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 Response
Claims 60-69, 71-73, and 79-81 are pending and currently under prosecution.
Priority
Should applicant desire to obtain the benefit of foreign priority under 35 U.S.C. 119(a)-(d) prior to declaration of an interference, a certified English translation of the foreign application must be submitted in reply to this action. 37 CFR 41.154(b) and 41.202(e).
Failure to provide a certified translation may result in no benefit being accorded for the non-English application.
Claim Objections
Claims 60 is objected to because of the following informalities: Claim 60 recites “TrkA”, this abbreviation has not been defined prior to recitation. Examiner advises to define abbreviation of antibody target. Appropriate correction is required.
Claims 62, 63, and 65-67 are objected to because of the following informalities: The claims use “~” in between the sequence numbers, this “~” should be replaced with “-“. Appropriate correction is required.
Claims 76 and 77 are objected to under 37 CFR 1.75 as being a substantial duplicate of claims 71 and 72, respectively. When two claims in an application are duplicates or else are so close in content that they both cover the same thing, despite a slight difference in wording, it is proper after allowing one claim to object to the other as being a substantial duplicate of the allowed claim. See MPEP § 608.01(m). Claims 71 and 72 is drawn to a method of treatment comprising administering the antibody or antigen-binding fragment of claim 60. Claims 76 and 77 are drawn to the same methods of treatment drawn to the nucleic acid molecule that encodes the heavy chain of the antibody according to claim 60. Thus, they are drawn to the same methods of treatment comprising the administering the same agent.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 60-69, 71-73, 79-81 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for 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. This is a WRITTEN DESCRIPTION rejection.
The claims are drawn to an antibody or antigen-binding fragment thereof capable of specifically recognizing TrkA, wherein the antibody comprises a CDR sequence selected from the instantly claimed sequences. The claims further recite “..an amino acid having at least 95% identity” with the claimed sequences. Thus, the written description is directed to the following:
the antibody, comprises “a” CDR sequences selected from the following; the claim as written is directed to an antibody comprising any single CDR of any heavy or light chain variable region to be used together;
the claim does not specify that any of the indicated heavy chain variable regions have to be used with any light chain variable regions.
the claim recites any antigen binding fragment without being drawn to any of the instantly claimed CDRs. The claim recites that the “antibody” comprises a CDR sequence.
the partial structure of the claims, wherein the sequences can have up to a 5% discrepancy from the disclosed SEQ ID Nos.
The instant specification discloses full and specific sequences of heavy chain and light chain CDRs that are used together [see at least pg 16]. However, does not disclose that any set of heavy chain CDR sets can be used interchangeably with any light chain CDRs, does not disclose the use of an antibody fragment, and does not disclose does not disclose any representative variants of the antibody that recognizes TrkA with less than 100% SEQ ID Nos.
By the time of the filing of the instant application, it was well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33; (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1). Humanized antibodies comprise only the CDRs, or in some cases an abbreviated subset of residues within the CDRs, of a parental rodent antibody in the context of human framework sequences. Id. at Section 4. All of the CDRs of the heavy and light chain, in their proper order of CDR1, then 2, then 3, and in the context of framework sequences which maintain their required conformation are generally required to produce a humanized antibody in which the heavy and light chains associate to form an antigen-binding region that binds the same antigen as the parental rodent antibody. Id. at Section 4.
Antibody binding to the same antigen, or even the same epitope on that antigen, can be accomplished with an impressively wide variety of antibody structures, even when the antibodies are limited to those from a particular source (Gershoni et al., Epitope Mapping, Biodrugs 2007; 21 (3): 145-156 page 146 section 1.1). The skilled artisan therefore understood that antibodies from a variety of different sources may bind the same antigen and even mediate the same functional effects, but differ widely in the details of the structure of their antigen-binding sites, particularly in the amino acid sequence and length of VH-CDR3.
Further, it is not possible to predict the amino acid sequence when an epitope is recited, because there are many different epitope arrangements, such as linear and discontinuous epitopes that is dictated by the unique interaction between an antibody and its cognate epitope (Blythe et al., Benchmarking B cell epitope prediction: Underperformance of existing methods, Protein Science (2005), 14:246–248 pg. 246) . 3D structural analyses of antibody-epitope binding highlighting that the deficiency in the ability to predict the structural features of an antibody when the epitope is disclosed (Schreiber et al.,3D-Epitope-Explorer (3DEX): Localization of Conformational Epitopes within Three-Dimensional Structures of Proteins, Wiley Interscience, 2005 42–44, 60596, page 879).
Furthermore, changes in amino acid structures, particularly in CDR regions, can have impacts on antigen binding that are unpredictable. Rabia et al (Understanding and overcoming trade-offs between antibody affinity, specificity, stability and solubility. Biochemical engineering journal, 137, 365–374, 2018) and Vajdos et al (Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis. Journal of molecular biology, 320(2), 415–428, 2022) teaches that changes to CDRs are unpredictable in terms of affinity, specificity, and solubility, (see Rabia whole documents), and teaches that even minute changes to the CDR region can impact binding affinities. (see Figure 2, effects of CDR mutations on binding affinity), respectively. Rudikoff et al (Single amino acid substitution altering antigen-binding specificity. Proc Natl Acad Sci U S A. 1982 Mar;79(6):1979-83) teaches that single amino acid substitutions alter antigen-binding specificity. [Abstract] L stly, Herold et al (Sci Rep. 2017 Sep 25;7(1):12276) teaches and demonstrates that single and double mutations in exemplary antibodies, and found that single point mutations in the VH CDR region can completely abolish antigen binding. [see pg 8]
The structure activity relationship of the CDR antigen binding region that recognizes TrKA is not known and the binding epitopes cannot be predicted based on the antibody sequences. Walsh et al (A tale of two TrkA inhibitor trials: same target, divergent results. Osteoarthritis Cartilage. 2019;27(11):1575-1577) teaches the challenges of targeting TrkA. Walsh teaches and that although it is a promising therapeutic target, there needs to be more biologic insight into the mechanisms of the agents, and due to pharmacological differences no two agents can produce the same result. [whole document]
To provide adequate written description and evidence of possession of the claimed composition antibody genus, the instant specification can structurally describe representative antibodies or antigen binding fragments, that function to recognize TrkA and treating functions as claimed, or describe structural features common to the members of the genus, which features constitute a substantial portion of the genus. Alternatively, the specification can show that the claimed invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics (see University of California v. Eli Lilly and Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997) and Enzo Biochem, Inc. V. Gen-Probe Inc.). A disclosure that does not adequately describe a product itself logically cannot adequately describe a method of using that product.
Although Applicants may argue that it is possible to screen for antibodies that function as claimed, the court found in (Rochester v. Searle, 358 F.3d 916, Fed Cir., 2004) that screening assays are not sufficient to provide adequate written description for an invention because they are merely a wish or plan for obtaining the claimed chemical invention. “As we held in Lilly, “[a]n adequate written description of a DNA … ‘requires a precise definition, such as by structure, formula, chemical name, or physical properties,’ not a mere wish or plan for obtaining the claimed chemical invention.” 119 F.3d at 1566 (quoting Fiers, 984 F.2d at 1171). For reasons stated above, that requirement applies just as well to non-DNA (or RNA) chemical inventions.” Knowledge of screening methods provides no information about the structure of any future antibodies yet to be discovered that may function as claimed. The TrkA antigen provides no information about the structure of an antibody inhibits it.
Applicants have not established any reasonable structure-function correlation with regards to the sequences of the claimed antibody that can be altered and still maintain function. Therefore, one could not readily envision members of the broadly claimed genus.
Given the lack of representative examples to support the full scope of the claimed antibodies that inhibit one or more activities of TrkA, and lack of reasonable structure-function correlation with regards to the unknown sequences in the variable domains or CDRs of the antibodies that function as claimed, the present claims lack adequate written description. Thus, the specification does not provide an adequate written description of antibodies that is required to practice the claimed invention. Since the specification fails to adequately describe the product to which the claimed method uses, it also fails to adequately describe the method.
Claims 71, 72, 76, and 77 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 treating pain, does not reasonably provide enablement for treating and preventing all the diseases and disorders listed in claims. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to practice the invention commensurate in scope with these claims.
BREADTH OF THE CLAIMS: Claims 71 and 76 recites a method of treating or preventing pain, cancer, inflammation or inflammatory diseases, neurodegenerative diseases, Sjogren's syndrome, endometriosis, diabetic peripheral neuropathy, prostatitis, pelvic pain syndrome, diseases related to imbalance in the regulation of bone remodeling and diseases caused by abnormal signaling of connective tissue growth factor in a subject, comprising administering the claimed antibody or antigen binding fragment. Claims 72 and 77 recites a method of treating or preventing neuropathic pain inflammatory pain, cancer-related pain, fracture-related pain, surgery-related pain, inflammatory lung disease, interstitial cystitis, painful bladder syndrome, inflammatory bowel disease, inflammatory skin disease, Raynaud's syndrome, idiopathic pulmonary fibrosis, scar (hypertrophy, keloid type and other forms), sclerosis, endocardial myocardial fibrosis, atrial fibrosis, bone marrow fibrosis, progressive massive fibrosis (lung), renal-derived systemic fibrosis, scleroderma, systemic sclerosis, joint fibrosis, ocular fibrosis, non-small cell lung cancer, papillary thyroid cancer, glioblastoma multiforme, colorectal cancer, melanoma, bile duct cancer or sarcoma, acute myeloid leukemia, large cell neuroendocrine cancer, neuroblastoma, prostate cancer, pancreatic cancer, melanoma, head and neck squamous cell carcinoma or gastric cancer in a subject, comprising administering the claimed antibody or antibody binding fragment.
PRESENCE OR ABSENCE OF EXAMPLES: The instant specification discloses the use of an antibody that recognized TrkA for the treatment of pain only, as demonstrated in Examples 17 and 18. Example 17 summary states that the antibody is effective for chronic pain in a formalin-induced pain model, whereas Example 18 states that that the antibody resulted in analgesic effects in a Freund’s adjuvant-induced inflammatory pain model. The specification does not provide any examples of the claimed antibody for the treatment of prevention of cancer, inflammation or inflammatory diseases, neurodegenerative diseases, Sjogren's syndrome, endometriosis, diabetic peripheral neuropathy, prostatitis, pelvic pain syndrome, diseases related to imbalance in the regulation of bone remodeling and diseases caused by abnormal signaling of connective tissue growth factor in a subject, inflammatory lung disease, interstitial cystitis, painful bladder syndrome, inflammatory bowel disease, inflammatory skin disease, Raynaud's syndrome, idiopathic pulmonary fibrosis, scar (hypertrophy, keloid type and other forms), sclerosis, endocardial myocardial fibrosis, atrial fibrosis, bone marrow fibrosis, progressive massive fibrosis (lung), renal-derived systemic fibrosis, scleroderma, systemic sclerosis, joint fibrosis, ocular fibrosis, non-small cell lung cancer, papillary thyroid cancer, glioblastoma multiforme, colorectal cancer, melanoma, bile duct cancer or sarcoma, acute myeloid leukemia, large cell neuroendocrine cancer, neuroblastoma, prostate cancer, pancreatic cancer, melanoma, or head and neck squamous cell carcinoma or gastric cancer in a subject.
STATE OF THE ART: A search of relevant art discloses that targeting TrkA can result in the treatment of pain. Ugolini et 2007 (The function neutralizing anti-TrkA antibody MNAC13 reduces inflammatory and neuropathic pain. Proc Natl Acad Sci U S A. 2007;104(8):2985-2990) that teaches that NGF (nerve growth factor) exerts its biological functions by TrkA (tyrosine kinase A) receptor, and that NGF is a peripherally produced mediator of persistent pain sites, including those associated with inflammation. Urgolini teaches the use of MNAC13, an anti-TrkA monoclonal antibody, that can be used to target TrkA signaling. Ugolini teaches that the antibody resulted in potent analgesic effects in inflammatory and chronic pain. [Abstract] Walsh et al (A tale of two TrkA inhibitor trials: same target, divergent results. Osteoarthritis Cartilage. 2019;27(11):1575-1577) also teaches the role of NGF and TrkA in the role of pain.
However, the art does not reveal any demonstration that targeting TrKA can treat or prevent any other of the claimed disease and disorders.
With regards to anti-cancer therapy, it is well known that the art of anti-cancer therapy is highly unpredictable, for example, Gura (Science, 1997, 278:1041-1042) teaches that researchers face the problem of sifting through potential anticancer agents to find ones promising enough to make human clinical trials worthwhile and teach that since formal screening began in 1955, many thousands of drugs have shown activity in either cell or animal models that only 29 have actually been shown to be useful for chemotherapy See p. 1041, see 1st and 2nd para. Furthermore, Kaiser (Science, 2006, 313: 1370) teaches that 90% of tumor drugs fail in patients. See 3rd col., 2nd to last para. Additionally Chames et al (British J. of Pharmacology, 2009, 157, 220-233) teach that there are several challenges to development therapeutic antibodies. These challenges include functional limitations such as inadequate pharmacokinetics, tissue accessibility and impaired interactions with the immune system (Abstract). Additionally, Chames teaches several limitations of therapeutic antibodies such as affinity between the antibody and its antigen, competition with patient’s IgG, and efficiency issues in triggering the immune response (pages 224-225). With regards to prevention of cancer, Cancer has a wide variety of causes, from environmental and/or developmental exposure to ionizing radiation and/or chemical exposure in addition to some types viral and bacterial exposure (Lichtman MA et al. The Oncologist 2017; 22(5); 542–548). Even though cancer is featured by the infinite cell proliferation, its pathogenesis is extremely complex and related to many mechanisms. In general, the hallmarks of cancer consist of ten biological capabilities during the development of cancers, namely sustaining proliferative signaling, evading growth suppressors, resisting cell death, enabling replicative immortality, inducing angiogenesis, activating invasion and metastasis, tumor-promoting inflammation, genome instability and mutation, evading immune destruction and reprogramming energy metabolism (Hanahan D et al. Cell 2011 144(5) p646-674, Figures 1 and 3). More than 100 types of cancer have been identified which are typically termed for the organs or tissues where they occur. Hanahan taught over the past decade, tumors have increasingly been recognized as organs whose complexity approaches and may even exceed that of normal healthy tissues (page 661, right column second to last paragraph). Hanahan taught many human tumors are histopathologically diverse, containing regions demarcated by various degrees of differentiation, proliferation, vascularity, inflammation, and/or invasiveness (page 662, left column, first paragraph). Szabo et al (Selecting targets for cancer prevention: where do we go from here? Nat Rev Cancer 6, 867–874; 2006) teaches the intricacies and complications of cancer prevention. Szabo teaches that in addition to efficacy and toxicity concerns of cancer drugs targeting functions, there are a number of practical issues that should be considered, including drug formulation and dosing schedule to ensure adherence, as well as the cost. Szabo also teaches that in some cases the targets selected for drug therapy may even cause harm. [Whole document] Clinical trials aimed at proving preventative cancer activity attributable to a specific intervention are largely infeasible, due to the impossibly large number of subjects and an equally impossible long timeframe. Although cancer is a common disease, specific types of cancer are still relatively infrequent events in an otherwise healthy population. Therefore, trials with cancer incidence as endpoints would necessarily involve several thousands of subjects followed for several decades. Such logistic difficulties have precluded cancer prevention trials with cancer incidence as an endpoint in all but a selected few malignancies for treatments such as tamoxifen and finasteride (Lee KW et al. Nature Reviews Cancer 2011 11 211-218, page 211, left column last paragraph)
PREDICITABILITY: The specification lacks the critical steps necessary in presenting some type of predictable response in a population of hosts deemed necessary to prevent all the claimed disorders and diseases. There is no evidence in the instant application or the art that as noted in the prior that demonstrate that a drug that treats a disease or disorder, including cancer, would prevent its onset in subjects as claimed. The amount of experimentation to require to formulate such guidance would be enormous; one would have to demonstrate the efficacy of the agent in several models across several different types of diseases for use of the agent or composition in a preventative and treatment setting. Further, one would have to conduct population analysis to identify definitive characteristics which indicate that a subject is at risk of developing any disease, or cancer, to a degree that would outweigh potential adverse effects of treatment with the claimed composition. Each disease state encompassed within the claim varies at minimum the expression, pathophysiology, organ affected, whether it’s genetic, metabolic, infectious, and time to expression. Thus, considering the high level of skill in the art, the state of the art, the level of predictability, and the guidance and examples provided, the experimentation required to enable the full scope of the claimed invention would not be reasonable.
QUANTITY OF EXPERIMENTATION: Undue experimentation would be required to determine claimed agent is administered to which population of subjects could predictably treat and prevent each disorder claimed. MPEP 2164.01 recites that “The test of enablement is not whether any experimentation is necessary, but whether, if experimentation is necessary, it is undue. In re Angstadt, 537 F.2d 498, 504, 190 USPQ 214, 219 (CCPA 1976)”. The experimentation needed to practice this method is undue and unreasonable as it requires determining whether the claimed antibodies treats and prevents as claimed. A person skilled in the art will not be able to use the invention without undue experimentation. (In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988))
Accordingly, the instant claims do not comply with the enablement requirement of §112, since to practice the invention claimed in the patent a person of ordinary skill in the art would have to engage in undue experimentation, with no assurance of success.
Claims 76 and 77 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 treatment of pain comprising administering the claimed nucleic acid that encodes both a heavy chain and a light chain, does not reasonably provide enablement for treatment of pain comprising administering a nucleic acid that encodes only a heavy chain of the claimed antibody. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to practice the invention commensurate in scope with these claims.
BREADTH OF THE CLAIMS: The claims are drawn to methods of treatment comprising the nucleic acid molecule according to claim 67. Claim 67 is drawn to a nucleic acid molecule wherein the nucleic acid molecule encodes a heavy chain of the antibody or the antigen-binding fragment thereof of claim 60.
PRESENCE OR ABSENCE OF EXAMPLES: The instant specification discloses the uses and production of antibodies that recognized TrkA with both a heavy chain and light chains. There is no example use of a nucleic acid encoding only the heavy chain of the antibody.
STATE OF THE ART: It is well known in the art that full structures of antibodies are needed for function and that any changes in amino acid structures can have impacts on antigen binding that are unpredictable. Rabia et al (Understanding and overcoming trade-offs between antibody affinity, specificity, stability and solubility. Biochemical engineering journal, 137, 365–374, 2018) and Vajdos et al (Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis. Journal of molecular biology, 320(2), 415–428, 2022) both teach that changes to the structure unpredictable in terms of affinity, specificity, and solubility, (see Rabia whole documents), and teaches that even minute changes to the CDR region can impact binding affinities. (see Figure 2, effects of CDR mutations on binding affinity), respectively. Thus, without knowing the complete structure of the antibody, it does not provide any support that the antibody will be have the same function properties.
PREDICITABILITY: The specification lacks the critical steps necessary in presenting some type of predictable response in a population of hosts deemed necessary to treat all the claimed disorders comprising administering a nucleic acid that only encodes the heavy chain of the antibody. There is no evidence in the instant application or the art that as noted in the prior that would function as claimed. demonstrate that a drug that treats a disease or disorder, including cancer, would prevent its onset in subjects as claimed. Thus, considering the high level of skill in the art, the state of the art, the level of predictability, and the guidance and examples provided, the experimentation required to enable the full scope of the claimed invention would not be reasonable.
QUANTITY OF EXPERIMENTATION: Undue experimentation would be required to determine claimed agent is administered to which population of subjects could treat as claimed. MPEP 2164.01 recites that “The test of enablement is not whether any experimentation is necessary, but whether, if experimentation is necessary, it is undue. In re Angstadt, 537 F.2d 498, 504, 190 USPQ 214, 219 (CCPA 1976)”. The experimentation needed to practice this method is undue and unreasonable as it requires determining whether the claimed nucleic acid encoding only the heavy chain treats as claimed. A person skilled in the art will not be able to use the invention without undue experimentation. (In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988))
Accordingly, the instant claims do not comply with the enablement requirement of §112, since to practice the invention claimed in the patent a person of ordinary skill in the art would have to engage in undue experimentation, with no assurance of success.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 66 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 66 is drawn to the antibody or antigen-binding fragment thereof according to claim 60, wherein “the antibody is a single chain antibody fragment.” Claim 60 is drawn to an antibody or antigen-binding fragment. The specification defines an antibody as an immunoglobulin molecule capable of binding to a specific antigen and consists of two lighter molecule weight light chains and two heavier molecule weight heavy chains. [see pg 220 of the instant specification] Based on the definition provided of an antibody, “a single chain antibody” falls within the scope of an “antibody”. However, claim 66 states that the antibody is drawn to a “single chain antibody fragment”, and therefore does not further limit the antibody of claim 60 as it changes the definition of what is included by reference to “an antibody”. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
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 60-69, 71-73, 79-81 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 35-48, 50, 52 and 53 of copending Application No. 17/911,571 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the co-pending application is drawn to an antibody or antigen-binding fragment that recognizes TrkA, in which the antibody comprises the instantly claimed sequences. The co-pending application also recites methods of treatment comprising administering the instantly claimed antibody.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
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/SARAH A ALSOMAIRY/ Examiner, Art Unit 1646
/Zachariah Lucas/ Supervisory Patent Examiner, Art Unit 1600