DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
The examiner of your application in the USPTO has changed. To aid in correlating any papers for this application, all further correspondence regarding this application should be directed to Joseph Spangler in Art Unit 1656.
Claims 1-5, 7-10, 13, 16-20, 23-24 and 27 are pending.
Applicant’s amendment to the claims filed 08/12/2026 is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Election
Applicant’s election with traverse of
Group I, claims 1-5, 7-10, 13 and 16-19, drawn to the technical feature of a genetically engineered yeast cell capable of producing xylitol, the engineered yeast cell comprising an exogenous polynucleotide sequence encoding a xylulokinase (XKS) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 8 and 20
in the reply filed 08/12/2026 is acknowledged.
The traversal is on the grounds that the shared same or corresponding technical feature between the inventions of Groups I and II should be the yeast cell recited in claim 1 requiring an exogenous XKS enzyme sharing at least 80% identity with at least one of SEQ ID NOs: 8 and 20, wherein the recited XKS enzyme is not disclosed by Toivari et al. (Appl Environ Microbiol, 2007, 73:5471; cited on the IDS filed 11/07/2024; herein Toivari). Applicant further contends the method of Group II requires the cell of claim 1 and therefore the inventions are not unrelated and do not require separate search and examination.
Applicant’s arguments regarding the teachings of Toivari are found persuasive. Applicant’s arguments regarding the lack of requirement for restriction because the invention of Group II requires the cell of claim 1 is found not convincing. Requirement for restriction under 35 USC 372 is based on the lack of unity, and related inventions such as those identified as Groups I and II in the requirement for restriction can be considered to have a lack of unity if the groups do not share a common technical feature, or if their shared technical feature is determined not to be a special technical feature as it is not contributing over the prior art of record. As shown in the prior art rejection under 35 USC 102 below, the shared technical feature of a genetically engineered yeast cell capable of producing xylitol, the engineered yeast cell comprising an exogenous polynucleotide sequence encoding a xylulokinase (XKS) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 8 and 20 is not a special technical feature as it does not contribute over the prior art.
Therefore, the requirement is still deemed proper and is therefore made FINAL.
Applicant’s election with traverse of
the species of Moniliella and Moniliella pollinis for the yeast cells,
the species of SEQ ID NO: 8 for the sugar phosphate enzyme,
the species of SEQ ID NO: 1 for the XDH enzyme,
the species of ER1 locus for the yeast cell genome locus, and
the species of PYK1p corresponding to SEQ ID NO: 61 for the promoter
in the reply filed 08/12/2026 is acknowledged.
The traversal is on the grounds that the species election requirement is not warranted as the species are presented within common generic claim frameworks directed to engineered yeast cells, XKS-related sequences, XDH-related sequences, integration loci, and promoters used in the same xylitol-production technology.
Applicant’s arguments are persuasive, and the requirement for species election is withdrawn.
Claims 20, 23-24 and 27 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made with traverse in the reply filed on 08/12/2026.
Claims 1-5, 7-10, 13 and 16-19 are being examined on the merits only to the extent they read on the elected subject matter.
Priority
The instant application is a national stage filing under 35 U.S.C. 371 of international application PCT/US2023/066627 filed on 05/05/2023, which claims domestic priority to U.S. Application No. 63/364,363 filed on 05/09/2022.
Information Disclosure Statement
The Information Disclosure Statements (IDSs) submitted on 11/07/2024, 05/12/2025, 05/12/2025 and 05/12/2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDSs have been considered by the examiner.
Non-Patent Literature Document 13 on the IDS filed 11/07/2024 has been lined through because there is no reference with the title "Moniliella megachiliensis using nonrefined glycerol waste as carbon source" in the application file.
Non-Patent Literature Documents 19 and 22 on the IDS filed 05/12/2025 have been lined through because there is no copy of these references in the application file.
Objections to Specification
The disclosure is objected to because of the following informalities.
The use of the term GENESYS 20, which is a trade name or mark used in commerce, have been noted in this application in paragraphs 0077, 0081, 0086, 0091, and 0096. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Appropriate correction is required.
Claim Objections
Claims 1, 13 and 16-19 are objected for the phrase “a sequence at least … % identical to”. In the interest of improving claim form, Applicant should consider an amendment to recite “an amino acid sequence having … % identity with.”
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
Claims 1-5, 7-10, 13 and 16-19 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
Claim 1 (claims 2-5, 7-10, 13 and 16-19 dependent therefrom) is indefinite for the phrase “a xylulokinase (XKS) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 8 and 20”, as this limitation encompasses an embodiment where the amino acid sequence of the XKS enzyme is 100% identical to both SEQ ID NOs: 8 and 20, while SEQ ID NOs: 8 and 20 are not identical to each other.
Claim 9 recites the limitations “the ER1 locus”, “the ER3 locus”, “the PDC1 locus”, “the pyrF locus”, “the TRP3” locus, “the gpdIIA locus”, and “the gpdIIB” locus. There is insufficient antecedent basis for these limitations in the claim.
Claim 10 is indefinite for the recitation of “pyruvate kinase 1 promoter (PYK1p; SEQ ID NO:61), 6-phosphogluconate dehydrogenase promoter (6PGDp; SEQ ID NO:52), glyceraldehyde-3-phosphate dehydrogenase promoter (TDH3p; SEQ ID NO:54), translational elongation factor 1 promoter (TEFp; SEQ ID NO:55), modified TEFp (SEQ ID NO:53), phosphoglucomutase 1 promoter (PGM1p; SEQ ID NO:56), 3-phosphoglycerate kinase promoter (PGK1p; SEQ ID NO:57), enolase promoter (ENO1p; SEQ ID NO:58), asparagine synthetase promoter (ASNSp; SEQ ID NO:59), 50S ribosomal protein L1 promoter (RPLAp; SEQ ID NO:60), and RPL16B (SEQ ID NO:62)”, as the phrases comprising SEQ ID NOs and gene names in parentheses are narrower embodiments of the generic version of each promoter recited before the parentheses, and it is unclear whether the phrases in parentheses are intended to be limiting or exemplary according to MPEP 2173.05(d).
Claim 13 (claims 18-19 dependent therefrom) is indefinite for the phrase “a xylitol dehydrogenase (XDH) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 1, 13 and 14”, as this limitation encompasses an embodiment where the enzyme is 100% identical to all three of SEQ ID NOs: 1, 13 and 14, while SEQ ID NOs: 1, 13 and 14 are not identical to each other.
Claims 16-17 recite the limitation “the sugar phosphatase enzyme”. There is insufficient antecedent basis for this limitation in the claims.
Claim 16 is indefinite for the phrase “the sugar phosphatase enzyme has a sequence at least 85% identical to at least one of SEQ ID NOs: 8 and 20”, as this limitation encompasses an embodiment where the enzyme is 100% identical to both SEQ ID NOs: 8 and 20, while SEQ ID NOs: 8 and 20 are not identical to each other.
Claim 17 is indefinite for the phrase “the sugar phosphatase enzyme has a sequence at least 90% identical to at least one of SEQ ID NOs: 8 and 20”, as this limitation encompasses an embodiment where the enzyme is 100% identical to both SEQ ID NOs: 8 and 20, while SEQ ID NOs: 8 and 20 are not identical to each other.
Claim 18 is indefinite for the phrase “the XDH enzyme has a sequence at least 85% identical to at least one of SEQ ID NOs: 1, 13 and 14”, as this limitation encompasses an embodiment where the enzyme is 100% identical to all three of SEQ ID NOs: 1, 13 and 14, while SEQ ID NOs: 1, 13 and 14 are not identical to each other.
Claim 19 is indefinite for the phrase “the XDH enzyme has a sequence at least 90% identical to at least one of SEQ ID NOs: 1, 13 and 14”, as this limitation encompasses an embodiment where the enzyme is 100% identical to all three of SEQ ID NOs: 1, 13 and 14, while SEQ ID NOs: 1, 13 and 14 are not identical to each other.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1, 8 and 16-17 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Applicant’s attention is directed to the "Guidance for Determining Subject Matter Eligibility Of Claims Reciting Or Involving Laws of Nature, Natural Phenomena, & Natural Products”, released on December 16, 2014.
Claim Interpretation: Claim 1 is drawn to a genetically engineered yeast cell capable of producing xylitol, the engineered yeast cell comprising an exogenous polynucleotide sequence encoding a xylulokinase (XKS) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 8 and 20. Claims 16-17 further limit the cell to have a sugar phosphatase enzyme with a sequence that is at least 85% and 90% identical, respectively, to at least one of SEQ ID NOs: 8 and 20. UniProt Accession No. DOG1_YEAST (3 pages, 29 Sep 2021; cited on the attached Form PTO-892; herein UNI1) discloses a Saccharomyces cerevisiae cell comprising an enzyme having sugar phosphatase activity that shares 100% identity with SEQ ID NO: 8 [see Appendix A]. The limitations “genetically engineered yeast cell” and “exogenous polynucleotide sequence” are considered product-by-process limitations according to MPEP 2113.I that are drawn to the method of making the claimed yeast cell, and do not impart any structural limitations on the cell. The limitation of the yeast cell being capable of producing xylitol is a functional limitation according to MPEP 2173.05(g) which does not structurally limit the claimed cell. As the cell of UNI1 satisfies all of the structural limitations of the claimed cell of a yeast cell comprising an XKS enzyme that shares >80% identity with at least one of SEQ ID NOs: 8 and 20, the cell of UNI1 is presumed to have the capability of producing xylitol, as the capability for xylitol production is presumed to be inherent to the structure of the cell according to MPEP 2112.
Claim 8 limits the cell of claim 1 to be capable of producing xylitol at a titer of at least 1.0 g/L when used in a fermentation process in the presence of dextrose for 96 hours. The limitations of claim 8 are considered to be functional limitations as described above and are drawn to an intended use of the cell according to MPEP 2111.02.II. Therefore the limitations of the claim do not structurally limit the cell.
Given a broadest reasonable interpretation, claims 1, 8 and 16-17 are directed to a naturally-occurring Saccharomyces cerevisiae cell.
Patent Eligibility Analysis Step 1: The claims are drawn to a composition of matter, which is one of the statutory categories of invention.
Patent Eligibility Analysis Step 2A Prong 1: The claims recite a naturally occurring bacteria, which is considered to be a law of nature or natural phenomena (a natural product). Accordingly, claims 1-2, 8 and 16-17 are directed to a judicial exception.
Patent Eligibility Analysis Step 2A Prong 2: There are no additional elements recited in the claims beyond the judicial exception.
Patent Eligibility Analysis Step 2B: The claims only recite the product of nature, without more and do not include any additional elements that could add significantly more to the judicial exception.
As such, the claims do not qualify as eligible subject matter. For these reasons the claim is rejected under section 101 as being directed to non-statutory subject matter.
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 1, 8 and 16-17 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Accession No. DOG1_YEAST (3 pages, 29 Sep 2021; cited on the attached Form PTO-892; herein UNI1).
Claim 1 is drawn to a genetically engineered yeast cell capable of producing xylitol, the engineered yeast cell comprising an exogenous polynucleotide sequence encoding a xylulokinase (XKS) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 8 and 20.
Claim 8 is drawn to the yeast cell of claim 1, wherein the yeast cell is capable of producing xylitol at a titer of at least 1.0 g/L when used in a fermentation process in the presence of dextrose for 96 hours.
Claim 16 is drawn to the yeast cell of claim 1, wherein the sugar phosphatase enzyme has a sequence at least 85% identical to at least one of SEQ ID NOs: 8 and 20.
Claim 17 is drawn to the yeast cell of claim 1, wherein the sugar phosphatase enzyme has a sequence at least 90% identical to at least one of SEQ ID NOs: 8 and 20.
Regarding claim 1, UNI1 discloses a Saccharomyces cerevisiae cell comprising an enzyme having sugar phosphatase activity that shares 100% identity with SEQ ID NO: 8 [see Appendix A], which is understood to be a yeast cell. The limitations “genetically engineered yeast cell” and “exogenous polynucleotide sequence” are considered product-by-process limitations according to MPEP 2113.I that are drawn to the method of making the claimed yeast cell, and do not impart any structural limitations on the cell. The limitation of the yeast cell being capable of producing xylitol is a functional limitation according to MPEP 2173.05(g) which does not structurally limit the claimed cell. As the cell of UNI1 satisfies all of the structural limitations of the claimed cell of a yeast cell comprising an XKS enzyme that shares >80% identity with at least one of SEQ ID NOs: 8 and 20, the cell of UNI1 is presumed to have the capability of producing xylitol, as the capability for xylitol production is presumed to be inherent to the structure of the cell according to MPEP 2112.
Regarding claim 8, the limitations of the claim are considered to be functional limitations according to MPEP 2173.05(g), and these limitations are drawn to an intended use of the cell according to MPEP 2111.02.II. Therefore, as the limitations of claim 8 do not structurally limit the cell, UNI1 satisfies the structural limitations of the claimed cell as discussed in the rejection of claim 1.
Regarding claims 16-17, for the sake of compact prosecution, the recited “sugar phosphatase” enzyme in the claims is being interpreted to correspond to the recited XKS enzyme in claim 1. UNI1 discloses a Saccharomyces cerevisiae cell comprising an enzyme that shares 100% identity with SEQ ID NO: 8 [see Appendix A].
For these reasons, UNI1 anticipates claims 1, 8 and 16-17.
Claim Rejections - 35 USC § 103
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.
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 2-5 and 7 are rejected under 35 U.S.C. 103 as being unpatentable over UNI1 in view of Rzechonek et al. (Crit Rev Biotechnol, 2018, 38:620; cited on the IDS filed 05/12/2025; herein Rzechonek), Toivari et al. (Appl Environ Microbiol, 2007, 73:5471; cited on the IDS filed 11/07/2024) and evidentiary reference Kurtzman et al. (FEMS Yeast Res, 2015, 15:1; cited on the attached Form PTO-892; herein Kurtzman).
Claim 2 is drawn to the yeast cell of claim 1, wherein the yeast cell is an osmotolerant yeast cell.
Claim 3 is drawn to the yeast cell of claim 1, wherein the yeast cell is a cell of the subphylum Ustilaginomycotina.
Claim 4 is drawn to the yeast cell of claim 1, wherein the yeast cell is selected from the group consisting of Trichosporonoides megachiliensis, Trychosporonoides oedocephalis, Trychosporonoides nigrescens, Pseudozyma tsukubaensis, Trigonopsis variabilis, Moniliella, Ustilaginomycetes, Trichosporon, Yarrowia lipolytica, Penicillium, Torula, Pichia, Candida, Candida magnoliae, and Aureobasidium.
Claim 5 is drawn to the yeast cell of claim 1, wherein the yeast cell is of the Moniliella genus.
Claim 7 is drawn to the yeast cell of claim 5, wherein the yeast cell is a Moniliella pollinis cell.
The teachings of UNI1 as applied to claims 1, 8 and 16-17 are discussed above. UNI1 does not teach a yeast cell of the subphylum Ustilaginomycotina.
Rzechonek relates to recent advances in the biological production of erythritol [title] and discusses the production of erythritol along with other polyols such as xylitol for use as sugar substitutes [p 621, col 1, para 1] in industrial settings by yeast-like fungi such as Moniliella pollinis [p 622, col 2, para 2].
Regarding claim 2, Rzechonek teaches polyols function as osmolytes that maintain cell fluid balance as a response to osmotic stress [p 624, col 1, final paragraph; col 2, para 1], and further teaches the optimization of erythritol production has been successful in Moniliella tomentosa var. Pollinis [p 626, col 1, para 2] which is considered to correspond to Moniliella pollinis that is an osmotolerant member of the Ustilaginomycotina subphylum as evidenced by Kurtzman [p 13, col 2, para 1]. Rzechonek teaches further improvements in polyol production can be achieved by modifying organisms via genetic engineering [p 629, col 1, para 2].
Toivari relates to engineering Saccharomyces cerevisiae to produce xylitol [title], and discusses that while xylitol can be reduced from xylose, glucose is a cheaper substrate compared to xylose, and therefore the production of xylitol from glucose would be attractive [p 5471, col1, paras 1-2].
Regarding claim 2, Toivari teaches the enzyme referred to as Dog1p encoded by the gene DOG1 from Saccharomyces cerevisiae [p 5472, col 2, para 2], which is considered to correspond to the enzyme disclosed by UNI1, can catalyze the dephosphorylation of xylulose-5-P (Xu5P) to xylulose for the production of xylitol from the carbon source glucose [Figure 1].
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to combine UNI1 and Rzechonek by inserting the enzyme of UNI1 into the yeast cell of Rzechonek to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to insert the enzyme of UNI1 into the cell of Rzechonek because Rzechonek teaches improvements in polyol production can be achieved by modifying osmotolerant organisms such as Moniliella pollinis via genetic engineering, and Toivari teaches the enzyme of UNI1 participates in the production of the polyol xylitol from a cheaper carbon source of glucose. One of ordinary skill in the art would have had a reasonable expectation of success because UNI1 and Toivari relate to the DOG1-encoded protein of S. cerevisiae, and Rzechonek and Toivari relate to genetically modifying yeast to optimize polyol production.
Regarding claims 3-5 and 7, Rzechonek teaches a Moniliella pollinis cell that is a member of the Ustilaginomycotina subphylum as evidenced by Kurtzman [p 13, col 2, para 1].
Therefore, the invention of claims 2-5 and 7 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claim 9 is rejected under 35 U.S.C. 103 as being unpatentable over UNI1, Rzechonek and Toivari as applied to claims 2-5 and 7 above, and further in view of Ishida et al. (Appl Environ Microbiol, 2005, 71:1964; cited on the attached Form PTO-892; herein Ishida).
Claim 9 is drawn to the yeast cell of claim 1, wherein the exogenous polynucleotide sequence is integrated into the genome of the yeast cell at a locus selected from the ER1 locus, the ER3 locus, the PDC1 locus, the pyrF locus, the TRP3 locus, the gpdIIA locus, and the gpdIIB locus.
The combined teachings of UNI1, Rzechonek and Toivari as applied to claims 1-5, 7-8 and 16-17 are discussed above. These references do not teach integration into the genome of a yeast cell at the loci recited in the claim.
Ishida relates to metabolically engineered Saccharomyces cerevisiae via genome integration [title].
Regarding claim 9, Ishida teaches the metabolic engineering of the yeast S. cerevisiae through replacement of the PDC1 coding region with a gene of interest LDH via homologous recombination to efficiently produce lactic acid under the control of the native PDC1 promoter [abstract].
In view of Ishida, it would have been prima facie obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of UNI1, Rzechonek and Toivari by integrating the gene encoding the enzyme of UNI1 into the genome of the cell, as taught by Ishida to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of UNI1, Rzechonek and Toivari because Ishida teaches the genome integration of an exogenous gene results in efficient activity of the resulting expressed enzyme under the control of a native promoter. One of ordinary skill in the art would have had a reasonable expectation of success because Rzechonek and Ishida relate to genetically modifying yeast cells.
Therefore, the invention of claim 9 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claim 10 is rejected under 35 U.S.C. 103 as being unpatentable over UNI1, Rzechonek and Toivari as applied to claims 2-5 and 7 above, and further in view of Partow et al. (Yeast, 2010, 27:955; cited on the attached Form PTO-892; herein Partow).
Claim 10 is drawn to the yeast cell of claim 1, wherein the exogenous polynucleotide sequence is operably linked to a heterologous or artificial promoter selected from the group consisting of pyruvate kinase 1 promoter (PYK1p; SEQ ID NO:61), 6-phosphogluconate dehydrogenase promoter (6PGDp; SEQ ID NO:52), glyceraldehyde-3-phosphate dehydrogenase promoter (TDH3p; SEQ ID NO:54), translational elongation factor 1 promoter (TEFp; SEQ ID NO:55), modified TEFp (SEQ ID NO:53), phosphoglucomutase 1 promoter (PGM1p; SEQ ID NO:56), 3-phosphoglycerate kinase promoter (PGK1p; SEQ ID NO:57), enolase promoter (ENO1p; SEQ ID NO:58), asparagine synthetase promoter (ASNSp; SEQ ID NO:59), 50S ribosomal protein L1 promoter (RPLAp; SEQ ID NO:60), and RPL16B (SEQ ID NO:62).
In view of the indefiniteness of the claim set forth above, and for the sake of compact prosecution, the limitations in parentheses are being interpreted as non-limiting and exemplary.
The combined teachings of UNI1, Rzechonek and Toivari as applied to claims 1-5, 7-8 and 16-17 are discussed above. These references do not teach the polynucleotide sequence is operably linked to one of the promoters recited in the claim.
Partow relates to different promoters for yeast expression [title] and discusses the use of promoters in expression constructs for different regulation profiles and strengths [p 955, col 1, para 1].
Regarding claim 10, Partow teaches the generation of a polynucleotide comprising a detectable gene-of-interest lacZ whose expression is controlled by various promoters including PYK1 [p 956, col 2, para 2], wherein PYK1 is expressed during growth on glucose [abstract] and PYK1-driven expression of lacZ displayed an activity profile which decreased over time in batch culture [p 957, col 1, final paragraph; Table 2]. Therefore, the polynucleotide of Partow is considered to comprise a gene-of-interest that is operably linked to the PYK1 promoter.
In view of Partow, it would have been prima facie obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of UNI1, Rzechonek and Toivari by operably linking the UNI1 gene to the PYK1 promoter of Partow to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of UNI1, Rzechonek and Toivari because Partow teaches a method to operably link a gene-of-interest to the PYK1 promoter that results in gene expression during growth on glucose. One of ordinary skill in the art would have had a reasonable expectation of success because Toivari relates to genetically engineering yeast to produce polyols from glucose, and Partow relates to genetically engineering yeast to express specific genes when grown on glucose.
Therefore, the invention of claim 10 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claims 13 and 18-19 are rejected under 35 U.S.C. 103 as being unpatentable over UNI1, Rzechonek and Toivari as applied to claims 2-5 and 7 above, and further in view of UniProt Accession No. XYL2_PICST (3 pages, 29 Sep 2021; cited on the attached Form PTO-892; herein UNI2).
Claim 13 is drawn to the yeast cell of claim 1, wherein the yeast cell additionally comprises an exogenous polynucleotide sequence encoding a xylitol dehydrogenase (XDH) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs:1, 13, and 14.
Claim 18 is drawn to the yeast cell of claim 13, wherein the XDH enzyme has a sequence at least 85% identical to at least one of SEQ ID NOs:1, 13, and 14.
Claim 19 is drawn to the yeast cell of claim 13, wherein the XDH enzyme has a sequence at least 90% identical to at least one of SEQ ID NOs:1, 13, and 14.
The combined teachings of UNI1, Rzechonek and Toivari as applied to claims 1-5, 7-8 and 16-17 are discussed above. These references do not teach the yeast cell additionally comprises an exogenous polynucleotide sequence encoding a xylitol dehydrogenase (XDH) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs:1, 13, and 14.
Regarding claim 13, Toivari teaches the XDH enzyme is responsible for generating xylitol by reducing the xylulose produced from dephosphorylation of Xu5P by Dog1p [Figure 1] as discussed further in the rejection of claim 2 above.
Regarding claim 13, UNI2 discloses a xylitol dehydrogenase from Scheffersomyces stipitis which shares 97.1% identity with SEQ ID NO: 1 [see Appendix B].
In view of UNI2, it would have been prima facie obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of UNI1, Rzechonek and Toivari by engineering the combined cell to express the XDH of UNI2, as taught by Toivari, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of UNI1, Rzechonek and Toivari because Rzechonek teaches optimization of polyol production can be achieved by genetic modification of yeast cells, Toivari teaches the production of xylitol from glucose requires the XDH enzyme, and UNI2 teaches an XDH enzyme. One of ordinary skill in the art would have had a reasonable expectation of success because Toivari and UNI2 relate XDH enzymes.
Regarding claims 18-19, UNI2 discloses a xylitol dehydrogenase from Scheffersomyces stipitis which shares 97.1% identity with SEQ ID NO: 1 [see Appendix B].
Therefore, the invention of claim 13 and 18-19 would have been obvious to one of ordinary skill in the art before the effective filing date.
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.
A. Claims 1, 8 and 16-17 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,702 (herein “reference application”) in view of Toivari and UNI1.
Regarding instant claim 1, claim 1 of the reference application recites a genetically engineered yeast cell capable of producing xylitol.
The claims of the reference application do not recite the yeast cell comprises an exogenous polynucleotide sequence encoding a xylulokinase (XKS) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 8 and 20.
Toivari relates to engineering Saccharomyces cerevisiae to produce xylitol [title], and discusses that while xylitol can be reduced from xylose, glucose is a cheaper substrate compared to xylose, and therefore the production of xylitol from glucose would be attractive [p 5471, col1, paras 1-2].
Regarding instant claim 1, Toivari discloses the enzyme referred to as Dog1p encoded by the gene DOG1 from Saccharomyces cerevisiae [p 5472, col 2, para 2] can catalyze the dephosphorylation of xylulose-5-P (Xu5P) to xylulose for the production of xylitol from the carbon source glucose [Figure 1], wherein the Dog1p enzyme is considered to correspond to the enzyme of UNI1 that shares 100% identity with SEQ ID NO: 8 [see Appendix A].
In view of Toivari and UNI1, it would have been obvious for one of ordinary skill in the art before the effective filing date to modify the claims of the reference application by adding the enzyme of UNI1 to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the claims of the reference application because Toivari discloses the enzyme of UNI1 participates in the production of the xylitol from a cheaper carbon source of glucose. One of ordinary skill in the art would have had a reasonable expectation of success because the reference application and Toivari relate to yeast cells that produce xylitol, and Toivari and UNI1 relate to enzymes that participate in the production of xylitol.
Regarding instant claim 8, the limitations of the claim are considered to be functional limitations according to MPEP 2173.05(g), and these limitations are drawn to an intended use of the cell according to MPEP 2111.02.II. Therefore, as the limitations of instant claim 8 do not structurally limit the cell, UNI1 satisfies the structural limitations of the claimed cell as discussed in the rejection of instant claim 1.
Regarding instant claims 16-17, for the sake of compact prosecution, the recited “sugar phosphatase” enzyme in the claims is being interpreted to correspond to the recited XKS enzyme in instant claim 1. UNI1 discloses a Saccharomyces cerevisiae cell comprising an enzyme that shares 100% identity with SEQ ID NO: 8 [see Appendix A].
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 2-5 and 7 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,702 (herein “reference application”) in view of Toivari and UNI1 as applied to claims 1, 8 and 16-17 above, and further in view of Rzechonek and evidentiary reference Kurtzman.
The claims of the reference application and disclosures of UNI1 and Toivari as applied to claims 1, 8 and 16-17 are discussed above. The claims of the reference application do not recite a yeast cell of the subphylum Ustilaginomycotina.
Rzechonek relates to recent advances in the biological production of erythritol [title] and discusses the production of erythritol along with other polyols such as xylitol for use as sugar substitutes [p 621, col 1, para 1] in industrial settings by yeast-like fungi such as Moniliella pollinis [p 622, col 2, para 2].
Regarding instant claim 2, Rzechonek discloses polyols function as osmolytes that maintain cell fluid balance as a response to osmotic stress [p 624, col 1, final paragraph; col 2, para 1], and further discloses the optimization of erythritol production has been successful in Moniliella tomentosa var. Pollinis [p 626, col 1, para 2] which is considered to correspond to Moniliella pollinis that is an osmotolerant member of the Ustilaginomycotina subphylum as evidenced by Kurtzman [p 13, col 2, para 1]. Rzechonek discloses further improvements in polyol production can be achieved by modifying organisms via genetic engineering [p 629, col 1, para 2].
In view of Rzechonek, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the combined cell of the reference application, UNI1 and Toivari by using the cell of Rzechonek to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of the reference application, UNI1 and Toivari because Rzechonek discloses improvements in polyol production can be achieved by modifying osmotolerant organisms such as Moniliella pollinis via genetic engineering. One of ordinary skill in the art would have had a reasonable expectation of success because Rzechonek and Toivari relate to genetically modifying yeast to optimize polyol production.
Regarding instant claims 3-5 and 7, Rzechonek discloses a Moniliella pollinis cell that is a member of the Ustilaginomycotina subphylum as evidenced by Kurtzman [p 13, col 2, para 1].
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claim 9 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,702 (herein “reference application”) in view of Toivari and UNI1 as applied to claims 1, 8 and 16-17 above, and further in view of Ishida.
The claims of the reference application and disclosures of UNI1 and Toivari as applied to claims 1, 8 and 16-17 are discussed above. The claims of the reference application do not recite integration into the genome of a yeast cell at the loci recited in the claim.
Ishida relates to metabolically engineered Saccharomyces cerevisiae via genome integration [title].
Regarding instant claim 9, Ishida discloses the metabolic engineering of the yeast S. cerevisiae through replacement of the PDC1 coding region with a gene of interest LDH via homologous recombination to efficiently produce lactic acid under the control of the native PDC1 promoter [abstract].
In view of Ishida, it would have been obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of the reference application, UNI1 and Toivari by integrating the gene encoding the enzyme of UNI1 into the genome of the cell, as disclosed by Ishida to arrive at the claimed invention. One of ordinary skill in the art would have been motivated modify the combined cell of the reference application, UNI1 and Toivari because Ishida discloses the genome integration of an exogenous gene results in efficient activity of the resulting expressed enzyme under the control of a native promoter. One of ordinary skill in the art would have had a reasonable expectation of success because Toivari and Ishida relate to genetically modifying yeast cells.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claim 10 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,702 (herein “reference application”) in view of Toivari and UNI1 as applied to claims 1, 8 and 16-17 above, and further in view of Partow.
The claims of the reference application and disclosures of UNI1 and Toivari as applied to claims 1, 8 and 16-17 are discussed above. The claims of the reference application do not recite the polynucleotide sequence is operably linked to one of the promoters recited in the claim.
Partow relates to different promoters for yeast expression [title] and discusses the use of promoters in expression constructs for different regulation profiles and strengths [p 955, col 1, para 1].
Regarding instant claim 10, Partow discloses the generation of a polynucleotide comprising a detectable gene-of-interest lacZ whose expression is controlled by various promoters including PYK1 [p 956, col 2, para 2], wherein PYK1 is expressed during growth on glucose [abstract] and PYK1-driven expression of lacZ displayed an activity profile which decreased over time in batch culture [p 957, col 1, final paragraph; Table 2]. Therefore, the polynucleotide of Partow is considered to comprise a gene-of-interest that is operably linked to the PYK1 promoter.
In view of Partow, it would have been obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of the reference application, UNI1 and Toivari by operably linking the UNI1 gene to the PYK1 promoter of Partow to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of the reference application, UNI1 and Toivari because Partow discloses a method to operably link a gene-of-interest to the PYK1 promoter that results in gene expression during growth on glucose. One of ordinary skill in the art would have had a reasonable expectation of success because Toivari relates to genetically engineering yeast to produce polyols from glucose, and Partow relates to genetically engineering yeast to express specific genes when grown on glucose.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 13 and 18-19 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,702 (herein “reference application”) in view of Toivari and UNI1 as applied to claims 1, 8 and 16-17 above, and further in view of UNI2.
The claims of the reference application and disclosures of UNI1 and Toivari as applied to claims 1, 8 and 16-17 are discussed above. The claims of the reference application do not recite the yeast cell additionally comprises an exogenous polynucleotide sequence encoding a xylitol dehydrogenase (XDH) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs:1, 13, and 14.
Regarding instant claim 13, Toivari discloses the XDH enzyme is responsible for generating xylitol by reducing the xylulose produced from dephosphorylation of Xu5P by Dog1p [Figure 1] as discussed further in the rejection of claim 2 above.
Regarding instant claim 13, UNI2 discloses a xylitol dehydrogenase from Scheffersomyces stipitis which shares 97.1% identity with SEQ ID NO: 1 [see Appendix B].
In view of UNI2, it would have been obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of the reference application, UNI1 and Toivari by engineering the combined cell to express the XDH of UNI2, as disclosed by Toivari, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of the reference application, UNI1 and Toivari because Toivari discloses the production of xylitol from glucose requires the XDH enzyme, and UNI2 discloses an XDH enzyme. One of ordinary skill in the art would have had a reasonable expectation of success because Toivari and UNI2 relate XDH enzymes.
Regarding instant claims 18-19, UNI2 discloses a xylitol dehydrogenase from Scheffersomyces stipitis which shares 97.1% identity with SEQ ID NO: 1 [see Appendix A].
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
B. Claims 1, 8 and 16-17 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,709 (herein “reference application”) in view of Toivari and UNI1.
Regarding instant claim 1, claim 1 of the reference application recites a genetically engineered yeast cell capable of producing xylitol.
The claims of the reference application do not recite the yeast cell comprises an exogenous polynucleotide sequence encoding a xylulokinase (XKS) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 8 and 20.
Toivari relates to engineering Saccharomyces cerevisiae to produce xylitol [title], and discusses that while xylitol can be reduced from xylose, glucose is a cheaper substrate compared to xylose, and therefore the production of xylitol from glucose would be attractive [p 5471, col1, paras 1-2].
Regarding instant claim 1, Toivari discloses the enzyme referred to as Dog1p encoded by the gene DOG1 from Saccharomyces cerevisiae [p 5472, col 2, para 2] can catalyze the dephosphorylation of xylulose-5-P (Xu5P) to xylulose for the production of xylitol from the carbon source glucose [Figure 1], wherein the Dog1p enzyme is considered to correspond to the enzyme of UNI1 that shares 100% identity with SEQ ID NO: 8 [see Appendix A].
In view of Toivari and UNI1, it would have been obvious for one of ordinary skill in the art before the effective filing date to modify the claims of the reference application by adding the enzyme of UNI1 to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the claims of the reference application because Toivari discloses the enzyme of UNI1 participates in the production of the xylitol from a cheaper carbon source of glucose. One of ordinary skill in the art would have had a reasonable expectation of success because the reference application and Toivari relate to yeast cells that produce xylitol, and Toivari and UNI1 relate to enzymes that participate in the production of xylitol.
Regarding instant claim 8, the limitations of the claim are considered to be functional limitations according to MPEP 2173.05(g), and these limitations are drawn to an intended use of the cell according to MPEP 2111.02.II. Therefore, as the limitations of instant claim 8 do not structurally limit the cell, UNI1 satisfies the structural limitations of the claimed cell as discussed in the rejection of instant claim 1.
Regarding instant claims 16-17, for the sake of compact prosecution, the recited “sugar phosphatase” enzyme in the claims is being interpreted to correspond to the recited XKS enzyme in instant claim 1. UNI1 discloses a Saccharomyces cerevisiae cell comprising an enzyme that shares 100% identity with SEQ ID NO: 8 [see Appendix A].
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 2-5 and 7 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,709 (herein “reference application”) in view of Toivari and UNI1 as applied to claims 1, 8 and 16-17 above, and further in view of Rzechonek and evidentiary reference Kurtzman.
The claims of the reference application and disclosures of UNI1 and Toivari as applied to claims 1, 8 and 16-17 are discussed above. The claims of the reference application do not recite a yeast cell of the subphylum Ustilaginomycotina.
Rzechonek relates to recent advances in the biological production of erythritol [title] and discusses the production of erythritol along with other polyols such as xylitol for use as sugar substitutes [p 621, col 1, para 1] in industrial settings by yeast-like fungi such as Moniliella pollinis [p 622, col 2, para 2].
Regarding instant claim 2, Rzechonek discloses polyols function as osmolytes that maintain cell fluid balance as a response to osmotic stress [p 624, col 1, final paragraph; col 2, para 1], and further discloses the optimization of erythritol production has been successful in Moniliella tomentosa var. Pollinis [p 626, col 1, para 2] which is considered to correspond to Moniliella pollinis that is an osmotolerant member of the Ustilaginomycotina subphylum as evidenced by Kurtzman [p 13, col 2, para 1]. Rzechonek discloses further improvements in polyol production can be achieved by modifying organisms via genetic engineering [p 629, col 1, para 2].
In view of Rzechonek, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the combined cell of the reference application, UNI1 and Toivari by using the cell of Rzechonek to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of the reference application, UNI1 and Toivari because Rzechonek discloses improvements in polyol production can be achieved by modifying osmotolerant organisms such as Moniliella pollinis via genetic engineering. One of ordinary skill in the art would have had a reasonable expectation of success because Rzechonek and Toivari relate to genetically modifying yeast to optimize polyol production.
Regarding instant claims 3-5 and 7, Rzechonek discloses a Moniliella pollinis cell that is a member of the Ustilaginomycotina subphylum as evidenced by Kurtzman [p 13, col 2, para 1].
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claim 9 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,709 (herein “reference application”) in view of Toivari and UNI1 as applied to claims 1, 8 and 16-17 above, and further in view of Ishida.
The claims of the reference application and disclosures of UNI1 and Toivari as applied to claims 1, 8 and 16-17 are discussed above. The claims of the reference application do not recite integration into the genome of a yeast cell at the loci recited in the claim.
Ishida relates to metabolically engineered Saccharomyces cerevisiae via genome integration [title].
Regarding instant claim 9, Ishida discloses the metabolic engineering of the yeast S. cerevisiae through replacement of the PDC1 coding region with a gene of interest LDH via homologous recombination to efficiently produce lactic acid under the control of the native PDC1 promoter [abstract].
In view of Ishida, it would have been obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of the reference application, UNI1 and Toivari by integrating the gene encoding the enzyme of UNI1 into the genome of the cell, as disclosed by Ishida to arrive at the claimed invention. One of ordinary skill in the art would have been motivated modify the combined cell of the reference application, UNI1 and Toivari because Ishida discloses the genome integration of an exogenous gene results in efficient activity of the resulting expressed enzyme under the control of a native promoter. One of ordinary skill in the art would have had a reasonable expectation of success because Toivari and Ishida relate to genetically modifying yeast cells.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claim 10 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,709 (herein “reference application”) in view of Toivari and UNI1 as applied to claims 1, 8 and 16-17 above, and further in view of Partow.
The claims of the reference application and disclosures of UNI1 and Toivari as applied to claims 1, 8 and 16-17 are discussed above. The claims of the reference application do not recite the polynucleotide sequence is operably linked to one of the promoters recited in the claim.
Partow relates to different promoters for yeast expression [title] and discusses the use of promoters in expression constructs for different regulation profiles and strengths [p 955, col 1, para 1].
Regarding instant claim 10, Partow discloses the generation of a polynucleotide comprising a detectable gene-of-interest lacZ whose expression is controlled by various promoters including PYK1 [p 956, col 2, para 2], wherein PYK1 is expressed during growth on glucose [abstract] and PYK1-driven expression of lacZ displayed an activity profile which decreased over time in batch culture [p 957, col 1, final paragraph; Table 2]. Therefore, the polynucleotide of Partow is considered to comprise a gene-of-interest that is operably linked to the PYK1 promoter.
In view of Partow, it would have been obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of the reference application, UNI1 and Toivari by operably linking the UNI1 gene to the PYK1 promoter of Partow to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of the reference application, UNI1 and Toivari because Partow discloses a method to operably link a gene-of-interest to the PYK1 promoter that results in gene expression during growth on glucose. One of ordinary skill in the art would have had a reasonable expectation of success because Toivari relates to genetically engineering yeast to produce polyols from glucose, and Partow relates to genetically engineering yeast to express specific genes when grown on glucose.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 13 and 18-19 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/863,709 (herein “reference application”) in view of Toivari and UNI1 as applied to claims 1, 8 and 16-17 above, and further in view of UNI2.
The claims of the reference application and disclosures of UNI1 and Toivari as applied to claims 1, 8 and 16-17 are discussed above. The claims of the reference application do not recite the yeast cell additionally comprises an exogenous polynucleotide sequence encoding a xylitol dehydrogenase (XDH) enzyme comprising a sequence at least 80% identical to at least one of SEQ ID NOs: 1, 13, and 14.
Regarding instant claim 13, Toivari discloses the XDH enzyme is responsible for generating xylitol by reducing the xylulose produced from dephosphorylation of Xu5P by Dog1p [Figure 1] as discussed further in the rejection of claim 2 above.
Regarding instant claim 13, UNI2 discloses a xylitol dehydrogenase from Scheffersomyces stipitis which shares 97.1% identity with SEQ ID NO: 1 [see Appendix B].
In view of UNI2, it would have been obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined cell of the reference application, UNI1 and Toivari by engineering the combined cell to express the XDH of UNI2, as disclosed by Toivari, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to modify the combined cell of the reference application, UNI1 and Toivari because Toivari discloses the production of xylitol from glucose requires the XDH enzyme, and UNI2 discloses an XDH enzyme. One of ordinary skill in the art would have had a reasonable expectation of success because Toivari and UNI2 relate XDH enzymes.
Regarding instant claims 18-19, UNI2 discloses a xylitol dehydrogenase from Scheffersomyces stipitis which shares 97.1% identity with SEQ ID NO: 1 [see Appendix A].
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Examiner Comment
The polynucleotide sequences of SEQ ID NOs: 52 and 54-60 are free of the prior art of record.
Conclusion
Status of the Application:
Claims 1-5, 7-10, 13, 16-20, 23-24 and 27 are pending.
Claims 20, 23-24 and 27 are withdrawn.
Claims 1-5, 7-10, 13 and 16-19 are rejected.
No claim is in condition for allowance.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JOSEPH SPANGLER whose telephone number is (571)270-0314. The examiner can normally be reached M-F 7:30 am - 4:30 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath Rao can be reached at (571) 272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/JOSEPH R SPANGLER/
Examiner
Art Unit 1656
/David Steadman/Primary Examiner, Art Unit 1656
APPENDIX A
PNG
media_image1.png
455
581
media_image1.png
Greyscale
Sequence alignment of SEQ ID NO: 8 with UniProt Accession No. DOG1_YEAST
APPENDIX B
PNG
media_image2.png
597
561
media_image2.png
Greyscale
Sequence alignment of SEQ ID NO: 1 with UniProt Accession No. XYL2_PICST
