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 .
EXAMINER’S NOTE
To overcome the rejections under 35 U.S.C. 112(a) that are detailed below, Examiner suggests that Applicant amend Claim 1, for example, to recite the function of SEQ ID NO: 26 and its claimed sequence variants within the claim. In view of the disclosure in the instant specification, SEQ ID NO: 26 and variants thereof appear to function as a “morphogenic regulator” or a “heterologous morphogenic regulator” in the context of the instant invention.
Priority
Examiner notes that this application is a Divisional Application of U.S. Application No. 17/630,973, filed January 28, 2022, which is a U.S. National Phase of PCT/US20/44268, filed July 30th , 2020, which claims the benefit of U.S. Provisional Patent Application No. 62/880,131, filed July 30th 2019. Acknowledgment is made of Applicant' s claim for domestic benefit under 35 U.S.C. 119(e). As such, the effective filing date of Claims 1-5 is July 30th 2019.
Status of the Claims
Claims 1-5 are pending.
Claims 1-5 are examined herein.
Information Disclosure Statement
The Information Disclosure Statement filed on 05/27/2025 is in compliance with the provisions of 37 CFR 1.97 and has been considered in full. A signed copy of the list of references cited are included with this Office Action.
Claim Rejections - 35 USC § 112
Written Description
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 1-5 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.
The Federal Circuit has clarified the written description requirement. The court stated that a written description of an invention "requires a precise definition, such as by structure, formula, [or] chemical name, of the claimed subject matter sufficient to distinguish it from other materials". University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568; 43 USPQ2d 1398, 1406 (Fed. Cir. 1997). The court also concluded that "naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not description of that material". Id. Further, the court held that to adequately describe a claimed genus, Patent Owner must describe a representative number of the species of the claimed genus, and that one of skill in the art should be able to "visualize or recognize the identity of the members of the genus". Id.
Claims 1-5 require an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 26.
Applicant does not describe polypeptides with at least 95% sequence identity to instant SEQ ID NO: 26 that have any function.
Polypeptides with 95% identity to the 297 amino acids long SEQ ID NO: 26 encompass polypeptides with 15 unspecified amino acid additions, deletions, and substitutions relative to SEQ ID NO: 26. Polypeptides with 15 amino acid substitutions relative to SEQ ID NO: 26 encompass approximately 1915 (6.587903823E+24) unique polypeptides. The instant specification fails to provide guidance for which amino acids of SEQ ID NO: 26 can be altered or duplicated, and to which amino acids, as well as failing to provide guidance for which amino acids must not be changed, to maintain the function of the encoded transcription factor. The specification fails to provide guidance for which amino acids can be deleted and which region of the sequence can tolerate additions and still function have any function. The specification does not provide adequate guidance with respect to the structure/function relationship of the claimed genera of polypeptides that perform any function, much less the function recited in the specification of a WUS transcription factor that provides morphogenic gene regulation.
Applicant has only provided one polypeptide out of the myriad of polypeptides encompassed by the vast genus they currently claim. As such, there is substantial variation within the genus of polypeptides and polynucleotides encoding polypeptides that have at least 95% identity to instant SEQ ID NO: 26, and the Applicant has only provided one example species from this vast genus. While it is known in the art that computer programs can predict proteins that have 95% identity to instant SEQ ID NO: 26, the prior art teaches that protein-based predictors are still limited in their predictive ability to model mutations that do not negatively affect protein structure and function because of the unbalance and intrinsic variability of the thermodynamic data and their prediction performance [See Liu et al. (2022); pg. 7, left column, last paragraph; IDS Document]. Although the Applicant would be able to predict amino acid sequences with 95% sequence identity to instant SEQ ID NO: 26, it is uncertain if these predicted proteins would have any function, much less the function recited in the specification of a WUS transcription factor that provides morphogenic gene regulation. Therefore, the mere fact that the Applicant discloses SEQ ID NO: 26 and polynucleotides that encode SEQ ID NO: 26 is insufficient to adequately describe a representative number of species of the vast and highly diverse genus of sequence variants.
The instant specification discloses SEQ ID NO: 26 (pg. 3, paragraph [0006]), but does not disclose any other polypeptides with at least 95% identity to SEQ ID NO: 26. SEQ ID NO: 27 (pg. 3, paragraph [0006]) has 54.5% sequence identity to SEQ ID NO: 26, however, the other polypeptides disclosed by the instant specification have less than 30.1% sequence identity to SEQ ID NO: 26.
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Polypeptides with 95-100% sequence identity to SEQ ID NO: 26 do not appear to be known in the art. An NCBI BLAST search for SEQ ID NO: 26 did not disclose any accessions with 95-100% sequence identity to SEQ ID NO: 26, with the closest prior art accession having 77.08% sequence identity to SEQ ID NO: 26 (XP_004289091.1, published 03/04/2015) and a disclosed function as a WUSCHEL-like Homeobox.
A UniProt search for SEQ ID NO: 26 did not disclose any accessions with 95-100% sequence identity to SEQ ID NO: 26, with the closest prior art accession (A0A2P6RLV6_ROSCH, published 05/23/2018) having 87.4% sequence identity to SEQ ID NO: 26, which disclosed the function of being a WUSCHEL-like HOMEOBOX protein.
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However, one of ordinary skill in the art would not consider these proteins to be species of the claimed genus due to their less than 95% sequence identity to instant SEQ ID NO: 26 and that there is no well-developed field of prior art of proteins with at least 95% identity to SEQ ID NO: 26, much less any proteins having at least 95% sequence identity relative to SEQ ID NO: 26 that have any function.
Additionally, a search of the patent literature reveals that there is no well-developed field of prior art regarding polypeptides having at leave 95% sequence identity relative to SEQ ID NO: 26, , much less any proteins having at least 95% sequence identity relative to SEQ ID NO: 26 that have any function (in the case of SEQ ID NO: 26, as a WUS transcription factor) when introduced to a cell, plant part, or plant, as described in the instant specification .
The specification discloses a group of morphogenic regulators including, Wuschel (WUS) genes (e.g., from blackberry and/or cherry), Baby boom (BBM, e.g., from blackberry and/or cherry), Knotted1 (KN1) genes (e.g., from maize, blackberry, and/or cherry), isopentenyl transferase (ipt) genes (e.g., from Agrobacterium tumefaciens, blackberry, and/or cherry), a CLAVATA3 (CLV3) mutant, miR156 (e.g., from citrus), AtGRF5 (e.g., from Arabidopsis thaliana), NTT (e.g., from Arabidopsis thaliana, blackberry, and/or cherry), HDZipII (e.g., from Arabidopsis thaliana, blackberry, and/or cherry), and orthologs or polypeptides thereof. While it is acknowledged that SEQ ID NO: 26 comprises a 63 ammo acid HD domain at positions 31-93 (RWTPTTDQIRILKELYYNKGVRSPSAEQIQRICLQLKRYGKIEGKNVFYWFQNHKARER QKKR), a conserved ETLPLFP motif at positions 240-246, and a conserved SLELSL motif at positions 281-286, these domains only account for 25.5% of the 297 amino acid long SEQ ID NO: 26, the recitation of this protein being a WUS protein because it comprises these domains is generic in regard to function— without actually describing how these domains provide morphogenic gene regulation in a cell, plant part, or plant. The specification does not disclose any structures, domains or motifs encompassed by the remaining 74.5% of the amino acid encoded by SEQ ID NO: 26, nor does the specification provide any guidance as to whether these undescribed portions can tolerate mutations. It is also known in the art that the homeodomain in WUS proteins form dimers through interactions of specific residues in the homeodomain, and that these dimers stabilize WUS DNA interaction, resulting in high sequence specificity, wherein disrupting the dimer interface on the protein or DNA level reduced DNA-binding specificity [See Sloan et al. (2020); IDS Document]. As such, mutations that produce sequences with at least 95% sequence identity to instant SEQ ID NO: 26 would lose the DNA-binding specificity of the HD, which would result in a less functionally active WUS transcription factor. Additionally, when searching for SEQ ID NO: 26, it is noted above that the closest protein (either prior art or post filing art) was UniProt Accession A0A2P6RLV6_ROSCH, which only had 87.5% sequence identity to instant SEQ ID NO: 26 although being annotated as a Homobox-WOX family protein. As such, due to the disclosure of the specification and art, while SEQ ID NO: 26 may be denoted as a WUS transcription factor in the instant application, the RoWUS encoded by SEQ ID NO: 26 is clearly a derived WUS that does not comprise all the structural features that are common to the art-recognized family of WUS transcription factors found in other plants, and the identity of the structural features that make RoWUS diverge from other WUS transcription factors is not disclosed in the specification. Therefore, the mere fact that SEQ ID NO: 26 comprises the domains recited above is insufficient to adequately describe the structure-function relationship of the genus of polypeptides and polynucleotides that encode polypeptides with 95% sequence identity to SEQ ID NO: 26.
The prior art teaches that even minor changes in a polypeptide’s sequence can change or eliminate activity. Olsen et al. (2005; IDS Document) reviewed the amino acid backbone changes in three mutants of NAC transcription factors that abolished activity; two were found to be single amino acid substitutions and the third was a dipeptide insertion, wherein all mutated polypeptides were at least 90% sequence identical to the active polypeptide (pg. 84).
Furthermore, Guo et al. (2004; IDS Document) describes that while proteins are fairly tolerant to mutations resulting in single amino acid changes, increasing the number of substitutions additively increases the probability that the protein will be inactivated (pg. 9209, right column, paragraph 2).
In the transgenic transcription factor art, Zhang et al. (2003; ID Document) teaches that transgenic effects of transcription factor expression conceptually can be thought of as arising from hypermorph activity or neomorph activity (pg. 431). Especially in the case of neomorph activity, one skilled in the art would be uncertain what sections of the polypeptide’s amino acid sequence are necessary and/or sufficient for activity, and thus which amino acids of the polypeptide could be modified and retain activity in the instant invention.
Thus, the structural features that distinguish polypeptides with at least 95% identity to SEQ ID
NO: 26 that have any function from other polypeptides with at least 95% identity to SEQ ID NO: 26 that have no function are unknown.
One of ordinary skill in the art would not recognize that Applicant was in possession of the
necessary common attributes or features of the genus in view of the disclosed species. Since the
disclosure fails to describe the common attributes that identify members of the genus, and because the
genus is both vast and highly diverse, SEQ ID NO: 26 is insufficient to describe the claimed genus.
The number of species described by Applicant are insufficient to describe the recited genus by
virtue of example, given the vast size of the recited genus and the lack of written description in the
instant specification with regard to the structural and functional characteristics of the claimed
compositions.
Hence, Applicant has not, in fact, described the claimed methods within the full scope of the
claims, and the specification fails to provide an adequate written description of the claimed invention.
Scope of Enablement
Claims 1-5 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 an amino acid sequence having 100% sequence identity to the polypeptide sequence of SEQ ID NO: 26, does not reasonably provide enablement for an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 26. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims.
The Federal Circuit in In re Wands lists eight considerations for determining whether or not undue experimentation would be necessary to practice an invention. In re Wands, 858 F2d 731, 8 USPQ2d 1400, 1406 (Fed. Cir. 1988). These factors are: the quantity of experimentation necessary, the amount of direction or guidance presented, the presence or absence of working examples of the invention, the nature of the invention, the state of the prior art, the relative skill of those in the art, the predictability or unpredictability of the art, and the breadth of the claims. Id.
Claims 1-5 require a polynucleotide encoding an amino acid sequence having at least 95% sequence identity to the polypeptide sequence of SEQ ID NO: 26.
Applicant does not teach how to make or use polypeptides having at least 95% sequence identity to instant SEQ ID NO: 26 that elicit any function, without undue experimentation.
Polypeptides with 95% identity to the 297 amino acids long SEQ ID NO: 26 encompass polypeptides with 15 unspecified amino acid additions, deletions, and substitutions relative to SEQ ID NO: 26. Polypeptides with 15 amino acid substitutions relative to SEQ ID NO: 26 encompass approximately 1915 (6.587903823E+24) unique polypeptides. The instant specification fails to provide guidance for which amino acids of SEQ ID NO: 26 can be altered or duplicated, and to which amino acids, as well as failing to provide guidance for which amino acids must not be changed, to maintain any function, much less the function recited in the specification of a WUS transcription factor (morphogenic regulator) that provides morphogenic gene regulation. The specification fails to provide guidance for which amino acids can be deleted and which region of the sequence can tolerate additions and have any function, much less the function recited in the specification of a WUS transcription factor that provides morphogenic gene regulation. The specification does not provide adequate guidance with respect to the structure/function relationship of the claimed genera of polypeptides and if they can perform any function, much less the function recited in the specification of a WUS transcription factor that provides morphogenic gene regulation.
The instant specification teaches SEQ ID NO: 26 (pg. 3, paragraph [0006]), but does not teach any other polypeptides with at least 95% identity to SEQ ID NO: 26. SEQ ID NO: 27 (pg. 3, paragraph [0006]) has 54.5% sequence identity to SEQ ID NO: 26, however, the other polypeptides taught by the instant specification have less than 30.1% sequence identity to SEQ ID NO: 26.
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Polypeptides with 95-100% sequence identity to SEQ ID NO: 26 do not appear to be known in the art. An NCBI BLAST search for SEQ ID NO: 26 did not teach any prior art accessions with 95-100% sequence identity to SEQ ID NO: 26, with the closest prior art accession having 77.08% sequence identity to SEQ ID NO: 26 (XP_004289091.1, published 03/04/2015) and a disclosed function as a WUSCHEL-like Homeobox.
A UniProt search for SEQ ID NO: 26 did not teach any accessions with 95-100% sequence identity to SEQ ID NO: 26, with the closest prior art accession (A0A2P6RLV6_ROSCH, published 05/23/2018) having 87.4% sequence identity to SEQ ID NO: 26, which disclosed the function of being a WUSCHEL-like HOMEOBOX protein.
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Additionally, a search of the patent literature reveals that there is no well-developed field of prior art regarding polypeptides having at leave 95% sequence identity relative to SEQ ID NO: 26 that have any function (in the case of SEQ ID NO: 26, as a WUS transcription factor) when introduced to a cell, plant part, or plant.
The specification does not provide any teachings, working examples, or prophetic examples of making or using the claimed polypeptides within the claimed range of 95-99% sequence identity to instant SEQ ID NO: 26, other than SEQ ID NO: 26. While it is known in the art that computer programs can predict proteins that have 95% identity to instant SEQ ID NO: 26, the prior art teaches that protein-based predictors are still limited in their predictive ability to model mutations that do not negatively affect protein structure and function because of the unbalance and intrinsic variability of the thermodynamic data and their prediction performance [See Liu et al. (2022); pg. 7, left column, last paragraph; IDS Document]. Although the Applicant would be able to predict amino acid sequences with 95% sequence identity to instant SEQ ID NO: 26, it is not clear that the Applicant would be able to make these mutations in the claimed sequence variants wherein the predicted proteins would have any function, much less the recited function of a WUS transcription factor that provides morphogenic gene regulation. At the most basal level, this would require one of ordinary skill in the art to identify all proteins within any diverse source in the art that have at least 95% sequence identity to instant SEQ ID NO: 26 that have any function, or all of the mutations that can be made to sequences from any diverse source in the art with at least 95% sequence identity to instant SEQ ID NO: 26 so that the encoded protein does not lose its function as a morphogenic regulator as described in the instant specification, and would require one or ordinary skill in the art to design expression cassettes that can be transformed into any known species of cell, plant part, or plant wherein the encoded amino acid with at least 95% sequence identity to SEQ ID NO: 26 has the capacity to have DNA-binding specificity in any known cell, plant part, or plant, to produce any function. Accordingly, the Applicant has not demonstrated that all proteins with at least 95% sequence identity to instant SEQ ID NO: 26 would be able to perform any function, much less the function of morphogenic regulation in any cell, plant part, or plant from any diverse source in the art, and without the function, the claimed genus does not have an obvious use. The single example using RoWUS in Example 8 (paragraph 00410) does not provide adequate teachings to enable the scope of the invention without undue experimentation, because it doesn’t even denote SEQ ID NO: 26 as the RoWUS sequence used in the methods of the invention, much less any variants of SEQ ID NO: 26. Therefore, the mere fact that the Applicant teaches SEQ ID NO: 26 and polynucleotides that encode SEQ ID NO: 26 is insufficient to adequately enable the making or use of the claimed genus of polypeptides across the entire scope of the claims.
Thus, from the teachings of the instant specification, it would appear that one of ordinary skill in the art would need to make the claimed polypeptides by making random amino acid deletions, substitutions, and additions which would be unpredictable.
Making additions, deletions and substitutions relative to SEQ ID NO: 26 while retaining the activity as a WUS transcription factor is unpredictable. The amino acid, which is the primary structure of the polypeptide, is the basis for the spatial structure of the polypeptide, which in turn directly determines its function. Small changes in the amino acid sequences produced by SEQ ID NO: 26 may lead to large changes in spatial structure, in turn altering the function of the polypeptide. Such differences in sequence structure will result in changes or even loss of function in certain nucleic acids/polypeptide molecules. While it is known that many amino acid substitutions, additions or deletions are generally possible in any given protein, the positions within the protein’s sequence where such amino acid changes can be made with a reasonable expectation of success (without altering protein function) are limited. Certain positions in the sequence are critical to the protein’s structure/function relationship, for example various sites or regions directly involved in binding, activity, and in providing the correct three-dimensional spatial orientation of binding and active sites. These regions can tolerate only relatively conservative substitutions or no substitutions at all. See Keskin et al., 2004, Protein Science 13: 1043-1055 (IDS Document), who teach that proteins with similar structure may have different functions (Abstract; pages 1043-1044). See also Guo et al., 2004, Proceedings of the National Academy of Sciences USA 101: 9205-9210 (IDS Document), who teach that there is a probability factor of 34% that a random amino acid replacement in a given protein will lead to its inactivation (Abstract; page 9206; Table 1). In the instant case, such a probability factor will be much higher as the claims encompass more than a single amino acid change in the proteins encoded by SEQ ID NO: 26. Furthermore, Thornton et al. (2000) (Nature Structural Biology, structural genomic supplement, November 2000: 991-994; IDS Document), teach that structural data may carry information about the biochemical function of a protein, while its biological role in the cell or organism is much more complex and additional experimentation is needed to elucidate actual biological function (page 992, left column, paragraph 2).
Undue experimentation would be required by one of ordinary skill in the art to make or use all polypeptides having at least 95% sequence identity to instant SEQ ID NO: 26 that would still retain any function, much less the function of the encoded polypeptide.
The specification teaches a group of morphogenic regulators including, Wuschel (WUS) genes (e.g., from blackberry and/or cherry), Baby boom (BBM, e.g., from blackberry and/or cherry), Knotted1 (KN1) genes (e.g., from maize, blackberry, and/or cherry), isopentenyl transferase (ipt) genes (e.g., from Agrobacterium tumefaciens, blackberry, and/or cherry), a CLAVATA3 (CLV3) mutant, miR156 (e.g., from citrus), AtGRF5 (e.g., from Arabidopsis thaliana), NTT (e.g., from Arabidopsis thaliana, blackberry, and/or cherry), HDZipII (e.g., from Arabidopsis thaliana, blackberry, and/or cherry), and orthologs or polypeptides thereof. The specification does teach an example of a RoWUS morphogenic regulator being used with different promoters in an expression cassette that was transformed into tobacco (pg. 108, Example 8) as well as RoWUS expression cassette being transformed into blackberry explants (pg. 109, Example 9) with a CRISPR-Cas9 expression cassette. However, the instant specification fails to mention which specific sequences of RoWUS were used in the assays, failing to specifically teach SEQ ID NO: 26 or any other polypeptides with 95-100% identity to SEQ ID NO: 26 in any working embodiments of the invention.
While it is acknowledged that SEQ ID NO: 26 comprises a 63 ammo acid HD domain at positions 31-93 (RWTPTTDQIRILKELYYNKGVRSPSAEQIQRICLQLKRYGKIEGKNVFYWFQNHKARER QKKR), a conserved ETLPLFP motif at positions 240-246, and a conserved SLELSL motif at positions 281-286, these domains only account for 25.5% of the 297 amino acid long SEQ ID NO: 26, the recitation of this protein being a WUS protein because it comprises these domains is generic in regard to function, without actually teaching how these domains provide morphogenic gene regulation in a cell, plant part, or plant. The specification does not teach any structures, domains or motifs encompassed by the remaining 74.5% of the amino acid encoded by SEQ ID NO: 26, nor does the specification teach whether these undescribed portions can tolerate mutations. It is also known in the art that the homeodomain in WUS proteins form dimers through interactions of specific residues in the homeodomain, and that these dimers stabilize WUS DNA interaction, resulting in high sequence specificity, wherein disrupting the dimer interface on the protein or DNA level reduced DNA-binding specificity [See Sloan et al. (2020); IDS Document]. As such, mutations that produce sequences with at least 95% sequence identity to instant SEQ ID NO: 26 would lose the DNA-binding specificity of the HD, which would result in a less functionally active WUS transcription factor, meaning the sequence variants would not have a use in the methods of the invention because they would lose their purported function. Additionally, when searching for SEQ ID NO: 26, it is noted in the above rejection that the closest protein (either prior art or post filing art) was UniProt Accession A0A2P6RLV6_ROSCH, which only had 87.5% sequence identity to instant SEQ ID NO: 26 although being annotated as a Homobox-WOX family protein. As such, due to the teachings of the specification and art, while SEQ ID NO: 26 may be taught as a WUS transcription factor in the instant application, RoWUS is clearly a derived WUS that does not comprise all the structural features that are common to the art-recognized family of WUS transcription factors found in other plants, and the identity of the structural features that make RoWUS diverge from other WUS transcription factors is not taught in the specification. Therefore, the mere fact that SEQ ID NO: 26 comprises the domains recited above is insufficient to adequately enable the making or use of the claimed genus of polypeptides across the entire scope of the claims.
Therefore, the specification fails to overcome the unpredictability in the art of making amino acid substitutions in polypeptides with at least 95% identity to SEQ ID NO: 26 and which have any function, much less that function as a morphogenic regulator, as it provides no working or prophetic examples of plant cells that have been transformed with an expression cassette comprising a polypeptide with 95-100% identity to SEQ ID NO: 26 that function to cause and/or stimulate morphogenesis in the plant cell.
The prior art teaches that even minor changes in a polypeptides sequence can change or eliminate activity. Olsen et al. (2005; IDS Document) reviewed the amino acid backbone changes in three mutants of NAC transcription factors that abolished activity; two were found to be single amino acid substitutions and the third was a dipeptide insertion, wherein all mutated polypeptides were at least 90% sequence identical to the active polypeptide (pg. 84).
In the transgenic transcription factor art, et al. (2003) teaches that transgenic effects of transcription factor expression conceptually can be thought of as arising from hypermorph activity or neomorph activity (pg. 431). Especially in the case of neomorph activity, one skilled in the art would be uncertain what sections of the polypeptide’s amino acid sequence are necessary and/or sufficient for activity, and thus which amino acids of the polypeptide could be modified and retain activity in the instant invention.
Undue experimentation would be required by one of ordinary skill in the art to use and evaluate polypeptides having at least 95% sequence identity to instant SEQ ID NO: 26 and to determine whether the broadly claimed genus of all possible claimed polypeptides with the given limitations of at least 95% sequence identity to instant SEQ ID NO: 26 have any function in a plant cell.
In the absence of guidance from either the instant disclosure or the art, and the unpredictability
discussed above, it would require undue trial and error experimentation for a skilled artisan to use the broadly claimed genus of amino acid sequences comprising a polypeptide having at least 95% identity relative to SEQ ID NO: 26, with no reasonable expectation of success. For this reason, the specification does not teach a person with skill in the art how to use the subject matter within the full scope of the claims.
Closest Prior Art
Claims 1-5 appear to be free of the prior art in regard to SEQ ID NO: 26. Regarding SEQ ID NO: 26, UniProt discloses A0A2P6RLV6_ROSCH (published 05/23/2018, See 20231120_125732_us-17-630-973-26.rup in file wrapper) having 87.4% sequence identity to SEQ ID NO: 26, encoding a putative WUSCHEL-like HOMEOBOX protein. However, the accession and the associated publication does not teach an amino acid that has at least 95% sequence identity relative to the polypeptide sequence of SEQ ID NO:26, much less the combination of A0A2P6RLV6_ROSCH operably linked or operably associated with a heterologous promoter. The accession and the associated publication also does not teach the integration of A0A2P6RLV6_ROSCH into any cell, plant part, or plant known in the art, or the integration of A0A2P6RLV6_ROSCH into expression cassette or vector. The teachings of UniProt A0A2P6RLV6_ROSCH, its associated publication, and the prior art does not provide any motivation to target this sequence to use as a heterologous morphogenic regulator in an expression cassette.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to KELSEY L. MCWILLIAMS whose telephone number is (703)756-4704. The examiner can normally be reached M-F 08:00-17:30.
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/KELSEY L MCWILLIAMS/Examiner, Art Unit 1663
/Anne Kubelik/Primary Examiner, Art Unit 1663
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