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 .
Status of the Claims
The preliminary amendment filed 01/02/2024 is acknowledged. Claims 1-8 are canceled and claims 9-16 are new. No restriction is being imposed in this case. Claims 9-16 are under examination.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 365(c) is acknowledged. The priority date of claims 9-16 is 08/19/2022, the filing date of PCT/KR2022/012416.
Claim Objections
Claim 12 is objected to because of the following informalities. Claim 12 recites the “osmotic protein”, but presumably the “osmotin protein” was intended. Appropriate correction is required.
Claim Rejections - 35 USC § 112(a)
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 9-16 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for methods of ameliorating or treating Parkinson’s disease comprising administering a composition comprising an osmotin protein,
wherein the osmotin protein has at least 95% sequence identity to instant SEQ ID NO: 1; or alternatively
wherein the osmotin is a wild type osmotin from Nicotiana tabacum, Citrus sinensis, Rosa roxburghii, Solanum tuberosum, Piper colubrinum, Ricinus communis, or Arabidopsis thaliana, or alternatively
wherein the osmotin is an osmotin-derived peptide having the sequence CTQGPCGPT (as set forth in the prior art);
does not reasonably provide enablement for the claims as broadly recited. 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 or use the invention commensurate in scope with these claims.
There are many factors to be considered when determining whether there is sufficient evidence to support a determination that a disclosure does not satisfy the enablement requirement and whether any necessary experimentation is “undue.” (See In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 Fed. Cir. 1988). These factors include, but are not limited to: (a) the breadth of the claims; (b) the nature of the invention; (c) the state of the prior art; (d) the level of one of ordinary skill; (e) the level of predictability in the art; (f) the amount of direction provided by the inventor; (g) the existence of working examples; and (h) the quantity of experimentation needed to make or use the invention based on the content of the disclosure.
The claims are broad with respect to the osmotin protein, encompassing an embodiment in which no upper limit of residues may be substituted, deleted or inserted within the amino acid sequence of SEQ ID NO: 1. The instant specification teaches that administration of SEQ ID NO: 1 improved a number of endpoints in two separate mouse models of Parkinson’s disease, the MPTP-induced and NSE-haSyn transgenic mice. The improvements are summarized as follows:
Effect of Osmotin Treatment
Citation
Increased total distance traveled in the open field test
p. 18 and FIG 1
Reduced motor skill deficits and increased neuro-muscular strength
pages 18-19 and FIG 2
Restored TH levels
p. 19, FIG. 3
Increased TH-positive neurons in the SN pc and striatum of the MPTP-induced mice
pages 19-20, FIGs 4-5
Upregulated Nurr1, VMAT2, and DAT expression levels in the SNpc and striatum
p. 20, FIG 6
Upregulated Nurr1, DAT, VMAT2, and TH expression in MPP+-induced SH-SY5Y cells
p. 20, FIG 7
Decreased p-p38 expression and increased p-JNK and p-ERK expression
p. 20, FIG 8
Increased p-ERK/ERK and p-JNK/JNK ratios in MPP+/α-synuclein (A53T)-induced SH-SY5Y cells
p. 20-21, FIG 9
Reduced GFAP and Iba-1 expression
p. 21, FIGs. 10-11
Reduced reactive oxygen species (ROS)
p. 21, FIG 12
Reduced iNOS and COX-2 expression
p. 21, FIG 13
Increased cell viability
pages 21-22, FIG 14
Reduced Bax and cytochrome c expression and increased Bcl-2 and Bcl-xL expression
pages 22-23, FIGs 15-16 and 17C
Restored NeuN expression
p. 22, FIGs 17A-17B
Restored Nissl-stained neurons
p. 23, FIGs 18-19
Increased spine density and spine number
pages 23-24, FIGs 20-21
Increased PSD-95, SYP, SNAP-25 and CREB phosphorylation
pages 24-25, FIGs 22-23
Improved Morris Water Maze (MWM) test results
p. 25, FIG 24
The prior art discloses that wild-type osmotin may be administered to treat Parkinson’s disease (see claim 2; paragraphs [0018]-[0019] of US 2013/0210738). The ‘738 PGPUB discloses that osmotin is a stable 24 kDa protein and that they are referring to the naturally occurring protein “contained in ripe fruits of plants, for example, Nicotiana tabacum” (see paragraphs [0006] [0016]). Singh et al. (Plant Physiol. 90, 1096-1101, 1989—on IDS filed 01/02/2024) teach an osmotin protein derived from Nicotiana tabacum has >99% sequence identity (a conservative substitution at residue 129) to instant SEQ ID NO: 1 (see APPENDIX I for alignment), thus suggesting that osmotin proteins with high homology to SEQ ID NO: 1 are enabled. Finally, the PGPUB US 2018/0036365 teaches that an osmotin-derived peptide, CTQGPCGPT, may be administered to treat Parkinson's disease (see claims 13-15). Nevertheless, the evidence in the specification and the art is not commensurate with the broad scope of the recited osmotin protein, which encompasses up to a 100% divergence from SEQ ID NO: 1.
Miele et al. (PLoS One, 2011; 6: 1-11) provide structure to function support for an osmotin peptide contained within the osmotin protein sequence, corresponding amino acids residues 157-165 (PeptideOSM), which is present at the interface between osmotin and its receptor PHO36, as well as adiponectin receptor has biological activity (see p. 10, left column, 2nd-3rd paragraphs). While Miele et al. teach that PeptideOSM could potentially be used for “generating biologically active molecules, as a drug design template” (p. 10, right column, last paragraph), two other peptides based thereupon did not show any activity (see p. 7, left column), thus indicating that any random change to this region is not predictable. Applicant does not teach how an unlimited number of residues within SEQ ID NO: 1 may be substituted, deleted or inserted and still result in an osmotin capable of treating Parkinson’s disease.
Generally speaking, the number of mutations generally possible in any given protein that can be made with a reasonable expectation of success are limited. Certain positions in the sequence are critical to the protein's structure/function relationship, e.g., such as various sites or regions directly involved in binding, activity and in providing the correct three-dimensional spatial orientation of binding and active sites. The art provides evidence that mutations can be destabilizing and their effects unpredictable. Bhattacharya et al. (PLoS ONE 12(3): e0171355. https://doi.org/10.1371/journal. pone. 0171355; 22 pages total) teach even single nucleotide variations have a “range of effects at the protein level that are significantly greater than assumed by existing software prediction methods, and that correct prediction of consequences remains a significant challenge” (p. 18, 1st and 2nd paragraphs). In addition, Fenton et al. (Medicinal Chemistry Research (2020) 29:1133–1146) review the unpredictability of making substitutions at non-conserved positions in a protein, which can have significant effects on protein function that computational algorithms cannot predict very well (p. 1134, right column, middle paragraph).
Although machine learning algorithms have improved the ability to predict protein 3D structure from sequences, methods based on artificial intelligence for predicting the impact of mutations on protein stability still face challenges, including prediction biases towards “generalization”, “data set”, “destabilizing mutations” and the inability to predict the effects of multiple mutations. See Figure 1, at p. 162 and the discussion at pages 165-166 of Pucci et al. (Current Opinion in Structural Biology 2022, 72: 161-168). Even in the case of single mutations, artificial intelligence programs do not accurately “predict the impact of mutation on protein stability” or function (see p. 2, 2nd paragraph and p. 7, 1st full paragraph of Pak et al., PLoS ONE 18(3): e0282689. https://doi.org/10.1371/ journal.pone.0282689).
In the instant case, the claims encompass up to a 100% divergence from SEQ ID NO: 1, which in practical terms constitutes a deletion, substitution or insertion of at least 243 amino acid residues. Applicants have provided little or no guidance beyond the mere presentation of sequence data to enable one of ordinary skill in the art to determine, without undue experimentation, the positions in the protein which are tolerant to change by amino acid substitutions or deletions, and the nature and extent of changes that can be made in these positions. The specification does not provide adequate guidance as to the nature of active derivatives that may be constructed, but is merely an invitation to the artisan to use the current invention as a starting point for further experimentation.
Due to the large quantity of experimentation necessary to generate and test the osmotin proteins for the ability to treat Parkinson’s disease, the lack of direction/ guidance presented in the specification regarding and the absence of working examples directed to the same, the complex nature of the invention, the unpredictability of the effects of mutation on protein structure and function and the breadth of the claims which fail to recite limitations on the osmotin protein in the alternative, undue experimentation would be required of the skilled artisan to make and/or use the claimed invention in its full scope.
Claims 9-16 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 claims contain 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 inventors, at the time the application was filed, had possession of the claimed invention.
In deciding whether the application complies with the written description requirement of 35 USC 112(a) or 35 USC 112 (pre-AIA ), first paragraph, it is necessary to understand what Applicant has possession of and what Applicant is claiming. The claims are drawn to treating Parkinson’s with an osmotin protein in which “one or more amino acid residues” may be substituted within SEQ ID NO: 1. Thus, the claims encompass an embodiment in which no upper limit of residues may be substituted, deleted or inserted within the amino acid sequence of SEQ ID NO: 1.
To provide evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof. The instant specification teaches that administration of SEQ ID NO: 1 improved a number of endpoints in two separate mouse models of Parkinson’s disease, the MPTP-induced and NSE-haSyn transgenic mice.
The MPEP 2163(A) states “‘[a]n invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function.’” For inventions in emerging and unpredictable technologies, or for inventions characterized by factors not reasonably predictable which are known to one of ordinary skill in the art, more evidence is required to show possession. (See MPEP 2163(II)(A)(3)(a)(i)). From the specification, it is clear that Applicant has possession of SEQ ID NO: 1 as an osmotin protein capable of treating Parkinson’s disease. Miele et al. (PLoS One, 2011; 6: 1-11) provide structure to function support for an osmotin peptide contained within the osmotin protein sequence, corresponding amino acids residues 157-165 (PeptideOSM), which is present at the interface between osmotin and its receptor PHO36, as well as adiponectin receptor has biological activity (see p. 10, left column, 2nd-3rd paragraphs). While Miele et al. teach that PeptideOSM could potentially be used for “generating biologically active molecules, as a drug design template” (p. 10, right column, last paragraph), two other peptides based thereupon did not show any activity (see p. 7, left column). In summary, Applicant does not teach how an unlimited number of residues within SEQ ID NO: 1 may be substituted, deleted or inserted and still result in an osmotin capable of treating Parkinson’s disease. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116). With the exception of SEQ ID NO: 1, the skilled artisan cannot envision the detailed chemical structure of the encompassed osmotin proteins, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. Therefore, only the osmotin protein comprising the amino acid sequence set forth in SEQ ID NO: 1, but not the full breadth of the claim meets the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115).
Notice for all US Patent Applications filed on or after March 16, 2013: In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 9-14 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Kim (US 2018/0036365). Kim teaches treating a neurological disease, wherein said disease is Parkinson's disease, comprising administering to a subject in need thereof, a composition comprising a 9mer osmotin derived peptide having the sequence CTQGPCGPT (see claims 13-15; sequence listing). Instant claim 9 recites administering a composition comprising SEQ ID NO: 1, which is the full-length wild-type osmotin protein, or a composition having one or more amino acid residues substituted, deleted or inserted within the amino acid sequence of SEQ ID NO: 1. Since Kim teaches an osmotin-derived peptide, this meets the limitation of a sequence having more amino acid residues “substituted, deleted or inserted with the amino acid sequence of SEQ ID NO: 1” as recited in claim 9. Regarding the formulation, Kim teaches the osmotin peptide is contained in an amount of 0.1 to 100% by weight based on the total weight of the composition in the form of a health functional food in any one formulation selected from the group consisting of a beverage, a pill, a tablet, a capsule, powder and pharmaceutical composition (see claims 16-18), thereby meeting the limitations of claims instant claims 10, 11 and 13. Finally, Kim teaches that a functional food composition comprising the osmotin peptide decreases expression levels of p-JNK (see paragraphs [0025] [0035], [0063] and Figure 13), thereby meeting the limitation of instant claim 12.
Claims 9-14 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Kim (US 2013/0210738). Kim teaches administering osmotin to treat Parkinson’s disease (see claim 2; paragraphs [0018]-[0019]). Kim teaches that osmotin is a stable 24 kDa protein and that is naturally occurring and “contained in ripe fruits of plants, for example, Nicotiana tabacum” (see paragraphs [0006] [0016]). It flows therefrom that Kim teaches the wild-type osmotin protein having a sequence highly homologous to instant SEQ ID NO: 1. Evidence for this is found in Singh et al. (Plant Physiol. 90, 1096-1101, 1989—on IDS filed 01/02/2024), who teach an osmotin protein derived from Nicotiana tabacum, having >99% sequence identity (a conservative substitution at residue 129) to instant SEQ ID NO: 1. See the alignment between the osmotin protein taught by Singh et al. and instant SEQ ID NO: 1 in Appendix I. Note MPEP 2131.01, which has found the use of evidentiary references in rejections under 35 U.S.C. 102 as proper when used to show that a characteristic no disclosed in the reference is nevertheless inherent. Thus, Kim mees the limitation of instant claim 9.
Kim contemplates that when formulated as a food or beverage, the osmotin protein is contained between 10-15% by weight relative to the weight of the food/beverage composition (see paragraph [0034]), thus meeting the limitation of claim 10. Kim teaches that the osmotin can be formulated as a pharmaceutically acceptable composition or functional health food composition, for instance, as a powder, granule, tablet, pill, capsule, suspension, extract, emulsion, syrup or aerosol formulation (see claims 8-12), thereby meeting the limitations of claims 11, 13 and 14.
Regarding claim 12, although the Kim reference does not recite that osmotin peptide regulates Nurr1, VMAT2, DAT, TH, p-p38, p-JNK or p-ERK, because it teaches administration of the same protein to treat Parkinson’s, (i.e., treating the same patient population with the same agent), the same clinically significant improvements as recited in claim 12 with regard to protein regulation must have been inherently occurring in the prior art of Kim (see Ex parte Novitski, 26 USPQ2d 1389 (BPAI 1993); also Integra LifeSciences I Ltd. V. Merck KGaA, (DC SCalif) 50 USPQ2d 1846). Further, “[f]rom the standpoint of patent law, a compound and all its properties are inseparable” (see In re Papesch, 315 F.2d 381, 391, 137 USPQ 43, 51 (CCPA 1963)). In other words, the treatment methods set forth in Kim must, by definition achieve the same effects as recited in claim 12 absent evidence to the contrary.
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 9-16 are rejected under 35 U.S.C. 103 as being unpatentable over Kim (US 2018/0036365—hereafter the ‘365 document) in view of Kim (US20170246245—hereafter the ‘245 document) and Kim (WO2016143981 Machine Translation—hereafter the ‘981 document). The first factor to consider when making a rejection under 35 U.S.C. 103(a) is to determine the scope and contents of the prior art. The ‘365 document teaches treating a neurological disease, wherein said disease is Parkinson's disease, comprising administering to a subject in need thereof, a composition comprising a 9mer osmotin derived peptide having the sequence CTQGPCGPT (see claims 13-15; sequence listing). Instant claim 9 recites administering a composition comprising SEQ ID NO: 1, which is the full-length wild-type osmotin protein, or a composition having one or more amino acid residues substituted, deleted or inserted within the amino acid sequence of SEQ ID NO: 1. Since the ‘365 document teaches an osmotin-derived peptide, this meets the limitation of a sequence having more amino acid residues “substituted, deleted or inserted with the amino acid sequence of SEQ ID NO: 1” as recited in claim 9. Regarding the formulation, the ‘365 document teaches the osmotin peptide is contained in an amount of 0.1 to 100% by weight based on the total weight of the composition in the form of a health functional food in any one formulation selected from the group consisting of a beverage, a pill, a tablet, a capsule, powder and pharmaceutical composition (see claims 16-18), thereby meeting the limitations of claims instant claims 10, 11 and 13. Finally, the ‘365 document teaches that a functional food composition comprising the osmotin peptide decreases expression levels of p-JNK (see paragraphs [0025] [0035], [0063] and Figure 13), thereby meeting the limitation of instant claim 12.
The second factor to consider is to ascertain the differences between the prior art and the instant claims. The ‘365 document does not teach administering the wild-type osmotin as set forth in SEQ ID NO: 1. In addition, the ‘365 document does not explicitly teach formulating the composition into a veterinary composition or an animal feed additive. Regarding the full length osmotin, the ‘245 document discloses improving cognitive function comprising administering an osmotin protein sharing 100% sequence identity with instant SEQ ID NO: 1 (see claim 1; sequence listing). The alignment between the osmotin protein disclosed in the ‘245 document and instant SEQ ID NO: 1 is found in APPENDIX II.
It would have been obvious to the person of ordinary skill in the art at the time of the filing to administer full-length osmotin, as taught in the ‘245 document because both the osmotin peptide of the ‘365 document and the full-length osmotin protein of the ‘245 document reduce BACE-1 levels (see paragraph [0054] of the ‘245 document and paragraph [0035] of the ‘365 document). The person having ordinary skill in the art would have recognized that this represents a simple substitution of one element known to be effective for another known to be effective in the same way. The person of ordinary skill in the art would have been motivated to use either the osmotin peptide or protein because both the ‘245 and ‘365 documents demonstrated they had equivalent effects. Express suggestion to substitute one equivalent for another need not be present to render such a substitution obvious (see MPEP 2143(I)(B)). Furthermore, the person of ordinary skill in the art could have reasonably expected success because the ‘365 and ‘245 documents report that both the osmotin peptide and full-length protein are effective in equivalent ways.
Regarding formulating the composition as a veterinary composition or an animal feed additive, the ‘365 document does contemplate administering the osmotin peptide to animals (see paragraph [0042], for example) as well as teaching that the peptide can be formulated as a functional food (claims 16-18). Further, the ‘981 document teaches that osmotin can be administered to humans, lab animals and livestock through oral routes (see p. 15, 2nd paragraph of the translation). It would have been obvious to the person of ordinary skill in the art at the time of the filing of the invention to formulate the osmotin-containing functional food as a veterinary composition or animal feed additive because the applied prior art taught treating animals. The person of ordinary skill in the art would have been motivated to treat animals with veterinary compositions or animal feed additives because these are designed for animals. Furthermore, the person of ordinary skill in the art could have reasonably expected success because the level of skill in the art with respect to formulating foodstuffs and compositions was high (see paragraph [0038] of the ‘365 document).
Thus, the claims do not contribute anything non-obvious over the prior art.
Claims 9-16 are rejected under 35 U.S.C. 103 as being unpatentable over Kim (US 2013/0210738—hereafter the ‘738 document) in view of Singh et al. (Plant Physiol. 90, 1096-1101, 1989—on IDS filed 01/02/2024) and Kim (WO2016143981 Machine Translation—hereafter the ‘981 document). The first factor to consider when making a rejection under 35 U.S.C. 103(a) is to determine the scope and contents of the prior art. The ‘738 document teaches administering osmotin to treat Parkinson’s disease (see claim 2; paragraphs [0018]-[0019]). The ‘738 document teaches that osmotin is a stable 24 kDa protein that is a naturally occurring protein “contained in ripe fruits of plants, for example, Nicotiana tabacum” (see paragraphs [0006], [0016]). It flows therefrom that the ‘738 document teaches the wild-type osmotin protein having a sequence highly homologous to instant SEQ ID NO: 1. Evidence for this is found in Singh et al., who teach an osmotin protein derived from Nicotiana tabacum, having >99% sequence identity (a conservative substitution at residue 129) to instant SEQ ID NO: 1 (see APPENDIX I for the alignment).
The effects recited in claim 12 with regard to Nurr1, VMAT2, DAT, TH, p-p38, p-JNK or p-ERK expression levels would have been inherent to the ‘738 document because it teaches the same osmotin protein as recited in the claims administered to the same patient population. The same clinically significant improvements as recited in claim 12 must occur as a result of administering the osmotin protein taught in the ‘738 document to a patient population being treated Parkinson’s disease. The recitation of the effects on Nurr1, VMAT2, DAT, TH, p-p38, p-JNK and p-ERK expression are part of to the understandings and expectations disclosed in the prior art. The method of treatment and the structure of the osmotin protein for carrying out that treatment was part of the disclosure of the ‘738 document, so the effects upon the body of the patients are inherent. Further, for the record, the express, implicit, and inherent disclosures of a prior art reference may be relied upon in the rejection of claims under 35 U.S.C. 103. “The inherent teaching of a prior art reference, a question of fact, arises both in the context of anticipation and obviousness.” In re Napier, 55 F.3d 610, 613, 34 USPQ2d 1782, 1784 (Fed. Cir. 1995) (affirmed a 35 U.S.C. 103 rejection based in part on inherent disclosure in one of the references). See also In re Grasselli, 713 F.2d 731, 739, 218 USPQ 769, 775 (Fed. Cir. 1983). See also MPEP 2112.
The ‘738 document contemplates that when formulated as a food or beverage, the osmotin protein is contained between 10-15% by weight relative to the weight of the food/beverage composition (see paragraph [0034]), thus meeting the limitation of claim 10. The ‘738 document teaches that the osmotin can be formulated as a pharmaceutically acceptable composition or functional health food composition, for instance, as a powder, granule, tablet, pill, capsule, suspension, extract, emulsion, syrup or aerosol formulation (see claims 8-12), thereby meeting the limitations of claims 11, 13 and 14. Finally, the ‘738 document contemplates treatment of non-human animals (see claim 13; paragraphs [0010] and [0038]).
The second factor to consider is to ascertain the differences between the prior art and the instant claims. The ‘738 document does not explicitly teach formulating the composition into a veterinary composition or an animal feed additive, although it does contemplate administering the osmotin peptide to animals (see claim 13; paragraph [0010]) as well as teaching that the peptide can be formulated as a functional food (claims 8-12). Further, the ‘981 document teaches that osmotin can be administered to humans, lab animals and livestock through oral routes (see p. 15, 2nd paragraph of the translation). It would have been obvious to the person of ordinary skill in the art at the time of the filing of the invention to formulate the osmotin-containing functional food as a veterinary composition or animal feed additive because the applied prior art taught treating animals. The person of ordinary skill in the art would have been motivated to treat animals with veterinary compositions or animal feed additives because these are designed for animals. Furthermore, the person of ordinary skill in the art could have reasonably expected success because the level of skill in the art with respect to formulating foodstuffs and compositions was high (see paragraphs [0035]-[0037] of the ‘738 document).
Thus, the claims do not contribute anything non-obvious over the prior art.
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 9-16 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 10,471,119 in view of the ‘365 document, the ‘245 document and the ‘981 document. All the references are cited above. The claims of the reference patent recite a method of treating Alzheimer's disease comprising administering a composition comprising an osmotin peptide that is contained in an amount of 0.1 to 100% by weight based on the total weight of the composition, wherein the composition is a health functional food in any one formulation selected from the group consisting of a beverage, a pill, a tablet, a capsule, and powder, wherein the composition is a pharmaceutical composition, wherein the subject is a human or an animal. The differences between the instant claims and those of the reference patent are as follows. The claims of the reference patent do not recite treatment of Parkinson’s disease, administering the wild-type osmotin as set forth in SEQ ID NO: 1, nor do they explicitly teach formulating the composition into a veterinary composition or an animal feed additive.
Regarding Parkinson’s disease, the ‘365 document, which shares the same specification as that of the reference patent, discloses treating Parkinson’s disease, in addition to Alzheimer’s disease. Regarding the full length osmotin, the ‘245 document discloses improving cognitive function administering an osmotin protein sharing 100% sequence identity with instant SEQ ID NO: 1 (see claim 1; sequence listing). Refer to Appendix II for the alignment. It would have been obvious to the person of ordinary skill in the art at the time of filing to administer full-length osmotin, as taught in the ‘245 document, because the person having ordinary skill in the art would have recognized that this represents a simple substitution of one element known to be effective for another known to be effective in the same way. The person of ordinary skill in the art would have been motivated to use either the osmotin peptide or protein because the ‘365 document and the ‘245 document demonstrated that the osmotin peptide and protein were effective in improving motor and cognitive function, respectively (see paragraph [0035] of the ‘365 document and paragraphs [0044]-[0062] of the ‘245 document). Express suggestion to substitute one equivalent for another need not be present to render such a substitution obvious (see MPEP 2143(I)(B)). Furthermore, the person of ordinary skill in the art could have reasonably expected success because the ‘245 document reports that the osmotin full-length protein is effective.
Regarding formulating the composition as a veterinary composition or an animal feed additive, the claims of the reference patent explicitly recite administering the osmotin peptide to animals (see claim 8) as well as formulating the osmotin peptide as a functional food (claim 3). Further, the ‘981 document teaches that osmotin can be administered to humans, lab animals and livestock through oral routes (see p. 15, 2nd paragraph of the translation). It would have been obvious to the person of ordinary skill in the art at the time of the filing of the invention to formulate the osmotin-containing functional food as a veterinary composition or animal feed additive because the applied prior art taught treating animals. The person of ordinary skill in the art would have been motivated to treat animals with veterinary compositions or animal feed additives because these are designed for animals. Furthermore, the person of ordinary skill in the art could have reasonably expected success because the level of skill in the art with respect to formulating foodstuffs and compositions was high (see paragraph [0038] of the ‘365 document).
Thus, when considered in light of the prior art, the instant claims are not patentably distinct over those of the reference patent.
Conclusion
No claim is allowed.
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/CHRISTINA M BORGEEST/Primary Examiner, Art Unit 1675
APPENDIX I
The alignment between the osmotin protein derived from Nicotiana tabacum, taught in Singh et al. (Plant Physiol. 90, 1096-1101, 1989—on IDS filed 01/02/2024), and instant SEQ ID NO: 1:
Query Match 99.8%; Score 1380; Length 243;
Best Local Similarity 99.6%;
Matches 242; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MGNLRSSFVFFLLALVTYTYAATIEVRNNCPYTVWAASTPIGGGRRLDRGQTWVINAPRG 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MGNLRSSFVFFLLALVTYTYAATIEVRNNCPYTVWAASTPIGGGRRLDRGQTWVINAPRG 60
Qy 61 TKMARVWGRTNCNFNAAGRGTCQTGDCGGVLQCTGWGKPPNTLAEYALDQFSGLDFWDIS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 TKMARVWGRTNCNFNAAGRGTCQTGDCGGVLQCTGWGKPPNTLAEYALDQFSGLDFWDIS 120
Qy 121 LLDGFNIPITFPTNPSGGKCHALCTAINGECPAELRVPGGCNNPCTTFGGQQYCCTQRPC 180
||||||||:|||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 LLDGFNIPMTFPTNPSGGKCHALCTAINGECPAELRVPGGCNNPCTTFGGQQYCCTQRPC 180
Qy 181 GPTFFSKFFKQRCPDAYSYPQDDPTSTFTCPGGSTNYRVIFCPNGQAHPNFPLEMPGSDE 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 GPTFFSKFFKQRCPDAYSYPQDDPTSTFTCPGGSTNYRVIFCPNGQAHPNFPLEMPGSDE 240
Qy 241 VAK 243
|||
Db 241 VAK 243
APPENDIX II
The alignment between the osmotin protein disclosed in the ‘245 document and instant SEQ ID NO: 1:
Query Match 100.0%; Score 1383; Length 243;
Best Local Similarity 100.0%;
Matches 243; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MGNLRSSFVFFLLALVTYTYAATIEVRNNCPYTVWAASTPIGGGRRLDRGQTWVINAPRG 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MGNLRSSFVFFLLALVTYTYAATIEVRNNCPYTVWAASTPIGGGRRLDRGQTWVINAPRG 60
Qy 61 TKMARVWGRTNCNFNAAGRGTCQTGDCGGVLQCTGWGKPPNTLAEYALDQFSGLDFWDIS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 TKMARVWGRTNCNFNAAGRGTCQTGDCGGVLQCTGWGKPPNTLAEYALDQFSGLDFWDIS 120
Qy 121 LLDGFNIPITFPTNPSGGKCHALCTAINGECPAELRVPGGCNNPCTTFGGQQYCCTQRPC 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 LLDGFNIPITFPTNPSGGKCHALCTAINGECPAELRVPGGCNNPCTTFGGQQYCCTQRPC 180
Qy 181 GPTFFSKFFKQRCPDAYSYPQDDPTSTFTCPGGSTNYRVIFCPNGQAHPNFPLEMPGSDE 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 GPTFFSKFFKQRCPDAYSYPQDDPTSTFTCPGGSTNYRVIFCPNGQAHPNFPLEMPGSDE 240
Qy 241 VAK 243
|||
Db 241 VAK 243
Prosecution Insights