DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Priority
The instant application, filed 12/06/2023, is a 371 filing of PCT/JP2021/048612, filed 12/27/2021, and claims foreign priority to JP2021-089040, filed 05/27/2021, and JP2020-218091, filed 12/27/2020.
Status of Claims/Application
Applicant’s preliminary amendment of 12/06/2023 is acknowledged. Claims 2 and 4-7 are amended; claims 1, 3, and 8-16 are cancelled; and claims 17-28 are new. Claims 2, 4-7, and 17-28 are currently pending and are examined on the merits herein.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 06/26/2023 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered by the examiner.
Nucleotide and/or Amino Acid Sequence Disclosures
The Incorporation by Reference paragraph required by 37 CFR 1.821(c)(1) is missing. See item 1) a) or 1) b) below.
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency - The Incorporation by Reference paragraph required by 37 CFR 1.821(c)(1) is missing or incomplete. See item 1) a) or 1) b) above.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required incorporation-by-reference paragraph, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Claim Interpretation
The instant claims encompass compositions for nerve outgrowth and methods of treating nerve injury in “postnatal” mammalian individuals. In the art, “postnatal” is commonly associated with the period of time immediately following child birth. In the instant office action; however, the recitation of “postnatal” in the claims is interpreted to mean any time after birth, including elderly individuals.
This interpretation is based on, for instance, claim 21, which states that “the postnatal mammalian individual is an elderly individual”. The instant specification, for instance, paragraph [0052] also suggests that postnatal encompasses elderly individuals. For instance, stating “the central nervous system and the peripheral nervous system in the elderly are under a condition in which an effective amount of GDNF is not present. Thus, the neurite outgrowth-promoting agent for neurons of postnatal mammalian individuals for use under a condition in which an effective amount of GDNF is not present can be used as a pharmaceutical composition for inducing nerve regeneration for treatment of injury in the central nerve system and for treatment of nerve injury in the elderly.”
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 2 and 5-7 are rejected under 35 U.S.C. 103 as being unpatentable over Mikaels-Edman, A., et al (2003) Soluble and bound forms of GFRα1 elicit different GDNF-Independent neurite growth responses in primary sensory neurons Developmental dynamics 227; 27-34.
Edman teaches that several studies have shown that GDNF and GFRαs are important for neurite growth and are expressed during nerve growth and targeting innervation in the developing sensory nervous system. Edman further teaches that both GDNF and GFRα1 are markedly up-regulated after sciatic nerve lesion in Schwann cells along the path of nerve regeneration and that GFRα1 can be released by the action of membrane proteases or phospholipases. Based on these findings, two non-cell autonomous modes of so-called action in trans of GFRαs have been proposed. GFRα1 present on the membrane of Schwann cells can interact with growing nerves and, alternatively, GFRα1 can be released from the Schwann cell and interact with the nerve in a soluble form (page 28, column 1, paragraph 1).
Edman teaches that previous studies on the roles of broadly expressed GFRα1 on nerve growth have been limited to its role as a GDNF co-receptor. In the studies provided by Edman, Bax -/- neurons were used allowing for the characterization of the effects of GDNF and soluble or bound forms of GFRα1, referenced as sGFRα1 and bGFRα1, respectively, on neurite growth (page 28, paragraph bridging columns 1 and 2). Edman also teaches that the studies have included postnatal and rat studies (paragraph bridging pages 27-28; page 30, left column, paragraph 2).
Edman teaches that previous studies support an important role of GFRα1 in trans for neuronal growth and guidance. Therefore, Edman studied the biological significance of stimulation in trans by GFRα1 by studying the effect of soluble or bound GFRα1 on neurite length in the presence or absence of GDNF. Neurons grown in the presence of soluble GFRα1 displayed a significant shift toward shorter neurites. Of interest, this effect was neutralized by the addition of GDNF. sGFRα1 was then used at a concentration of 300 ng/ml and, to evaluate the putative effect of endogenously produced GDNF, neutralizing antibodies against GDNF were added, which did not alter the effect of sGFRα1 (page 28, column 3, paragraph 2 – page 29, column 2, paragraph 1; Fig. 2).
DRG neurons were then cultured with GFRα1 immobilized on the surface of the culture dish. Bound GFRα1, in the absence of GDNF, led to extension of neurites leading to an overall increase in length. This effect of GFRα1 was partially neutralized by the addition of GDNF (Fig. 3) (page 29, right column, paragraph 1). It is noted that the immobilization of GFRα1 on the surface of the culture dish meets the instant claim 5 limitation of the protein being retained on a carrier per the instant specification, page 20, [0048], which states that examples of the carrier that retains GFRα1 include culture substrates such as well plates and petri dishes.
Edman further studied whether the effects of both sGFRα1 and bGFRα1 are limited to neurons cultured on laminin that interact with α1β1 integrin by culturing the neurons on fibronectin. Neurons cultured on fibronectin (binding α5β1 integrin) showed an overall smaller neurite growth compared to those on laminin. Edman teaches that these results are consistent with studies in which neural crest and sensory neurons primarily use α1β1 integrin for migration and neurite outgrowth. sGFRα1 and bGFRα1 elicited similar responses on fibronectin as on laminin. Neurons grown only in the presence of sGFRα1 displayed a shift towards shorter neurites and those on bGFRα1 significantly longer neurites. These effects were reversed by GDNF (page 29, right column, paragraph 2).
Edman teaches that, in agreement with the conclusion that GFRα1 also elicits neurite growth activity in the absence of GDNF, neutralizing antibodies against GDNF did not alter the effect of sGFRα1. Furthermore, anti-GDNF antibodies added alone to the cultures did not have any effect compared with controls without any addition of factor. These results show that GFRα1 may signal without GDNF and that this signaling controls neurite growth (page 31, column 1, paragraph 1).
Edman teaches that the findings suggest that GFRα1 might be involved in nerve regeneration. Supporting evidence for this notion was found in a recent study where cultured neuronal cells, Schwann cells, and injured sciatic nerve were shown to release biologically active soluble GFRα1 to the extracellular space, which indicates a naturally occurring release of this molecule in vivo and a biological relevance of trans activation by GFRα1 (page 31, column 3). The results presented confirm and extend previous findings and show that GFRα1 presented as an artificial target in either soluble or bound form markedly affects neurite outgrowth independent of GDNF. Thus, there is biochemical and functional evidence that GFRα1 in soluble and bound form can influence neurite growth (page 32, column 1, paragraph 1).
In the studies performed, Edman used GFRα1-Fc and anti-rhGDNF neutralizing antibodies (page 33, column 1, paragraph 3).
It would have been prima facie obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to modify the compositions disclosed by Edman to arrive at a composition comprising soluble or immobilized GFRα1 and anti-GDNF antibodies based on the teachings of Edman as a whole. An ordinarily skilled artisan would have been motivated to produce a composition comprising both GFRα1 and the anti-GDNF antibody as Edman demonstrates that GFRα1 elicits nerve growth responses independent of GDNF and that, GDNF, in the presence of soluble or immobilized GFRα1 reverses the GDNF-independent GFRα1 modulation of neurite growth. As such, an ordinarily skilled artisan would have had a reasonable expectation of success.
It is noted that, although Edman does teach that GFRα1 is involved neurite outgrowth, nerve regeneration, and teaches their role in postnatal mammals and injury, for instance in injured sciatic nerves, meeting the instant claim limitations, the limitations “for promoting neurite outgrowth for neurons of postnatal mammalian individuals” in claim 2 and “for inducing nerve regeneration” in claim 7 are intended use limitations. MPEP 2111.02 II states that “During examination, statements in the preamble reciting the purpose or intended use of the claimed invention must be evaluated to determine whether or not the recited purpose or intended use results in a structural difference (or, in the case of process claims, manipulative difference) between the claimed invention and the prior art. If so, the recitation serves to limit the claim. See, e.g., In re Otto, 312 F.2d 937, 938, 136 USPQ 458, 459 (CCPA 1963)… To satisfy an intended use limitation which is limiting, a prior art structure which is capable of performing the intended use as recited in the preamble meets the claim. See, e.g., In re Schreiber, 128 F.3d 1473, 1477, 44 USPQ2d 1429, 1431 (Fed. Cir. 1997).” As the composition disclosed by Edman would be capable of performing the claimed intended use, the composition meets the instant claim limitations.
Claims 4 and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Mikaels-Edman, A., et al (2003) Soluble and bound forms of GFRα1 elicit different GDNF-Independent neurite growth responses in primary sensory neurons Developmental dynamics 227; 27-34 as applied to claims 2, and 5 above, and in further view of US 2006/0166325 A1 (Fox, G.M., et al) 27 Jul 2006 and UniProt P56159; GDNF family receptor alpha-1; GFRA1_Human; entered 11-DEC 2019.
Edman teaches the compositions of claim 2 and 5 as discussed in detail above.
As discussed in detail above, Edman teaches compositions comprising GFRα1 and also teaches that the GFRα1 can be immobilized, indicating that the GFRα1 is retained on a carrier.
Edman; however, does not disclose that the GFRα1 comprises an amino acid sequence recited in claim 4 nor does Edman teach that the carrier is a biocompatible medical material as recited in claim 17.
US’325 teaches the cloning and characterization of a high affinity receptor for GDNF, called GDNFR, which was the first known component of the receptor system. Nucleic acid sequences are also described for GDNFR protein products (abstract).
US’325 teaches that, in contrast to the extensive studies on the distribution and bioactivity of GDNF, there have been no reports on the identification of a receptor or receptors that mediate binding of GDNF to a cell and thereby mediate intracellular signaling and a cell response. The disclosure is based on the discovery of a high affinity receptor first found on the surface of cultured retinal cells from postnatal rats. The receptor possesses an estimated GDNF binding affinity comparable to that found on receptors in dopaminergic and motor neurons; midbrain dopaminergic neurons; and facial and spinal cord motor neurons (page 5, [0043]).
US’325 teaches nucleic acid sequences which encode a neurotrophic factor receptor protein having the amino acid sequences depicted in Figs 2 and 4 of SEQ ID NOs: 2 and 4 as well as biologically equivalent analogs. GDNFR protein products are typically provided as a soluble receptor protein and in a substantially purified form (page 3, [0014]). US’325 teaches the production of GDNFR protein products by recombinant engineering techniques or synthesized by chemical techniques (page 3, [0015]). US’325, SEQ ID NO: 2 is identical to instant SEQ ID NO: 1 as shown in the ABSS alignment below:
PNG
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694
610
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Greyscale
US’325 further teaches pharmaceutical compositions comprising the GDNFR protein product which typically include a therapeutically effective amount of GDNFR protein product in a mixture with one or more pharmaceutically or physiologically acceptable formulation materials selected for suitability with the mode of administration. The term “pharmaceutically acceptable carrier” or “physiologically acceptable carrier” refers to a formulation material suitable for accomplishing or enhancing the delivery of the GDNFR protein product as a pharmaceutical composition (page 20, [0164]). US’325 teaches GDNFR protein products in pharmaceutically acceptable compositions including particulate preparations of polymeric compounds such as polylactic acid, polyglycolic acid, etc. or into liposomes. Hyaluronic acid may also be used (page 21, [0168]).
US’325 further teaches that the GNFR protein product can also be employed, alone or in combination with other growth factors, in the treatment of nerve diseases. US’325 teaches nerve diseases including nerve damage caused by (1) physical injury, which causes the degeneration of the axonal processes and/or nerve cell bodies near the site of injury; (2) temporal or permanent cessation of blood flow to parts of the nervous system, as in a stroke; (3) intentional or accidental exposure to neurotoxin such as chemotherapeutic agents; (4) chronic or metabolic diseases, such as diabetes or renal dysfunction; or (5) neurodegenerative diseases such as Parkinson’s disease, Alzheimer’s disease, and amyotrophic lateral sclerosis (ALS) which result from the degeneration of specific neuronal populations (pages 1-2, [0007]). US’325 also teaches that conditions that will benefit from GDNFR include, but are not limited to, motor neuron disorders including amyotrophic lateral sclerosis, neurological disorders associated with diabetes, Parkinson’s disease, Alzheimer’s disease, and Huntington’s chorea. US’325 also teaches the treatment of glaucoma sensory neuropathy caused by injury to, insults to, or degeneration of, sensory neurons, as well as pathological conditions, such as inherited retinal degenerations and age (page 8, [0067]).
UniProt_P56159 teaches a human GFRα1 protein sequence (pages 6-7), which is the same as the sequence above disclosed by US’325, demonstrating that the sequence disclosed by US’325 is an art recognized GFRα1 protein sequence.
It would have been prima facie obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to substitute the GFRα1 protein disclosed by Edman with the GDNFR protein disclosed by US’325 as supported by UniProt_P56159 and to use a biocompatible medical material, such as polymeric compounds including polylactic acid, polyglycolic acid, etc, or liposomes, to immobilize the protein as disclosed by US’325.
It would have been obvious to substitute the GFRα1 protein disclosed by Edman with the GDNFR protein taught by US’325 as US’325 teaches the protein as being suitable for administration in either soluble or immobilized form for the treatment of nerve diseases including those related to nerve degeneration. It would also have been obvious to use one of the polymeric compounds disclosed by US’325 to immobilize the GFRα1 protein in Edman as US’325 teaches that these materials are pharmaceutically acceptable materials for use in compositions used for the delivery of the GDNFR proteins. An ordinarily skilled artisan would have had a reasonable expectation of success in making these modifications to Edman as UniProt demonstrates that the GDNFR sequence taught by US’325 is a GFRα1 protein indicating that it would function in the compositions disclosed by Edman.
Claims 2, 4-7, and 17-28 are rejected under 35 U.S.C. 103 as being unpatentable over Xie, F., et al (2018) Glial cell line-derived neurotrophic factor (GDNF) attenuates the peripheral neuromuscular dysfunction without inhibiting the activation of spinal microglia/monocyte BMC geriatrics 18(110); 1-9 in view of US 2006/0166325 A1 (Fox, G.M., et al) 27 Jul 2006, UniProt P56159; GDNF family receptor alpha-1; GFRA1_Human; entered 11-DEC 2019, and Mikaels-Edman, A., et al (2003) Soluble and bound forms of GFRα1 elicit different GDNF-Independent neurite growth responses in primary sensory neurons Developmental dynamics 227; 27-34.
Xie teaches that skeletal muscle dysfunction, which manifests as acquired muscle weakness and a reduced capacity to continue muscle contractions, and other neurodegenerations, are observed in many elderly individuals. Historically, studies have shown that neuromuscular dysfunction was found in advanced age, and the demyelation of sciatic nerve is a factor. Although the peripheral motor nerve plays an important role in muscular function, the central nervous system also contributes to muscular function in elderly individuals (page 2, left column, paragraph 1). The blood-spinal cord barrier is injured more often in the aging spinal cord than the adult spinal cord, which is associated with increased cytokine levels (page 2, left column, paragraph 2).
It was shown that GDNF is a very potent trophic factor for spinal motorneurons and central noradrenergic neurons. Therefore, GDNF raised great expectations as a potential therapeutic agent for the treatment of neurodegenerative diseases. GDNF has a significant effect on the remyelation of neurons following spinal cord injury. Recently, the effect of GDNF on the regeneration of the peripheral nerve has been tested in some models of nerve injury (page 2, left column, paragraph 3).
Xie demonstrates with western blotting that the protein expression of NRG-1, GDNF, and GFRα1 were significantly decreased in the aged group studied (page 5, right column, paragraph 2; Fig. 4b). Xie further teaches that the protein expression of GFRα1 was significantly increased in GDNF treated groups (paragraph bridging pages 5-6). Xie teaches that the insufficient level of GDNF could be one of the factors that induces neuromuscular dysfunction in aged rats (page 6, paragraph bridging columns).
Xie teaches that previous studies also suggested that normal healthy aging is accompanied by neuroinflammation which enhances susceptibility to neurodegradation. Additionally, the ability of senescent CNS to react to deleterious neurotoxic responses is decreased following injury, infection, or stress (page 7, left column, paragraph 2).
The teachings of Xie suggest significantly decreased expression of GDNF and GFRα1 in advanced age and teaches that there is an insufficient level of GDNF in aged rats which leads to neuromuscular dysfunction. Xie also teaches the importance of the GDNF pathway in treating CNS and peripheral nerve injury. Xie; however, does not disclose a method of treating these injuries, in which there is an insufficient level of GDNF, with at least one protein claimed in a) to d).
The teachings of US’325, UniProt_P56159, and Edman are as discussed above.
It would have been prima facie obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to treat the CNS and peripheral nerve injuries in aged subjects, in which there is an insufficient level of GDNF and low expression of both GDNF and GFRα1, as disclosed by Xie, using the methods taught by US’325, in which a GDNFR protein, which is the same as GFRα1 according to UniProt_P56159, is administered for the treatment of nerve disease, as is further motivated by Edman. An ordinarily skilled artisan would have been motivated to administer the GFRα1 protein of US’325 to this patient population based on the teachings of Edman which demonstrates that soluble and bound forms of GFRα1 elicit GDNF-independent neurite growth response in primary sensory neurons and that GFRα1 can function as a nerve growth cue eliciting neurite growth activity even in the absence of GDNF. Thus, an ordinarily skilled artisan would have had a reasonable expectation of success in treating the patient population of Xie which have CNS or peripheral nerve injuries with insufficient expression of GDNF. Additionally, US’325 teaches that GFRα1 administration can benefit conditions including CNS disorders as well as sensory neuropathy caused by injury to, insults to, or degeneration of, sensory neurons and Edman also teaches that GFRα1 is involved in nerve regeneration and teaches that recent studies had shown that cultured neuronal cells, Schwann cells, and injured sciatic nerve release biologically active soluble GFRα1 into the extracellular space, demonstrating the biological relevance of trans activation by GFRα1.
Regarding claim 22, as discussed in detail above, Edman teaches that GFRα1 signals without GDNF and that this signaling controls neurite outgrowth. Edman also teaches that GDNF can reverse the effect of GFRα1 on neurite growth. Edman also demonstrates the effects of GFRα1 on neurite outgrowth in the presence of an anti-GDNF neutralizing antibody (page 31, column 1, paragraph 1; page 29, columns 2 and 3).
It would have been prima facie obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to modify the method taught by the combination of Xie, US’325, UniProt_P56159, and Edman to further administer an anti-GDNF neutralizing antibody based on the teachings of Edman. An ordinarily skilled artisan would have been motivated to further administer an anti-GDNF antibody as Edman demonstrates that GFRα1 elicits nerve growth responses independent of GDNF and that, GDNF, in the presence of soluble or immobilized GFRα1, reverses the GDNF-independent GFRα1 modulation of neurite growth. As such, an ordinarily skilled artisan would have had a reasonable expectation of success.
Conclusion
No claims are allowed.
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/AUDREY L BUTTICE/Examiner, Art Unit 1647
/SCARLETT Y GOON/Supervisory Patent Examiner
Art Unit 1693
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