen on their own with the smaller fragments retaining affinity and specificity, which is of great potential for drug design [e.g., pg. 6, paragraph 2]. A person of ordinary skill in the art would understand that although the above basics of antibody-antigen binding are known, that the specifics of antibody structure (e.g., within the CDRs) that underlie the antigen recognition are not well characterized [e.g., pg. 1, “The Motivations for…”].
Further, Herold et al. (Nature Scientific Reports, 7:12276, 25 Sep 2017, in instant PTO-892), hereinafter “Herold”, teaches that it should be emphasized that there is no correlation between experimentally determined change in antibody binding affinity and a given mutation and additionally that no such correlation is expected because antigen binding is “affected by each CDR loop differently” and changes thereto “can in principle affect antigen binding affinity in an unpredictable way” [e.g., pg. 14, paragraph 2]. Further, Herold asserts that multiple determinants regulate antigen affinity and the interactions with CDRs are complex [e.g., pg. 14, paragraph 3].
As further evidence, see Koenig et al. (PNAS, E486-E4995, January 5, 2017, in instant PTO-892), which provides a large mutation analysis study where every amino acid in both variable regions are substituted with every other amino acid. In review of figure 1, the bottom half of each section (labeled VEGF) relates to the ability of the mutant to bind the original target, with blue meaning a reduced affinity and black meaning complete loss of binding ability. In VL-CDR1, for example, mutating any given residue to cysteine resulted in reduced binding at 7 residues and a complete loss of binding (no longer binds same target) at 4 residues. That is, at 100% of positions, mutation to cysteine reduced or ablated the antibody’s ability to bind the target, even in the case of conservative mutations.
Thus, making changes to the CDR sequence of an antibody sequence is a highly unpredictable process and one skilled in the art could not a priori make any predications regarding such mutations with any reasonable expectation of success nor envisage the breadth of structurally unrelated CDR combinations that would still possess the required function(s).
As indicated by the art, a full complement of 6 CDRs are required for antigen binding and one cannot predict which CDR residues may be changed and still result in an antibody that binds transferrin (e.g., Transferrin Receptor). Written description can be met if the claims recite the minimal structure that is needed to perform the function recited in the claims. Above, the art indicates that the 6 CDRs in an antibody are the minimal structure that binds to a target antigen. Specifically, Applicant’s claim 4 would need to recite or depend from a claim that recites how the instant claimed variability (e.g., 80% identical) of the VH and VL sequence pair (e.g., totaling 6 CDRs) binds transferrin, without variability in the CDR sequences thereof.
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 1-7, 9, 11-12, and 14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-6 of copending Application No. 17/791,667, hereinafter ‘667. Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘667 claims anticipate the instant claims.
The instant claims are drawn to an antibody that binds to human transferrin receptor (TfR), wherein the antibody comprises the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55. Dependent claim 14 recites wherein the antibody is in a complex with a molecular payload.
The claims of the ‘667 application are drawn to a complex comprising an anti-transferrin receptor antibody covalently linked to a molecular payload configured for modulating expression or activity of a muscle disease gene, wherein the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55.
Thus, the difference between the two sets of claims is the claims to the instant application do not explicitly recite that the payload is targeted to a muscle disease gene for expression or activity modulation associated with a muscle disease. Given that the instant claims recite targeting muscle cells for treating a muscle disease using the same antibody and teach a broad genus of drugs that can be used as the molecular payload, they are anticipated by the species of molecular payload drugs recited in the copending ‘667 claims. Therefore, the instant claims are rejected as anticipated by the species recited in the copending claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-7, 9, 11-12, and 14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 of copending Application No. 17/791,681 hereinafter ‘681. Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘681 claims anticipate the instant claims.
The instant claims are drawn to an antibody that binds to human transferrin receptor (TfR), wherein the antibody comprises the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55. Dependent claim 14 recites wherein the antibody is in a complex with a molecular payload.
The claims of the ‘681 application are drawn to a complex comprising an anti-transferrin receptor antibody covalently linked to an oligonucleotide that targets DMPK activity, wherein the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55.
Thus, the difference between the two sets of claims is the claims to the instant application do not recite that the payload targets DMPK activity. However, the instant specification in paragraphs [00036-00038] recite that the molecular payload may comprise an oligonucleotide which targets drug metabolism and pharma kinetics (DMPK). Given that the instant claims when interpreted in light of the instant specification account for a genus of molecular payloads that target the DMPK of muscle cells for treating a muscle disease using the same antibody, they are anticipated by the species of molecular payload drugs recited in the copending ‘681 claims. Therefore, the instant claims are rejected as anticipated by the species recited in the copending claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-7, 9, 11-12, and 14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 3-6 of copending Application No. 17/791,701 hereinafter ‘681. Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘701 claims anticipate the instant claims.
The instant claims are drawn to an antibody that binds to human transferrin receptor (TfR), wherein the antibody comprises the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55. Dependent claim 14 recites wherein the antibody is in a complex with a molecular payload.
The claims of the ‘701 application are drawn to a complex comprising an anti-transferrin receptor antibody covalently linked to an oligonucleotide that induces dystrophin (DMD) exon skipping, wherein the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55.
Thus, the difference between the two sets of claims is the claims to the instant application do not recite that the payload is an oligonucleotide that induces dystrophin (DMD) exon skipping. However, the instant specification in paragraphs [000478] recites that the molecular payload may comprise an oligonucleotide which may induce exon skipping by blocking spliceosome recognition of a splice site. In some embodiments, exon skipping results in a truncated but functional protein compared to the reference protein (e.g., truncated but functional DMD protein as described below). Given that the claims when interpreted in light of the instant specification account for the genus of molecular payloads that target DMD exon skipping for treating a muscle disease using the same antibody, they are anticipated by the species of molecular payload drugs recited in the copending ‘701 claims. Therefore, the instant claims are rejected as anticipated by the species recited in the copending claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-7, 9, 11-12, and 14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-6 of copending Application No. 17/794,768 hereinafter ‘768. Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘681 claims anticipate the instant claims.
The instant claims are drawn to an antibody that binds to human transferrin receptor (TfR), wherein the antibody comprises the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55. Dependent claim 14 recites wherein the antibody is in a complex with a molecular payload.
The instant claims are drawn to a complex comprising an anti-transferrin receptor antibody covalently linked to an oligonucleotide that targets a pro-atrophy gene, wherein the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55.
Thus, the difference between the two sets of claims is the claims of ‘768 are drawn to a specific pro-atrophy muscle disease associated gene that is targeted by the molecular payload (oligonucleotide), whereas the instant claims are generic to this aspect and target the modulation of expression or activity to any muscle disease gene. As such, the claims of the ‘768 application would necessarily anticipate the instant claims because the inhibition of pro-atrophy gene expression and/or activity reads on the generic modulation of expression/activity of any muscle disease gene targeted by the molecular payload.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-7, 9, 11-12, and 14 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4-9 of copending Application No. 17/791,670, hereinafter ‘670, in view of US 2019/0298847 Al (hereinafter ‘847, in instant PTO-892), Latres et al. (hereinafter “Latres”, in instant PTO-892), and Pasteuning-Vuhman et al. (hereinafter “Vuhman”, in instant PTO-892). Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘670 claims anticipate the instant claims.
The instant claims are drawn to an antibody that binds to human transferrin receptor (TfR), wherein the antibody comprises the antibody comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55. Dependent claim 14 recites wherein the antibody is in a complex with a molecular payload.
The claims of the ‘670 application are drawn to a complex comprising a muscle-targeting agent covalently linked to a molecule payload that modulates the expression or activity of myostatin, inhibin beta A, and/or activin receptor type-1b, wherein the muscle-targeting agent specifically binds to an internalizing cell surface receptor on a muscle cell. The aforementioned complex also comprises an antibody that comprises a heavy chain complementarity determining region 1 (CDR-H1), a heavy chain complementarity determining region 2 (CDR-H2), a heavy chain complementarity determining region 3 (CDR-H3) of a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 54, and a light chain complementarity determining region 1 (CDR-L1), a light chain complementarity determining region 2 (CDR-L2), a light chain complementarity determining region 3 (CDR-L3) of a light chain variable region (VL) comprising the amino acid sequence of SEQ ID NO: 55.
However, the instant claims do not teach that the cytotoxic payload is a myostatin (MSTN), inhibin beta A (INHBA), and/or activin receptor type-1b (ACVR1B).
‘847 remedies this deficiency.
‘847 teaches composition and methods of treating muscle atrophy and myotonic dystrophy [e.g., title and abstract]. ‘847 teaches a molecule of Formula (I): A-X1-B-X2-C (a complex), wherein A is a binding moiety, B is a polynucleotide that hybridizes to a target sequence of an atrogene, C is a polymer, and X1/X2 are each independently selected from a bond or a non-polymeric linker (covalent link) [e.g., para 0005]. ‘847 further teaches gene suppression by RNA-induced gene silencing (e.g., RNAi) [e.g., para 0003]. ‘847 teaches a polynucleotide (molecular payload) for modulating a gene (expression) associated with muscle atrophy (atrogene) [e.g., para 0004], an embodiment in which the atrogene is MSTN, and an embodiment in which A is an anti-Transferrin Receptor (internalizing cell surface receptor) antibody (muscle-targeting agent) [e.g., para 0005]. ‘847 teaches the treatment of a variety of indications (e.g., chronic renal failure, congestive heart (cardiac muscle cells) disease, sarcopenia, chronic respiratory disease, myotonic dystrophy, cancer cachexia-associated atrophy) with the disclosed compositions and methods [e.g., paras 0006, 0008].
However, ‘847 does not teach the INHBA or ACVR1B. Latres remedies this deficiency.
Latres teaches Activin A (INHBA) prominently regulates muscle mass, is a negative muscle mass regulator, inhibition leads to muscle hypertrophy (growth) and force production and suggest Activin A as a preferred therapeutic target that maximizes the benefit-risk ratio for muscle diseases in man [e.g., title and abstract].
However, ‘847 and Latres does not teach ACVR1B as a therapeutic target. Vuhman remedies this deficiency.
Vuhman teaches ALK4 (ACVR1B) as a mediator of muscle atrophy and regeneration, that muscle wasting (atrophy) is negatively regulated by MSTN, that ALK4 is a key receptor of the MSTN pathway, and that ALK4 inhibition increases myogenesis (muscle growth) [e.g., title and abstract]. Vuhman further teaches blockage (inhibition) of the MSTN/ACVR2B pathway as a therapy for various types of muscle dystrophies has been the focus of many research groups [e.g., pg. 14, Discussion].
It would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to combine the molecule formula (complex) with covalent linkages (X1, X2), and the MSTN (atrogene) as well as the anti-transferrin receptor antibody embodiments taught by ‘847 and ‘670 with the INHBA (Activin a) preferred therapeutic target (which maximizes the benefit-risk ratio) for muscle disorders taught by Latres, and/or the ACVR1B (key MSTN pathway receptor) negative regulator of muscle atrophy therapeutic taught by Vuhman, in the context of designing and/or developing therapeutics to treat muscle atrophy and/or dystrophy. ‘847 teachings of the wide-ranging muscle atrophy and dystrophy-related indications (e.g., chronic renal failure, congestive heart failure, myotonic dystrophy, cancer cachexia-associated atrophy) treatable by disclosed embodiments would have motivated one of ordinary skill in the art to combine the teachings of ‘847 because the ability to treat a broad range of diseases with a given therapeutic benefits the public health (e.g., subjects) and has a financial incentive (e.g., treating many diseases instead of one opens the product to more markets and a greater return on investment). One of ordinary skill in the art would have been further motivated to combine the teachings (see above) of the claims of ‘670 and ‘847, with Latres’ teachings of INHBA (Activin a) as a target gene because it is taught as a “preferred” therapeutic target which maximizes the benefit-risk for muscle diseases in man. One of ordinary skill in the art would have been further motivated to combine the teachings (see above) of ‘670, ‘847, and Latres, with Vuhman’s teachings of ACVR1B (ALK4) as a target gene because it is taught as a mediator of muscle atrophy wherein inhibition results in muscle growth, a key regulator of the MSTN pathway and MSTN pathway inhibitors are a known therapeutic target of interest for muscle diseases as evidenced by the focus of research in the area, see rejection above.
This is an obviousness type provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
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/SELAM BERHANE/Examiner, Art Unit 1675
/JEFFREY STUCKER/Supervisory Patent Examiner, Art Unit 1675