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 .
Priority
This application claims benefit of priority to Provisional Application 63/024,010 filed on 05/13/2020 and is also a 371 of PCT/US2021/032054 filed on 05/12/2021. Support for the instant claims is found in the Provisional Application, therefore, for the purposes applying prior art, the effective filing date of the claimed invention is 05/13/2020.
Information Disclosure Statement
The Information Disclosure Statement of 11/11/2022 is acknowledged and has been considered.
Drawings
The Drawings filed on 11/11/2022 are accepted by the Examiner.
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-18, in the reply filed on 08/19/2025 is acknowledged. Claims 19-20 are withdrawn by the Examiner as they are not encompassed within the elected group.
Applicant’s election without traverse of the L-xylulose reductase of SEQ ID NO: 302, the aldose reductase of SEQ ID NO: 283, the L-arabinitol 4- dehydrogenase of SEQ ID NO: 293, the xylitol dehydrogenase of SEQ ID NO: 309, the glyceraldehyde-3-phosphate dehydrogenase of SEQ ID NO: 273 and xylulokinase as the specific heterologous polynucleotide encoding enzyme, in the reply filed on 08/19/2025 is acknowledged.
Applicant indicates claims 1-18 read upon the election invention and the election of species. However, Applicant elected the xylitol dehydrogenase of SEQ ID NO: 309 regarding species election 4). Therefore, a heterologous polynucleotide encoding a xylulokinase is non-elected and claim 6 is withdrawn by the Examiner as it is not encompassed within the election of species.
Amendments and Claim Status
Claims 1-20 are pending.
Claims 6 and 19-20 are withdrawn by the Examiner as they are not encompassed by the elections made on 08/19/2025.
Claims 1-5 and 7-18 are under examination.
Claim Objections
Claim 7 is objected to because of the following informalities: Claim 7 recites ‘wherein the cell further comprises heterologous polynucleotide encoding …’ It appears the claim should read ‘wherein the cell further comprises a heterologous polynucleotide encoding …’. Appropriate correction is required.
Claim 14 is objected to because of the following informalities: Claim 14 recites ‘wherein the cell is capable of higher anaerobic growth rate …’ It appears the claim should read ‘wherein the cell is capable of a higher anaerobic growth rate …’. Appropriate correction is required.
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.
Claims 1, 4, 9-11, 14-16 and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Zhao et al. (US 20130295631 A1, 11/07/2013) (IDS Reference of 11/11/2022) (hereinafter Zhao et al. of ‘631) in view of Mojzita et al. (FEBS Letters, 07/21/2010) (IDS Reference of 11/11/2022).
Regarding claims 1, 4 and 10-11, Zhao et al. of ‘631 disclose methods for assembly and selection of multi-step xylose and arabinose/xylose utilization from a library of fungal enzymes (See entire document, More specifically, the Abstract). The disclosure further relates to the production of highly efficient heterologous pathways in host cells by identifying favorable enzyme and promoter combinations, more specifically, recombinant yeast cells expressing such combinations (Paragraph [0001]). In a specific embodiment, Zhao et al. of ‘631 disclose the arabinose-utilization pathway containing the enzymes xylose reductase, xylitol dehydrogenase, xylulokinase, L-arabitol 4-dehydrogenase and L-xylulose reductase (Paragraph [0075]). Xylose reductase is another name for aldose reductase (Paragraph [0076]). The host cell is cultured in a composition comprising xylose and/or arabinose under conditions to produce ethanol (Paragraph [0014]).
Zhao et al. of ‘631 do not disclose wherein the L-xylulose reductase has at least 80% sequence identity to instant SEQ ID NO: 302.
However, Mojzita et al. disclose an L-xylulose reductase from Aspergillus niger with gene name lxrA (Abstract). Mojzita et al. also disclose L-xylulose reductase is part of the pathway for L-arabinose and the lxrA gene was upregulated on L-arabinose (Abstract). Confirming the activity of the lxrA gene, Mojzita et al. disclose when the lxrA gene was deleted, the strain lacked L-xylulose reductase activity (Abstract). The lxrA gene shares 80.2% sequence identity to instant SEQ ID NO: 302. An alignment of SEQ ID NO: 302 (Qy) and the lxrA gene (Db) is provided below.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the L-xylulose reductase of Mojzita et al. in the host cell of Zhao et al. of ’631 because it is known L-xylulose reductase is part of the arabinose pathway and the host cell does not require a specific L-xylulose reductase and the L-xylulose reductase of Mojzita et al. was a known and effective L-xylulose disclosed in the prior art.
Regarding claims 9-11, Zhao et al. of ‘631 disclose in one embodiment, the pathway is a xylose utilization pathway containing a xylose reductase, a xylitol dehydrogenase and a xylulokinase (Paragraph [0075]).
Regarding claims 14-16, Zhao et al. of ‘631 do not explicitly disclose wherein the cell is capable of a higher anaerobic growth rate on xylose compared to the same cell without the LXR, the cell is capable of a higher rate of xylose consumption compared to the same cell without the LXR or the cell is capable of higher xylose consumption compared to the same cell without the LXR at 120 hours of fermentation.
However, it appears these would be inherent characteristics of the host cell of combined Zhao et al. of ‘631/Mojzita et al. It is noted the instant Specification discloses ‘the recombinant cell is capable of higher anaerobic growth rate on a pentose (e.g., xylose and/or arabinose) compared to the same cell without the heterologous polynucleotide encoding L-xyluluose reductase’ and ‘ the recombinant cell is capable of higher anaerobic growth rate on pentose (e.g., xylose and/or arabinose) compared to the same cell encoding the L-xylulose reductase of SEQ ID NO. 305’ (Page 45, Lines 17-25). Therefore, it appears as though a recombinant cell having a heterologous polynucleotide encoding an aldose reductase, an L-arabinitol 4-dehydrogenase and an L-xylulose reductase with at least 80% sequence identity to instant SEQ ID NO. 302 would inherently have the properties disclosed above. As the host cell of Zhao et al. of ‘631/Mojzita et al. contains all three of the just mentioned enzymes, absent evidence to the contrary, it reads on the cell being capable of a higher anaerobic growth rate on xylose compared to the same cell without the LXR, the cell being capable of a higher rate of xylose consumption compared to the same cell without the LXR and the cell being capable of higher xylose consumption compared to the same cell without the LXR at 120 hours of fermentation
Regarding claim 18, Zhao et al. of ‘631 disclose the host cell can be Saccharomyces cerevisiae (Paragraph [0014]).
Claims 1-2, 4, 9-11, 14-16 and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Zhao et al. (US 20130295631 A1, 11/07/2013) (IDS Reference of 11/11/2022) (hereinafter Zhao et al. of ‘631) in view of Mojzita et al. (FEBS Letters, 07/21/2010) (IDS Reference of 11/11/2022) and further in view of Zhao et al. (US 7381553 B2, 06/03/2008) (hereinafter Zhao et al. of ‘553).
The teachings of Zhao et al. of ‘631 and Mojzita et al. are discussed above.
Regarding claim 2, neither Zhao et al. of ‘631 nor Mojzita et al. disclose wherein the aldose reductase, also known as xylose reductase, has at least 80% sequence identity to instant SEQ ID NO: 283.
However, Zhao et al. of ‘553 disclose a highly active xylose reductase from Neurospora crassa (Title), wherein the xylose reductase is represented by SEQ ID NO: 2 (Claim 1 of Zhao et al. of ‘553). SEQ ID NO: 2 of Zhao et al. of ‘553 shares 81.7% sequence identity to instant SEQ ID NO: 283. An alignment of instant SEQ ID NO: 283 (Qy) and SEQ ID NO: 2 of Zhao et al. of ‘553 (Db) is provided below.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the xylose reductase of Zhao et al. of ‘553 in the host cell of Zhao et al. of ‘631/Mojzita et al. because it is known xylose reductase is part of the arabinose pathway and the host cell does not require a specific xylose reductase and the xylose reductase of Zhoa et al. of ‘553 was a known and effective xylose reductase disclosed in the prior art.
Claims 1, 3-4, 9-11, 14-16 and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Zhao et al. of ‘631 (US 20130295631 A1, 11/07/2013) (IDS Reference of 11/11/2022) in view of Mojzita et al. (FEBS Letters, 07/21/2010) (IDS Reference of 11/11/2022) and further in view of UniProt (F8N538, 09/11/2011).
The teachings of Zhao et al. of ‘631 and Mojzita et al. are discussed above.
Regarding claim 3, neither Zhao et al. of ‘631 nor Mojzita et al. disclose wherein the L-arabinitol 4-dehydrogenase has at least 80% sequence identity to instant SEQ ID NO: 293.
However, UniProt discloses F8N538_NEUT8, an L-arabinitol 4-dehydrogenase from Neurospora tetrasperma (UniProt, Page 1). F8N538_NEUT8 of UniProt shares 100% sequence identity to instant SEQ ID NO: 293. An alignment of instant SEQ ID NO: 293 (Qy) and F8N538_NEUT8 of UniProt (Db) is provided below.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the L-arabinitol 4-dehydrogenase of UniProt. in the host cell of Zhao et al. of ‘631/Mojzita et al. because it is known L-arabinitol 4-dehydrogenase is part of the arabinose pathway and the host cell does not require a specific L-arabinitol 4-dehydrogenase and the L-arabinitol 4-dehydrogenase of UniProt was a known and effective L-arabinitol 4-dehydrogenase disclosed in the prior art.
Claims 1, 4-5, 9-11, 14-16 and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Zhao et al. of ‘631 (US 20130295631 A1, 11/07/2013) (IDS Reference of 11/11/2022) in view of Mojzita et al. (FEBS Letters, 07/21/2010) (IDS Reference of 11/11/2022) and further in view of UniProt (B5TYI1, 11/04/2008).
The teachings of Zhao et al. of ‘631 and Mojzita et al. are discussed above.
Regarding claim 5, neither Zhao et al. of ‘631 nor Mojzita et al. disclose wherein the xylitol dehydrogenase has at least 80% sequence identity to instant SEQ ID NO: 309.
However, UniProt discloses B5TYI1_SCHSH, a xylitol dehydrogenase (UniProt, Page 1). B5TYI1_SCHSH of UniProt shares 97.9% sequence identity to instant SEQ ID NO: 309. An alignment of instant SEQ ID NO: 309 (Qy) and B5TYI1_SCHSH of UniProt (Db) is provided below.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the xylitol dehydrogenase of UniProt. in the host cell of Zhao et al. of ‘631/Mojzita et al. because it is known xylitol dehydrogenase is part of the arabinose pathway and the host cell does not require a specific xylitol dehydrogenase and the xylitol dehydrogenase of UniProt was a known and effective xylitol dehydrogenase disclosed in the prior art.
Claim(s) 1, 4, 7-11 and 13-18 are rejected under 35 U.S.C. 103 as being unpatentable over Zhao et al. of ‘631 (US 20130295631 A1, 11/07/2013) (IDS Reference of 11/11/2022) in view of Mojzita et al. (FEBS Letters, 07/21/2010) (IDS Reference of 11/11/2022) and further in view of Marasco et al. (US 20180223271 A1, 08/09/2018).
The teachings of Zhao et al. of ‘631 and Mojzita et al. are discussed above.
Regarding claims 7 and 17, neither Zhao et al. of ‘631 nor Mojzita et al. disclose wherein the cell further comprises a heterologous polynucleotide encoding a non-phosphorylating NADP-dependent glyceraldehyde -3-phosphate dehydrogenase (GAPN) or wherein an endogenous GPD and/or GPP gene is inactivated.
However, Marasco et al. disclose an engineered yeast, reading on a recombinant microorganism, capable of producing a bioproduct, such as ethanol, in a fermentation medium that includes xylose (See entire document, More specifically, the Abstract), while reducing the production of glycerol (Paragraph [0011]). Marasco et al. further disclose an optional genetic modification to the cell is one that affects glycerol-3-phopsphate dehydrogenase (GPD) expression or activity, wherein a GPD gene can be deleted or mutated to eliminate or reduce its activity (Paragraph [0105]). Further, for strains that have eliminated or reduced GPD expression or activity, a non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) gene can be introduced into the cell (Paragraph [0106]). Marasco et al. disclose two specific strains, strain 40 which has GPD intact and strain 55 where the GPD gene has been deleted and GAPN has been inserted (Table 10-1). Both of the strains produced ethanol, but strain 40, which has GPD intact, produced a significant level of glycerol, while strain 55, which does not have GPD but does have GAPN, did not produce any glycerol (Paragraph [0287)].
As such, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have deleted or mutated, reading on inactivated, GPD and introduced a GAPN gene in the host cell of Zhoa et al. of ‘631/Mojzita et al. motivated by the desire to promote the production of the desired product, ethanol, while also reducing, or eliminating, the production of unwanted products, like glycerol, and inactivating endogenous GPD and introducing a heterologous GAPN gene was a known and effective means for doing so as taught by Marasco et al.
Regarding claim 8, neither Zhao et al. of ‘631 nor Mojzita et al. disclose wherein the GAPN has a sequence with 80% sequence identity to instant SEQ ID NO. 273.
However, Marasco et al. disclose SEQ ID NO. 79, a non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (Paragraph [0241]). SEQ ID NO. 79 of Marasco et al. shares 91.0% sequence identity to instant SEQ ID NO. 273. An alignment of instant SEQ ID NO: 273 (Qy) and SEQ ID NO. 79 of Marasco et al. (Db) is provided below.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase of Marasco et al. in the host cell of Zhao et al. of ‘631/Mojzita et al. because the host cell does not require a specific non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase and the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase of Marasco et al. was a known and effective non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase disclosed in the prior art.
Regarding claim 13, Zhao et al. of ‘631 disclose the pathways of the disclose can be used with other proteins of interest, including multiple different enzymes, one class of enzymes mentioned is amylases.
Neither Zhao et al. of ‘631 nor Mojzita et al. disclose wherein the cell further comprises a heterologous polynucleotide encoding an alpha-amylase.
However, Marasco et al. disclose one or more enzymes can be used for digesting starch, proteins and fats, one of which is alpha-amylase (Paragraph [0161]).
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized alpha-amylase as the amylase used in the arabinose pathway encoded by the host cell of Zhoa et al. of ‘631/Mojzita et al. because it was a known and effective amylase used for digesting starch, proteins and fats in a similar method as disclosed by Marasco et al.
Claims 1, 4, 9-16 and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Zhao et al. (US 20130295631 A1, 11/07/2013) (IDS Reference of 11/11/2022) in view of Mojzita et al. (FEBS Letters, 07/21/2010) (Of Record) as applied to claims … above, and further in view of Skinner et al. (WO 2020115716 A1, 06/11/2020, With priority to 12/07/2018).
The teachings of Zhao et al. and Mojzita et al. are discussed above.
Regarding claims 12-13, neither Zhao et al. of ‘631 nor Mojzita et al. disclose wherein the cell further comprises a heterologous polynucleotide encoding a glucoamylase or an alpha-amylase.
However, Skinner et al. disclose a process for making and improving the yield of a fermented product, such as ethanol, using a recombinant yeast cell (See entire document, More specifically, the Abstract). The recombinant yeast cell can include a genetic modification allowing the expression of a heterologous saccharolytic enzyme, wherein the saccharolytic enzyme can be any enzyme involved in carbohydrate digestion, metabolism and/or hydrolysis, including amylases (Page 37, Paragraph 1). Examples of amylases that can be used include alpha-amylases and glucoamylase (Page 37, Paragraph 1). Skinnner et al. further disclose many microbes produce an amylase to degrade extracellular starches (Page 37, Paragraph 2).
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have a heterologous polynucleotide encoding a glucoamylase or an alpha-amylase in the host cell of Zhao et al. of ‘631/Mojzita et al. because Skinner et al. disclose a similar recombinant yeast cell, also for producing ethanol, that expresses a heterologous alpha-amylase or glucoamylase to degrade extracellular starches motivated by the desire to effectively degrade extracellular starch as taught by Skinner et al.
The Supreme court acknowledged:
When a work is available in one field of endeavor, design incentives and other market forces can prompt variations of it, either in the same field or a different one. If a person of ordinary skill can implement a predictable varition..103 likely bars its patentability…if a technique has been used to improve one device, and a person of ordinary skill in the art would recognize that it would improve similar devices in the same way, using the technique is obvious unless its actual application is beyond that person’s skill. A court must ask whether the improvement is more than the predictable use of prior-art elements according to their established functions…
…the combination of familiar elements according to known methods is likely to be obvious when it does no more than yield predictable results (see KSR International Co. v. Teleflex Inc., 82 USPQ2d 1385 U.S. 2007) emphasis added.
In KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398 (2007), the Supreme Court reaffirmed "the conclusion that when a patent 'simply arranges old elements with each performing the same function it had been known to perform' and yields no more than one would expect from such an arrangement, the combination is obvious." Id. at 417 (quoting Sakraida v. Ag Pro, Inc., 425 U.S. 273,282 (1976)). The Supreme Court also emphasized a flexible approach to the obviousness question, stating that the analysis under 35 U.S.C. § 103 "need not seek out precise teachings directed to the specific subject matter of the challenged claim, for a court can take account of the inferences and creative steps that a person of ordinary skill in the art would employ." Id. at 418; see also id. at 421 ("A person of ordinary skill is... a person of ordinary creativity, not an automaton.").
The Examiner is therefore of the opinion that from the combined teachings of the references cited above, that one of ordinary skill in the art would have had a reasonable expectation of success in producing the claimed invention. Therefore, the invention as a whole would have been prima facie obvious to one of ordinary skill in the art especially in the absence of unexpected results.
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 1-5 and 7-18 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 and 21 of copending Application No. 17/924,944 (reference application).
Although the claims at issue are not identical, they are not patentably distinct from each other because both sets of claims are drawn to a recombinant host cell comprising an active pentose fermentation pathway and a heterologous NADP-dependent glyceraldehyde-3-phosphate dehydrogenase. It is noted arabinose is a pentose. Claims 1-2 and 6 of ‘944 correspond to instant claims 1 and 7-8. It is noted the GAPN of claim 2 of ‘944 represented by SEQ ID NO. 273 shares 100% sequence identity to the GAPN represented by SEQ ID NO. 273 (the elected species of the instant application) of instant claim 8. Claim 3 of ‘944 corresponds to instant claim 9. Claims 4-5 of ‘944 correspond to instant claims 4 and 10-11. Claim 8 of ‘944 corresponds to instant claims 1, 4 and 10-11. Claims 9-10 of ‘944 correspond to instant claims 12-13. Claims 11-13 correspond to instant claims 14-16. Claim 15 of ’944 corresponds to instant claim 18. Claim 21 of ‘944 corresponds to instant claim 17. This is an obvious type double patenting rejection.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-5 and 7-18 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6-8, 10-16 and 18 of copending Application No. 18/568,235 (reference application).
Although the claims at issue are not identical, they are not patentably distinct from each other for the same reasons as discussed above regarding Application ‘944. It is noted the GAPN of claim 4 of ‘235 represented by SEQ ID NO. 273 shares 100% sequence identity to instant SEQ ID NO. 273. This is an obvious type double patenting rejection.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Claims 1-5 and 7-18 are rejected.
No claims are allowed.
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/A.T.W./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653