FINAL 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 .
Status of Claims
Applicant’s amendment and response are acknowledged filed November 12, 2025. Claim 1 has been amended. Claims 2-13 have been canceled. Claims 1, and 14-37 are under examination.
Rejection Maintained
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.
Scope of Enablement:
Claims 1 and 14-37 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for the claimed method wherein the recited GDF15 modulator is an anti-GDF15 antibody or GDF15-binding fragment thereof comprising the amino acid sequences of SEQ ID NOs: 1, 4, 13, 16, 18, and 21 (i.e., the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2, and LCDR3 of the 01G06 antibody series), or the amino acid sequences of SEQ ID NOs: 37 and 25 (again, from antibody 01G06),does not reasonably provide enablement for the claimed methods using variations of this antibody-related subgenus. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
The factors to be considered in determining whether a disclosure would require undue experimentation include (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art and, (8) the breadth of the claims. In re Wands, 8 USPQ2d, 1400 (CAFC 1988).
In the instant case, claim 1 has been amended to recite a method for reducing chemotherapy-induced muscle and fat mass loss in a subject in need thereof, comprising treating the subject with at least one GDF15 modulator, wherein the subject is administered an anti-cancer agent selected from the group consisting of: capecitabine, doxorubicin, cisplatin, carboplatin and oxaliplatin, and wherein the GDF15 modulator is an anti-GDF15 antibody, or a GDF15-binding fragment thereof. (The phrase “antibody products” will be used herein to refer to anti-GDF15 antibodies or GDF15-binding fragments thereof.). Dependent claims 14-37 recite amino acid sequences for HCDR1, HCDR2, HCDR3, LCDR1, LCDR2, LCDR3, heavy chains, and/or light chains for the antibody products. However, none of the dependent claims are limited to antibody products comprising the amino acid sequences of SEQ ID NOs: 1, 4, 13, 16, 18, and 21 (i.e., the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2, and LCDR3 of the 01G06 antibody series), or the amino acid sequences of SEQ ID NOs: 37 and 25 (again, from antibody 01G06). Thus, the scope of the claims is significantly broader than the scope of what is deemed enabled.
The specification contains an assertion that antagonistic GDF15 antibody products have the activity of reducing chemotherapy-induced muscle and fat mass loss. However, the working examples only show inhibition of chemotherapy-induced body weight loss, and do not show that any of the disclosed GDF15 antibody products have the activity of reducing chemotherapy-induced muscle loss. This is an important distinction, since Applicant has amended claim 1 to address the previous rejection made under 35 U.S.C. 103 over Breit (WO 2005/099746) in view of Kiss (US2008/0098491), arguing that Breit teaches that muscle mass was unchanged in the presence of GDF15.
In view of this teaching in Breit, a finding that an antagonistic GDF15 antibody product would protect against loss of both muscle and fat upon chemotherapy treatment would have been considered unexpected. However, there are no data in the instantly filed application that supports this unexpected finding. Considering all of the evidence of record, data can be found in U.S. Patent No. 9,725,505 (of record) that antibody 01G06 has the ability to protect against loss of muscle and fat mass in tumor-xenograft cachexia models. See Figures 16A-E, Figures 29A-C, Example 20. However, these data are limited to effects of administering the 01G06 antibody, and thus the results are not commensurate in scope with what is being claimed.
Evidence that other anti-GDF15 antibody products are ineffective in reducing muscle and fat loss associated with cancer can be seen in Carneiro et al. (2025, Cancer Res Commun 5(6):896-905), wherein it was shown that anti-GDF15 antibody AZD8853 treatment did not correlate with trends in body weight changes. See abstract, p. 902 3rd paragraph of right column.
Based on this evidence, it is clear that the ordinary skilled artisan would have to resort to trial and error to determine which anti-GDF15 antibody products would have the activity required in the claims. “Make and test” is not the legal standard under 35 U.S.C.(a). In the absence of detailed guidance and/or working examples, “make and test” results in large quantities of experimentation.
Furthermore, the nature of the invention is complex and unpredictable, involving the effects of biological molecules on physiology in diseased subjects being treated with other chemical compounds. As was found in Ex parte Hitzeman, 9 USPQ2d 1821 (BPAI 1987), a single embodiment may provide broad enablement in cases involving predictable factors such as mechanical or electrical elements, but more will be required in cases that involve unpredictable factors such as most chemical reactions and physiological activity. 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). See also In re Fisher, 427 F.2d 833, 839, 166 USPQ 18, 24 (CCPA 1970); Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 927 F.2d 1200, 1212, 18 USPQ2d 1016, 1026 (Fed. Cir.), cert. denied, 502 U.S. 856 (1991).
Therefore, even though the level of skill in the art is high, due to the large quantity of experimentation necessary to determine which anti-GDF15 antibody products would have the required activity of reducing chemotherapy-induced muscle and fat loss other than antibody 01G06, the lack of direction/guidance presented in the specification regarding the same, the absence of working examples directed to the same, the complex nature of the invention, the contradictory state of the prior art (see Breit and Carneiro et al.), the unpredictability of the effects of complex biological molecules in combination with other chemical therapeutics on a diseased physiological system, and the breadth of the claims, undue experimentation would be required of the skilled artisan to make and/or use the claimed invention in its full scope.
Applicant’s Arguments – Enablement
Applicant argues that the claims have been amended to specify that the anti-GDF 15 antibody selectively binds GDF 15 and selectively and significantly reduces binding of GDF15 to its endogenous receptor. Applicant argues that the instant application teaches that a GDF15 modulator, i.e., "an agent that inhibits GDF 15 activity or the activity of the GDF 15 pathway," can reverse chemotherapy induced cachexia. Applicant argues that these modulators include anti-GDF15 antibodies, "that prevent GDF15 binding to its cognate binding partner." The cachexia is associated with muscle and fat mass loss. Applicant argues that the examples of the instant application show that both monoclonal antibody 14F 11 and polyclonal anti-GDF15 antibodies reversed cachexia and resulted in 100% sustained survival over up to 30 days in mouse models of cachexia. As shown in Lerner et al. J. Cachexia Sarcopenia Muscle, 7(4): 467-482 (Oct. 29, 2015) ("Lerner") this led to increases in muscle and fat.
Applicant argues that the evidence provided by the Examiner, and the evidence regarding other anti-GDF 15 antibodies suggests that the results for AZD8853 shown in Carneiro are the exception, not the rule. Carneiro teaches that there was a lack of clear trend in body weight when AZD8853 was administered, in contrast to ponsegromab. Carneiro teaches that, "[t]he anti-GDF15 antibody ponsegromab suppressed serum unbound GDF15 concentrations and was associated with weight gain in patients with advanced cancer in a phase Ib." Carneiro suggests that, "[t]he lack of clear trend in body weight change during AZD8853 treatment could reflect an absence of sustained effects on GDF 15. Elevated GDF15 concentrations are associated with weight loss and poor outcomes in patients with various types of cancer." Reduction in loss of muscle and fat mass has also been found with visugromab,' and FL-501.9 Applicant argues that AZD8853 does not appear to selectively and significantly reduce binding of GDF 15 to its endogenous receptor, which may be why it was not shown to be effective in reducing muscle and fat mass loss. Applicant submits that claim 1 excludes antibodies that do not selectively and significantly reduce binding of GDF 15 to its endogenous receptor. The Examiner has not provided evidence that such an antibody would not be effective in reducing muscle and fat mass loss.
Response to Arguments
Applicant’s arguments have been fully considered but they are not persuasive.
In response to Applicant’s argument that the claims have been amended to specify that the anti-GDF 15 antibody selectively binds GDF 15 and selectively and significantly reduces binding of GDF15 to its endogenous receptor, the amendment is acknowledged. However, this amendment is insufficient to overcome the rejection. The newly amended claims encompass an extremely large genus of antibodies that are described solely by their function. The claim requires that the antibodies exhibit specific functions, i.e., selectively and significantly reduce binding to GDF15 to its endogenous receptor and reduce chemotherapy-induced muscle and fat mass loss, but the specification provides limited guidance regarding which antibodies are capable of the required function. Although the specification provides two exemplary antibodies, the claims are not limited to these antibodies. Thus, the scope of the claim is broader than the scope of what is deemed enabled.
Further, the art provides evidence that not all anti-GDF15 antibodies have the claimed function. Although Applicant argues that the evidence provided by the examiner is the exception, no other antibodies encompassed by the claims have been provided. The evidence is still applicable in that it demonstrates that one of skill in the art would not know a priori which anti-GDF15 antibodies have the functions required by the claims. Given the breadth of the claims, coupled with the limited guidance in the specification and the art, one would have to resort to trial an error to identify which anti-GDF15 antibodies would have the claimed functions. As noted in the rejection above, the nature of the invention is complex and unpredictable. Even with the skill in the art being high, it would be undue experimentation for one of skill in the art to determine which antibodies exhibit the specific functions, i.e., selectively and significantly reduce binding to GDF15 to its endogenous receptor and reduce chemotherapy-induced muscle and fat mass loss, encompassed by the claims.
Written Description:
Claims 1 and 14-37 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.
As discussed above, claim 1 has been amended to recite a method for reducing chemotherapy-induced muscle and fat mass loss in a subject in need thereof, comprising treating the subject with at least one GDF15 modulator, wherein the subject is administered an anti-cancer agent selected from the group consisting of: capecitabine, doxorubicin, cisplatin, carboplatin and oxaliplatin, and wherein the GDF15 modulator is an anti-GDF15 antibody, or a GDF15-binding fragment thereof. (The phrase “antibody products” will be used herein to refer to anti-GDF15 antibodies or GDF15-binding fragments thereof.). Dependent claims 14-37 recite amino acid sequences for HCDR1, HCDR2, HCDR3, LCDR1, LCDR2, LCDR3, heavy chains, and/or light chains for the antibody products. However, none of the dependent claims are limited to antibody products comprising the amino acid sequences of SEQ ID NOs: 1, 4, 13, 16, 18, and 21 (i.e., the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2, and LCDR3 of the 01G06 antibody series), or the amino acid sequences of SEQ ID NOs: 37 and 25 (again, from antibody 01G06).
Therefore, all of the claims read on methods of using antibody products wherein the recited antibody or antigen-binding fragment thereof comprises less than the full complement of six CDR sequences comprising the amino acid sequences of SEQ ID NOs: 1, 4, 13, 16, 18, and 21. Additionally, the claims do not recite a structure for the recited antigen, GDF15.
In summary, the claims recite a genus of antibody products having (1) an explicitly recited functional feature of specifically binding any GDF15 protein and (2) an implied functional feature of inhibiting GDF15 such that the antibody products have the required activity of reducing chemotherapy-induced muscle and fat mass loss. However, the claims recite only partial structural features.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through establishment of a structure-function correlation (by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics) or through a sufficient description of a representative number of species. Either is considered sufficient to show the applicant was in possession of the claimed genus.
Regarding structure-function correlation, it is noted that one of skill in the art was aware that there is a lack of structure-function correlation in antibody molecules. Evidence of such in the form of publications in the art include the following.
First, the prior art recognizes that the full six CDR sequences are required to form the part of an antibody, i.e., the paratope, that specifically binds the target antigen. See Al Qaraghuli et al. (2020, Nature Scientific Reports 10:13969), who state that the six CDRs form a continuous surface to form the paratope that binds the epitope of the cognate antigen.
However, the prior art also recognizes that a single protein can be bound by a very large and structurally diverse genus of antibodies (i.e., there is no common structural relationship even for antibodies that bind to the same protein, epitope, or overlapping epitopes). For example, Edwards et al. (2003, JMB 334:103-118) teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences, and representative of almost the entire extensive heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines), and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well.
Lloyd et al. (2009, Protein Engineering, Eng. Design & Selection 22(3): 159-168) teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding. Said reference further teaches that in their studies, of the 841 unselected and 5,044 selected antibodies sequenced, all but one of the 49 functional VH gene segments was observed, and that there are on average about 120 different antibodies generated per antigen. Said reference also teaches that a wide variety of VH and VL pairings further increase diversity. (See entire reference.)
Goel et al. (2004, J. Immunol. 173: 7358-7367) teach that three mAbs that bind to the same short (12-mer) peptide, exhibit diverse V gene usage, indicating their independent germline origin. Said reference further teaches that two of these mAbs recognize the same set of amino acid residues defining the epitope (alternate amino acid residues spread over the entire sequence), however, the relative contribution of each set of residues in the peptide showed significant variation. The reference notes that all of the mAbs do not show any kind of V gene restriction among themselves, implying variable paratope structure, despite that two of these mAbs bind to the peptide through a common set of residues. (See entire reference).
Khan et al. (2014, J. Immunol. 192: 5398-5405) teach that two structurally diverse germline mAbs recognizing overlapping epitopes of the same short peptide do so in different topologies, the antibodies possessing entirely different CDR sequences. Said reference teaches that unrelated mAbs structurally adjust to recognize an antigen, indicating that the primary B cell response is composed of BCRs having a high degree of structural adaptability. Said reference also teaches that the common epitope(s) also adopt distinct conformations when bound to different mAbs, with the higher degree of structural plasticity inherent to the mAbs. Said reference further teaches “It has been shown that both the framework region and the CDRs have a considerable amount of inherent conformational plasticity...Therefore, it is not surprising that distinct germline Abs recognize the same epitope by rearranging the CDR conformations. This may well have implications of Ag specificity beyond the naive BCR repertoire, because Kaji et al... .have shown in a recent report that the B cell memory can contain both germline-encoded and somatically mutated BCRs.” (See entire reference).
Poosarla et al. (2017, Biotechn. Bioeng. 114(6): 1331 -1342) teach substantial diversity in designed mAbs (sharing less than 75% sequence similarity to all existing natural antibody sequences) that bind to the same 12-mer peptide, binding to different epitopes on the same peptide. Said reference further teaches “most B-cell epitopes... in nature consist of residues from different regions of the sequence and are discontinuous...de novo antibody designs against discontinuous epitopes present additional challenges...". (See entire reference.)
Rabia, et al. (2018, Biochemical Engineering Journal 137:365-374) teach what effects mutations can have on an antibody's stability, solubility, binding affinity and binding specificity. Rabia et al. report that an increase in antibody affinity can be associated with a decrease in stability (p. 366, col. 2 last paragraph; Fig. 2). Rabia et al. thus teach that affinity and specificity are not necessarily correlated and that and increase in affinity does not indicate an increase in specificity (Fig. 3; p. 368, col. 1, section 3,1st full paragraph to col. 2, 2nd full paragraph).
Conversely, evidence also shows that some functionally diverse antibodies can share some structural similarities, including an entire CDR region. See Igawa et al. (US 9,334,331 B2), who disclose antibody Q153 that binds human Factor IXa. Q153 comprises a VH-CDR1 identical to the VH-CDR1 of antibody 11E12 disclosed by Gonzales et al. (US 10,421,807 B2). However, 11E12 specifically binds canine IL-31, a protein having no structural or functional similarity to human Factor IXa. This illustrates that even when some CDR regions share 100% structural identity, the antibodies in which they are comprised can have completely different functions (i.e., binding specificities).
The combination of evidentiary publications thus underscores a lack of structure-function correlation in antibody molecules.
Regarding a representative number of species, the instant specification fails to describe a representative number of species to provide adequate written description of the claimed genus as per MPEP § 2163. While the specification provides general descriptions of how to make antibodies that bind GDF15 proteins and how to test them for desired binding and therapeutic activities, only one species of antibody within the claimed genus is described with sufficient identifying characteristics using precise definitions such as structure, formula, chemical name, or physical properties such that one skilled in the art could visualize or recognize the identity of the claimed subject matter. The one fully described species within this genus, 01G06, comprises CDRs comprising the amino acid sequence of SEQ ID NOs: 1, 4, 13, 16, 18, and 21. These CDR regions are comprised in an light chain and heavy chain amino acid sequences of SEQ ID NO: 25 and 37, respectively. Accordingly, the specification describes a single species of antibody having the structure and functions required by the claims.
Applicant’s attention is directed to the recent decision in Amgen Inc. v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017). The court discussed whether an antibody is adequately described by describing a newly characterized antigen. Specifically, the court referred to the decision in Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341 (Fed. Cir. 2011). In that case, the patentee claimed a genus of antibodies containing a human variable region that has particularly desirable therapeutic properties: high affinity, neutralizing activity, and A2 specificity. Despite the fact that the specification disclosed human TNF-α protein, and despite the disclosure of the structures of more than one species of antibody related to the genus, the court ruled that that the generic antibody claims at issue were invalid for lack of written description. The fact pattern is similar in the instant case. As in the court case, the instant claims recite a genus of antibodies that have affinity for a specific antigen and have a desirable special property, i.e., ability to be therapeutically effective in methods of treating tumors or inducing an immune response. Following the finding in Centocor, the instant claims are found to lack adequate written description. Similarly, in Juno Therapeutics, Inc., Sloan Kettering Institute for Cancer Research v. Kite Pharma, Inc. (Case 2020-1758, CAFC August 2021), the court found that the disclosure of two antibody products (scFv molecules) was insufficient to support written description for the claimed genera, specifying that the specification at issue failed to disclose “structural features common to the members of the genus to support that the inventors possessed the claimed invention;” i.e., the specification and evidence of record failed to provide a structure-function correlation. In the instant case, there is also no evidence of a structure-function correlation for antibodies, and thus the claims are properly rejected for lack of adequate written description.
Applicant’s Arguments – Written Description
Applicant argues that Applicant clearly had possession of the methods of claims 1 and 14-37 based on the teachings of the instant application as well as post-filing data showing that anti-GDF 15 antibodies have been repeatedly shown to reduce muscle and fat loss induced by a chemotherapeutic as explained above.
Response to Arguments
Applicant’s arguments have been fully considered but they are not persuasive. In response to Applicant’s argument that the claims have been amended to specify that the anti-GDF 15 antibody selectively binds GDF 15 and selectively and significantly reduces binding of GDF15 to its endogenous receptor, the amendment is acknowledged. However, this amendment is insufficient to overcome the rejection. The newly amended claims encompass an extremely large genus of antibodies that are described solely by their function. However, the encompassed antibodies have no correlation between their structure and function. The claim requires that the antibodies exhibit specific functions, i.e., selectively and significantly reduce binding to GDF15 to its endogenous receptor and reduce chemotherapy-induced muscle and fat mass loss, but the specification provides no guidance regarding antibodies having the claimed functions. Further, the specification does not provide a representative number of species. The specification discloses two exemplary antibodies that have the required functions. However, the specification does not provide any guidance regarding the structure that correlates with the required functions, and therefore, the two species disclosed do not describe the breadth of the claims.
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 §§ 706.02(l)(1) - 706.02(l)(3) 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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
Claims 1 and 14-37 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-36 of U.S. Patent No. 9,725,505 in view of Smith et al. (US 2009/0291077 A1; published 26 November 2009) and Kiss (US 2008/0098491 A1; published 24 April 2008) for the following reasons.
Both the patented claims and the instant claims recite a method of treating cachexia in a subject suffering from cancer, comprising treating the subject with at least one GDF15 modulator such as a GDF15 antibody. The claim sets differ in that the patented claims recite specific GDF15 antibodies, whereas the GDF15 modulators such as GDF15 antibodies recited in the instant claims are recited generically. However, the patented species anticipate the instant genus in this respect. Also, the patented claims do not recite co-administration with an anti-cancer agent. However, co-administration of anti-cancer agents and anti-anorexic/anti-cachexia agents was well known in the art at the time of the invention. For example, Smith et al. teach methods for increasing the overall survival in a subject having cancer anorexia-cachexia syndrome, comprising treating the subject with at least one anti-cancer agent and at least one anti-anorexia/anti-cachexia agent which in this case is an anti-IL-6 antibody. The anti-cancer agents can be gemcitabine. See abstract, [004], [0036]-[0037], [0065]-[0066]. Kiss also explains the importance of administering anti-anorexia/anti-cachexia agents with chemotherapeutic agents to improve overall survival of cancer patients.
Kiss explains that both tumors and anti-cancer drugs such as cisplatin can cause cachexia, which negatively impacts survival of cancer patients. See Abstract, [0002]-[0005].
Therefore, it would have been obvious to one of ordinary skill in the art at the time the invention was filed to modify the method of treating cachexia in subjects including those suffering from cancer as recited in the patented claims by also administering anti-cancer agents such as gemcitabine or cisplatin as suggested by Smith et al. and Kiss, with a reasonable expectation of success. The motivation to do so is provided by Smith et al. and Kiss, who explicitly discuss the importance of providing anti-anorexic/anti-cachexic therapy in combination with anti-cancer agents, as both types of drugs affect overall survival of the patient.
Applicant’s Arguments
Applicant request that the rejection be held in abeyance.
Response to Arguments
Applicant’s arguments have been fully considered but they are not persuasive. MPEP 804 states that a complete response to a nonstatutory double patenting (NDP) rejection is either a reply by applicant showing that the claims subject to the rejection are patentably distinct from the reference claims or the filing of a terminal disclaimer in accordance with 37 CFR 1.321 in the pending application(s) with a reply to the Office action. Such a response is required even when the nonstatutory double patenting rejection is provisional. As filing a terminal disclaimer, or filing a showing that the claims subject to the rejection are patentably distinct from the reference application's claims, is necessary for further consideration of the rejection of the claims, such a filing should not be held in abeyance. Only objections or requirements as to form not necessary for further consideration of the claims may be held in abeyance until allowable subject matter is indicated. Therefore, an application must not be allowed unless the required compliant terminal disclaimer(s) is/are filed and/or the withdrawal of the nonstatutory double patenting rejection(s) is made of record by the examiner. Accordingly, the rejection is maintained.
New Rejection Necessitated by Applicant’s Amendment
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.
Claim 1 is 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 pre-AIA the applicant regards as the invention.
Claim 1 recites “selectively binds GDF15 and selectively and significantly reduces binding ofGDF15 to its endogenous receptor”. It is unclear as to what applicant intends by the terms “selectively and significantly”. The level or degree in which the claims refer to cannot be determined. Correction/Clarification is required.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Conclusion
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/VANESSA L. FORD/Supervisory Patent Examiner, Art Unit 1674