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 .
Applicant’s election without traverse of group I and the species guide DNA, double, single-strand break, eukaryotic, and Clostridium perfringens in the reply filed on 1/26/24 is acknowledged.
Claims 152 and 156-161 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 without traverse in the reply filed on 1/26/24.
Claim Rejections - 35 USC § 112
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 144-151 and 153-155 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. THIS IS A NEW MATTER REJECTION.
The specification does not disclose the newly recited limitation “the additional functional polypeptide sequence reduces an energetic requirement for generating a break in a target nucleic acid as compared to a polypeptide construct lacking said additional functional polypeptide sequence”.
The specification discloses: [0005] Disclosed herein is a polypeptide construct comprising: a prokaryotic RNase H-like domain- containing (RHDC) polypeptide sequence and a nucleic acid unwinding polypeptide sequence. In sonic cases, the RHDC polypeptide sequence cleaves a nucleic acid in a target polynucleotide sequence at a mesophilic temperature. In some cases the target polynucleotide sequence is bound by a guide DNA. In some cases, the RHDC polypeptide sequence is fused to the nucleic acid unwinding polypeptide sequence. In some cases, at least one of the RHDC polypeptide sequence or said nucleic acid unwinding polypeptide sequence are derived from a mesophilic organism.
In some cases, the RHDC polypeptide sequence comprises a nuclease, nickase, RNase, recombinase, flippase, transposase, or a combination thereof. In some cases, the polypeptide construct further comprises an additional functional polypeptide sequence fused to the RHDC polypeptide sequence and the nucleic acid unwinding polypeptide sequence.
The only species of the instant nucleic acid system that meets the newly added limitations is: [0109] In some embodiments, the present disclosure provides an ex vivo system comprising an RNase H-like domain-containing (RHDC) polypeptide, a nucleic acid unwinding agent, and a guide nucleic acid, wherein the guide nucleic acid binds to a predetermined gene or to a nucleic acid sequence adjacent to the predetermined gene, the RHDC polypeptide is capable of introducing a double strand break in the predetermined gene, the nucleic acid unwinding agent lowers the energetic requirement for introducing the double strand break in comparison to introducing a double strand break with the RHDC polypeptide alone.
However, this is not commensurate in scope with the instant claims that are directed to any polypeptide construct comprising an Argonaute polypeptide sequence from a mesophilic organism and any additional functional polypeptide sequence reduces an energetic requirement for generating a break in a target nucleic acid as compared to a polypeptide construct lacking said additional functional polypeptide sequence; and a gRNA that binds to the target nucleic acid sequence. The claims do not recite the disclosed unwinding polypeptide sequence.
The remainder of the claims are rejected because they depend from claim 144.
MPEP §2163.06 notes:
If new matter is added to the claims, the examiner should reject the claims under 35 U.S.C. 112, first paragraph - written description requirement. In re Rasmussen, 650 F.2d 1212, 211 USPQ 323 (CCPA 1981).
MPEP §2163.02 teaches that:
Whenever the issue arises, the fundamental factual inquiry is whether a claim defines an invention that is clearly conveyed to those skilled in the art at the time the application was filed...If a claim is amended to include subject matter, limitations, or terminology not present in the application as filed, involving a departure from, addition to, or deletion from the disclosure of the application as filed, the examiner should conclude that the claimed subject matter is not described in that application.
A review of the specification does not reveal support for where the claim amendments are found. Should applicant disagree, applicants are encouraged to point out with particularity by page and line number where such support might exist for each claim limitation added in the amended claims filed on 8/20/25.
There is no support for this claim limitation in the claimed priority documents. Therefore, the effective filing date of the instant claims is considered, for purposes of prior art, to be 7/22/22, which is the filing date of the instant application.
Claims 144-151 and 153-155 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 claims are directed to any polypeptide construct comprising an Argonaute polypeptide sequence from a mesophilic organism and any additional functional polypeptide sequence reduces an energetic requirement for generating a break in a target nucleic acid as compared to a polypeptide construct lacking said additional functional polypeptide sequence; and a gRNA that binds to the target nucleic acid sequence.
For additional functional polypeptide sequences that reduce an energetic requirement for generating a break in a target nucleic acid, the specification discloses a single species, an unwinding polypeptide sequence fused to a RHDC.
The specification does not describe any other functional polypeptide sequences that reduce an energetic requirement for generating a break in a target nucleic acid. Therefore, the specification does not disclose species that are representative of the entire claimed genus.
The specification does not adequately describe the structure required for the function of the additional polypeptide; and therefore one would not be able to readily recognize which polypeptides are necessarily included or excluded from the recited genus. Even with regards to unwinding polypeptide sequences, the specification does not adequately describe which unwinding polypeptide sequences have the function as claimed.
The specification discloses: [0005] Disclosed herein is a polypeptide construct comprising: a prokaryotic RNase H-like domain- containing (RHDC) polypeptide sequence and a nucleic acid unwinding polypeptide sequence. In sonic cases, the RHDC polypeptide sequence cleaves a nucleic acid in a target polynucleotide sequence at a mesophilic temperature. In some cases the target polynucleotide sequence is bound by a guide DNA. In some cases, the RHDC polypeptide sequence is fused to the nucleic acid unwinding polypeptide sequence. In some cases, at least one of the RHDC polypeptide sequence or said nucleic acid unwinding polypeptide sequence are derived from a mesophilic organism.
In some cases, the RHDC polypeptide sequence comprises a nuclease, nickase, RNase, recombinase, flippase, transposase, or a combination thereof. In some cases, the polypeptide construct further comprises an additional functional polypeptide sequence fused to the RHDC polypeptide sequence and the nucleic acid unwinding polypeptide sequence.
The only species of the instant nucleic acid system that meets the newly added limitations is: [0109] In some embodiments, the present disclosure provides an ex vivo system comprising an RNase H-like domain-containing (RHDC) polypeptide, a nucleic acid unwinding agent, and a guide nucleic acid, wherein the guide nucleic acid binds to a predetermined gene or to a nucleic acid sequence adjacent to the predetermined gene, the RHDC polypeptide is capable of introducing a double strand break in the predetermined gene, the nucleic acid unwinding agent lowers the energetic requirement for introducing the double strand break in comparison to introducing a double strand break with the RHDC polypeptide alone.
The MPEP states that for a generic claim, the genus can be adequately described if the disclosure presents a sufficient number of representative species that encompass the genus. See MPEP § 2163. If the genus has a substantial variance, the disclosure must describe a sufficient variety of species to reflect the variation within that genus. See MPEP § 2163. Although the MPEP does not define what constitute a sufficient number of representative species, the courts have indicated what do not constitute a representative number of species to adequately describe a broad genus. In Gostelli, the courts determined that the disclosure of two chemical compounds within a subgenus did not describe that subgenus. In re Gostelli, 872, F.2d at 1012, 10 USPQ2d at 1618. Additionally, in Carnegie Mellon University v. Hoffman-La Roche Inc., Nos. 07-1266, -1267 (Fed. Cir. Sept. 8, 2008), the Federal Circuit affirmed that a claim to a genus described in functional terms was not supported by the specification’s disclosure of species that were not representative of the entire genus. Furthermore, for a broad generic claim, the specification must provide adequate written description to identify the genus of the claim. In Regents of the University of California v. Eli Lilly & Co. the court stated:
"A written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula, [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials." Fiers, 984 F.2d at 1171, 25 USPQ2d 1601; In re Smythe, 480 F.2d 1376, 1383, 178 USPQ 279, 284985 (CCPA 1973) ("In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus ...") Regents of the University of California v. Eli Lilly & Co., 43 USPQ2d 1398.
The claims are rejected under the written description requirement for failing to disclose adequate species to represent the claimed genus, the genus being functional polypeptide sequences that reduce an energetic requirement for generating a break in a target nucleic acid.
The Guidelines for Examination of Patent Applications under the 35 USC § 112, first paragraph, “Written Description” Requirement”, published at Federal Register, Vol. 66, No. 4, pp. 1099-1111 outline the method of analysis of claims to determine whether adequate written description is present. The first step is to determine what the claim as a whole covers, i.e., discussion of the full scope of the claim. Second, the application should be fully reviewed to understand how applicant provides support for the claimed invention including each element and/or step, i.e., compare the scope of the claim with the scope of the description. Third, determine whether the applicant was in possession of the claimed invention as a whole at the time of filing.
Thus, having analyzed the claims with regard to the Written Description guidelines, it is clear that the specification does not disclose a representative number of species for functional polypeptide sequences that reduce an energetic requirement for generating a break in a target nucleic acid. Thus, one skilled in the art would be led to conclude that Applicant was not in possession of the claimed invention at the time the application was filed.
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.
Claim(s) 144-151 and 153-155 is/are rejected under 35 U.S.C. 103 as being unpatentable over Valton et al. (WO 2016/166268 A1), in view of Welstead et al. (WO 2016/154596 A1).
The Valton et al. reference is of record and cited on the IDS filed on 1/25/24.
Valton et al. teach a nucleic acid editing system comprising an Argonaute polypeptide sequence from a mesophilic organism and a guide nucleic acid, that results in a single-stranded break (page 2) (instant claim 144).
Valton et al. teach: Here, the inventors surprisingly found that a set of Ago proteins isolated from diverse species other than Thermus thermophilus which are not thermophile could be heterologously expressed in mammalian cells. These Ago proteins have the particularity, and can be optimized, to be active in a wide temperature range, including a temperature at around 37°C and below, allowing their use in different function (such as gene editing), in animal cell as well as in plant cell. Based on this finding they have set up in particular a strategy of gene editing using DNA-guided Ago to engineer T-cells suitable for immunotherapy (pages 1-2) (instant claims 145 and 146).
Valton et al. teach a single or double stranded break; and teach that the construct can be a synthetic fusion polypeptide (instant clam 147). Valton et al. teach that the polypeptide-fusions can also be linked to other regulatory or functional domains, for example nucleases, transposases, or methylases, to modify endogenous chromosomal sequences. The target can be plant or mammalian (page 2) (instant clam 148).
Valton et al. teach that the Argonaute polypeptide sequence is from Clostridium, more specifically Clostridium butyricum or Clostridium sartagoforme (instant claims 149 and 150).
Valton et al. teach that the small interfering DNAs guide TtAgo cleave complementary DNA strands at high temperature (75°C) (instant claim 155).
Valton et al. teach: According to a preferred aspect of the invention, the Ago protein or the Ago protein variant from mesophilic prokaryote has at least 70%, more preferably at least 75%, and even more preferably at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% sequence identity with the Ago proteins from prokaryotic bacteria T Synechococcus sp. PCC 7002 (SEQ ID NO. 2), Synechococcus elongates (SEQ ID NO.3), Synechocystis sp, (SEQ ID NO.4 ), Aromatoleum aromaticum EbN1 (SEQ ID NO.5), Pseudomonas luteola (SEQ ID NO.6), Marinospirillum minutulum (SEQ ID NO.7 ), Haloferax denitricans (SEQ ID NO.8), Halorubrum kocurii (SEQ ID NO.9), Halobacterium satilanarum (SEQ ID NO.10), Natronobacterium gregoryi (SEQ ID NO.1 1 ), Clostridium butyricum (SEQ ID NO.12), Clostridium sartagoforme (SEQ ID NO.13), Halobacterium sp. DL1 (SEQ ID NO.14), Halorubrum lacusprofundi (SEQ ID NO.15 ), and Natrialba asiatica (SEQ ID NO.16 ) such as presented in Tables 1 and 2 (instant claim 151)ton et al. teach: As per the present invention, the inventors have established that DNA-guided Argonaute interference system (DAIS) from diverse mesophilic prokaryotic organisms provides an efficient and easy-to-implement tool for generating targeted modifications of genomic DNA. Among them, DAIS can be used for targeted mutagenesis, targeted chromosomal deletions, targeted gene inversion, translocation or insertion and for multiplexed genome modifications. Such technology can be used to engineer living cells for specific applications such as cellular immunotherapy, gene therapy, generation of genetically modified animals, as well as cells for bioproduction as non-limiting examples. This DAIS by using appropriate Ago proteins from mesophilic prokaryotes also allows targeted modifications of genomic DNA in plant cell.
Valton et al. teaches at Figure 1: Schematic representation of the method for inducing double strand cleavage in a nucleic acid target sequence according to the present invention through the heterologous expression of Ago from a mesophilic prokaryote in a cell in the presence of oligonucleotides that act as specific guides to the selected locus. The 2 cleavage events presented in this figure can be performed in a sequentially or concomitantly manner (instant claim 153).
Valton et al. teach: Optimized Ago proteins from a mesophilic prokaryote can be derived from such a protein, or from an Ago protein from other species, by directed evolution in order to optimize its performance at a range of temperature comprised between 30°C and 40°C.
Valton et al. teach: One method according to the invention for optimizing an Ago protein from a mesophilic prokaryote to have it induce more cleavage activity at a temperature below 40°C, can comprise the steps of:
a) Introducing oligonucleotides into a cell , said oligonucleotides being selected to hybridize a toxic gene, resistance gene or a reporter gene present into said cell;
b) Creating a variant of the gene encoding Ago protein from a mesophilic prokaryote and expressing said gene into said cell;
c) Cultivating said cell at a temperature below 40°C;
d) Recovering said variant encoding Ago protein from said cultured cells.
Such variant proteins obtainable form this method form a further object of the present invention.
Valton et al. recites:
1 . A method of modifying the genetic material of an animal or plant cell through expression of an Ago protein or an Ago protein variant from a mesophilic prokaryote into said cell in the presence of at least one exogenous oligonucleotide (DNA guide) providing specificity of cleavage to said Ago protein to a preselected locus (instant claim 154).
2. A method according to claim 1 , wherein said mesophilic prokaryotic organism is chosen among Synechococcus sp. PCC 7002, Synechococcus elongatus, Synechocystis sp,, Aromatoleum aromaticum EbN 1 , Pseudomonas luteola,, Marinospirillum minutulum, Haloferax denitricans Halorubrum kocurii, Halobacterium satilanarum, Natronobacterium gregoryi, Clostridium butyricum, Clostridium sartagoforme, Halobacterium sp. DL1 , Halorubrum lacusprofund, and Natrialba asiatica.
3. A method according to claim 1 or claim 2, wherein said mesophilic prokaryotic organism is chosen among Natronobacterium gregoryi, Synechococcus sp. PCC 700, Halobacterium satilanarum and Natrialba asiatica.
14. A method according to any one of claims 1 to 13, wherein said cell is a mammalian cell.
15. A method according to any one of claims 1 to 14, wherein said cell is a human cell.
16. A method according to any one of claims 1 to 15, wherein said cell is a T- cell.
18. A method according to any one of claims 1 to 17, wherein said oligonucleotide is 10 to 50 nucleotides in length, preferably 15 to 30 nucleotides, more preferably 20 to 25 nucleotides.
22. A method according to any one of claims 1 to 21 , wherein at least 2 oligonucleotides are selected to respectively hybridize each strand of a double-strand DNA at sites that are closed enough to each other to obtain double strand break (instant claim 155).
23. A method according to any one of claims 1 to 22, wherein the 2 oligonucleotides hybridize each strand at the same locus so that Ago will create a blunt double strand break.
24. A method according to any one of claims 1 to 22, further comprising the step of performing homologous recombination at the preselected locus by bringing a donor DNA comprising a sequence homologous to that of the preselected locus into contact with said genetic material.
25. A method according to claim 24, wherein said donor DNA comprises a transgene, a promoter, an expression cassette or a repairing sequence to be inserted at the preselected locus.
26. A method according to any one of claims 1 to 24, wherein said Ago protein is heterologously expressed from a polynucleotide introduced into said cell.
27. A method according to any one of claims 1 to 26, wherein said Ago or Ago variant protein has at least 70%, more preferably at least 75%, and even more preferably at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% sequence identity with SEQ ID NO.2 to SEQ ID NO.16 .
28. A method according to any one of claims 1 to 27, wherein said Ago or Ago variant protein is optimized to be more active at a temperature below 40 °C.
29. A method according to any one of claims 1 to 27, wherein said Ago or Ago variant protein is optimized to be more active at a temperature between 30 and 40 °C, preferably 37°C.
35. A method according to any one of claims 1 to 27 or claims 30 to 34, wherein said Ago or Ago variant protein is optimized to be more active at a temperature below 30 °C, and preferably between 20 and 25°C, and wherein said genetic material is a plant cell.
39. A polynucleotide vector comprising a gene encoding Ago or Ago variant protein from a mesophilic prokaryote.
42. A method for optimizing Ago protein to induce more cleavage activity at a temperature below 40°C, wherein said method comprises the following steps:
(a) Introducing oligonucleotides into a cell, said oligonucleotides being selected to hybridize a toxic gene, resistance gene or a reporter gene present into said cell; (b) Creating a variant of the gene encoding Ago protein and expressing said gene into said cell;
(c) Cultivating said cell at a temperature below 40°C;
(d) Recovering said variant encoding Ago protein from said cultured cells that do not express said toxic gene, resistance gene or reporter gene.
43. Method according to claim 42, wherein said Ago or Ago variant protein or an Ago variant has at least 70%, more preferably at least 75%, and even more preferably at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% sequence identity with SEQ ID NO.2 to SEQ ID NO.16
44. Method according to claim 42 or claim 43, wherein said temperature is between 30 and 40°C.
45. Method according to anyone of claim 42 to claim 44, wherein said cell is a mammalian cell.
46. Method according to anyone of claim 42 to claim 45, wherein said Ago or Ago variant protein from a mesophilic prokaryote is assayed for more stable expression in said cell at said temperature.
47. Optimized variant gene encoding Ago from a mesophilic prokaryote susceptible to be obtained by the method of any one of claims 42 to 46.
48. Ago or Ago variant protein from a mesophilic prokaryote encoded by the variant gene according to claim 47.
Valton et al. teaches a method to optimize the Ago protein to induce more cleavage activity at a temperature below 40°C.
Valton et al. teaches at Figure 1: Schematic representation of the method for inducing double strand cleavage in a nucleic acid target sequence according to the present invention through the heterologous expression of Ago from a mesophilic prokaryote in a cell in the presence of oligonucleotides that act as specific guides to the selected locus. The 2 cleavage events presented in this figure can be performed in a sequentially or concomitantly manner (instant claim 155).
Valton et al. teach: Optimized Ago proteins from a mesophilic prokaryote can be derived from such a protein, or from an Ago protein from other species, by directed evolution in order to optimize its performance at a range of temperature comprised between 30°C and 40°C.
Valton et al. clearly teach a nucleic acid editing system wherein the system comprises an Argonaute polypeptide from a mesophilic organism and a guide nucleic acid and induces the break at a mesophilic temperature. Valton teaches how to prepare and use the Argonaute polypeptide.
The reference teaches specific Ago sequences from mesophilic organisms and teaches methods for obtaining and using the system. The reference teaches temperature ranges of Ago activity for a set of mesophilic prokaryotes (Table 1, page 6) and polypeptide sequences (Table 2, starting at page 7).
Valton et al. does not teach incorporation of an additional polypeptide sequence that reduces an energetic requirement for generating a break in a target nucleic acid as compared to a polypeptide construct lacking said additional functional polypeptide sequence.
However, it was known to incorporate a Cas9 polypeptide into a CRISPR system because it is capable of cleaving a target nucleic acid molecule, as taught by Welstead et al. (page 88). Welstead et al. teach that Cas9 has helicase activity and therefore has the ability to unwind the helical structure of a double stranded nucleic acid (page 89).
Therefore, it would have been obvious to incorporate Cas9 with the expectation of helicase activity and therefore reduction in the energetic requirement for generating a break.
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 144-151 and 153-155 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 of U.S. Patent No. 11,447,774 B2. Although the claims at issue are not identical, they are not patentably distinct from each other because both of the claim sets recite a nucleic acid editing system comprising an Argonaute polypeptide from a mesophilic organism and a guide nucleic acid. Claim 1 of US ‘774 recites an additional agent, a nucleic acid unwinding agent, which meets the instant limitation of an additional functional polypeptide sequence that reduces the energetic requirement for generating a break. The activity of the system is recited at the same temperatures. Both claim sets recite that the Argonaute polypeptide is from a Clostridium and recite the same species of organisms (instant claim 150 and claim 9 of US ‘774 B2); and recite achieving the same outcomes of single or double stranded breaks (instant claim 144 and claim 12 of US ‘774). The applications have identical specifications and the claims are obvious variations of each other.
Applicant requires that the rejection be held in abeyance.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Amy R Hudson whose telephone number is (571)272-0755. The examiner can normally be reached M-F 8:00am-6:00pm.
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/AMY ROSE HUDSON/Primary Examiner, Art Unit 1636