DETAILED ACTION
Status of Application
The amendments and response filed 27 June 2025 are acknowledged and have been considered in their entireties. Claims 1-3, 5-9, 15-16, 18-19, 21, 23-26, 29, 32, 36, 42, 46, 49, 51-53, 60, 62, 65-66, 68-71, 73, 82-84 and 88 are pending. Claims 18-19, 21, 23-26, 29, 32, 36, 42, 46, 49, 51-53, 60, 62, 65-66, 68-71 and 82 remain withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected subject matter, there being no allowable generic or linking claim. Claims 1-3, 5-9, 15-16, 24-26, 73, 83-84 and 88 are subject to examination on the merits.
Withdrawal of Previous Objections/Rejections
The objection to claim 1 is withdrawn in view of the amendment to correct grammar in the last line.
The objection to claim 8 is withdrawn in view of the amendment to correct grammar in the second line.
The rejection of claim 16 under 35 U.S.C. 112(b), lack of antecedent basis is withdrawn in view of the amendment to make said claim dependent on claim 9.
Maintained Rejection(s)
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.
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Claims 1-3, 5-9, 15-16, 24-26, 73, 83-84 and 88 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 11840711 in view of Yu et al. (Biotechnology Advances, 2015 – cited previously).
The instant claim in their broadest are drawn to an engineered composition for site directed base editing comprising a Type VI CRISPR system Cas13 protein, or fragment thereof retaining RNA binding activity, a guide molecule and a cytidine deaminase that is fused directly or via a linker to the C-terminus of the Cas13 protein or fragment thereof. Dependent claim 6 recites the Cas13 is from various species including Prevotella sp. P5-125; dependent claim 7 recites the species are selected from Prevotella sp. P5-125 with specific substitutions at R128, H133, R1053, H1058; or at H133 and H1058; or Bergeyella zoohelcum ATCC 43767 and has substitutions at R116, H121, R1177 and H1182; or Listeria wadei and has substitutions at R474 and R1046. Dependent claim 15 recites the Cas13 and/or cytidine deaminase comprises NES or NLS. Claim 83 recites the same as claim 1 but with specific Cas13 proteins selected from various species and strains including Porphyromonas gingivalis.
The claims to the ‘711 patent in their broadest are drawn to A non-naturally occurring or engineered composition comprising; i) a Type VI-B Cas protein optimized for activity in a mammalian cell, and ii) one or more nucleic acid components, the one or more nucleic acid components capable of forming a complex with the Type VI-B Cas protein and comprising a guide sequence capable of directing site specific binding of the complex to a target RNA polynucleotide sequence wherein the Type VI-B Cas protein is selected from the group consisting of Porphyromonas gulae Cas13b as set forth in SEQ ID NO: 159, Prevotella sp. P5-125 Cas13b as set forth in SEQ ID NO: 160, Porphyromonas gingivalis Cas13b as set forth in SEQ ID NO: 164, Porphyromonas sp. COT-052 OH4946 Cas13b as set forth in SEQ ID NO: 165, Bacteroides pyogenes Cas13b as set forth in SEQ ID NO: 150, and Riemerella anatipestifer Cas13b as set forth in SEQ ID NO: 153. Dependent claim 3 recites the that Cas13 protein comprises an NES or NLS. Dependent claim 10 recites wherein the Type VI-B Cas protein contains one or more mutations within a HEPN domain corresponding to amino acid positions R116, H121, R1177, or H1182 of Type VI-B Bergeyella zoohelcum ATCC 43767 as set forth in SEQ ID NO: 146. And dependent claim 7 recites that the Cas13 is associated with a cytidine or adenosine deaminase. It is noted, in construing the scope of the claims (See MPEP 804(II)(B)(1)) of the ‘711 patent, it is understood that “associated with” is to include fusion or proteins of the Cas13 and cytidine deaminase – See Col. 162, line 57, to Col. 163, line 10. In addition, the attachment of the deaminase is clearly construed to mean either the N- or C-terminus (See Col. 166, lines 13-20).
The claims of the ‘711 patent, however, do not disclose that the cytidine deaminase is fused directly or with a linker to the C-terminus of the Cas13 protein.
Yu et al. teach at p. 156, 1st col., regarding the Design and Construction of Synthetic Fusion Proteins: “The order of fusion partners in the polypeptide chain is often critical, as the placement of one domain can affect the localization and functionality of the other (Sachdev and Chirgwin, 1998). Hence, in the case of a two component fusion, two sequence combinations should be attempted unless the possible effect of the order is known.” In the same section, Yu et al. also teach of optimization of linkers (e.g. whether to have them or not and if so, finding the optimal linker).
Therefore it would have been obvious to one of ordinary skill in the art to further modify the claims of the ‘711 patent to include to ascertain the optimal order of the fusion protein and determine the best possible order combinations of the cytidine deaminase and Cas13 protein fusions (e.g. N-cytidine deaminase-Cas13-C; AND N-Cas13-cytidine deaminase-C) because it taught this is critical in the design and function for all fusion proteins; which would also provide the motivation and expectation of success (while also optimizing linkers as also detailed in the same cited section of Yu et al). This would be motivation in and of itself for one of ordinary skill in the art wishing to obtain the most optimal Cas13-cytidine deaminase fusion protein. In addition, there would be a reasonable expectation of success in making a C-terminally fused Cas13-cytidine deaminase fusion protein given teachings for optimization in Yu et al.
Applicant’s Arguments and Examiner’s Response
Applicant’s traverse the rejection and state there is not a reasonable expectation of success (e.g. Yu et al. teaches making fusion proteins is daunting challenge, etc.) and the secondary reference of Yu et al. away teach from fusion proteins and there are not a finite number of solutions to the problem (See Remarks, p. 15-16).
The Examiner has considered these arguments but does not find them convincing. In the first instance, the claims to the ‘711 patent are broad enough to encompass fusion proteins on either side or anywhere. Said claims, however, do not specifically recite which side the fusion takes place. The claims are further broad enough to recite functional fusion proteins. Applicant’s arguments, however, almost seem to suggest that the claims of the ‘711 patent are not enabled for the breadth of the claimed fusion proteins because: there is no predictability of success, the state of the art suggests it is difficult, there would be a necessity of trial and error work mandated by a skilled artisan which is undue, etc. However, given the claims are patented, they are presumed valid and thus enabled. Thus, for this instance, as noted in the rejection itself, upon construing the scope of the patented claims (See MPEP 804(II)(B)(1)) of the ‘711 patent, it is understood that “associated with” is to include fusion or proteins of the Cas13 and cytidine deaminase – See Col. 162, line 57, to Col. 163, line 10. In addition, the attachment of the deaminase is clearly construed to mean either the N- or C-terminus (See Col. 166, lines 13-20). Thus, the patented claims themselves, suggest attaching the deaminase to the Cas13 protein either to the N-terminus of C-terminus but do not suggest a linker. While Yu et al. do indicate there are some challenges to making any fusion protein, they also provide sufficient and detailed analysis for achieving success, trying either terminus and finding optimal linkers (See Yu et al. at p. 156, 1st col.). Given the extensive list of successful enzyme fusion proteins as described in Yu et al. (See Custom tailored fusion proteins for multiple applications) alogn with the strategy for rational design of any fusion protein, then there would be a reasonable expectation of success and the rejection is maintained.
Claims 1-3, 5-9, 15-16, 24-26, 73, 83-84 and 88 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 11618896 in view of Yu et al. (Biotechnology Advances, 2015 – cited previously).
The instant claim in their broadest are drawn to an engineered composition for site directed base editing comprising a Type VI CRISPR system Cas13 protein, or fragment thereof retaining RNA binding activity, a guide molecule and a cytidine deaminase that is fused directly or via a linker to the C-terminus of the Cas13 protein or fragment thereof. Dependent claim 6 recites the Cas13 is from various species including Prevotella sp. P5-125; dependent claim 7 recites the species are selected from Prevotella sp. P5-125 with specific substitutions at R128, H133, R1053, H1058; or at H133 and H1058; or Bergeyella zoohelcum ATCC 43767 and has substitutions at R116, H121, R1177 and H1182; or Listeria wadei and has substitutions at R474 and R1046. Dependent claim 15 recites the Cas13 and/or cytidine deaminase comprises NES or NLS. Claim 83 recites the same as claim 1 but with specific Cas13 proteins selected from various species and strains including Porphyromonas gingivalis.
The claims to the ‘896 patent in their broadest are drawn to an engineered, non-naturally occurring system comprising a catalytically inactive Cas13 effector protein (dCas13) or a nucleotide sequence encoding the catalytically inactive Cas13 effector protein, wherein the dCas13 is Prevotella sp. P5-125 Cas13b protein or Porphyromonas gulae Cas13b protein. Dependent claim 20 recites the that system comprises a guide sequence. Dependent claims 8-12 recite the dCas13 protein is fused to a cytidine deaminase.
The claims of the ‘896 patent, however, do not disclose that the cytidine deaminase is fused directly or with a linker to the C-terminus of the Cas13 protein.
Yu et al. teach at p. 156, 1st col., regarding the Design and Construction of Synthetic Fusion Proteins: “The order of fusion partners in the polypeptide chain is often critical, as the placement of one domain can affect the localization and functionality of the other (Sachdev and Chirgwin, 1998). Hence, in the case of a two component fusion, two sequence combinations should be attempted unless the possible effect of the order is known.” In the same section, Yu et al. also teach of optimization of linkers (e.g. whether to have them or not and if so, finding the optimal linker).
Therefore it would have been obvious to one of ordinary skill in the art to further modify the claims of the ‘896 patent to include to ascertain the optimal order of the fusion protein and determine the best possible order combinations of the cytidine deaminase and Cas13 protein fusions (e.g. N-cytidine deaminase-Cas13-C; AND N-Cas13-cytidine deaminase-C) because it taught this is critical in the design and function for all fusion proteins; which would also provide the motivation and expectation of success (while also optimizing linkers as also detailed in the same cited section of Yu et al). This would be motivation in and of itself for one of ordinary skill in the art wishing to obtain the most optimal Cas13-cytidine deaminase fusion protein. In addition, there would be a reasonable expectation of success in making a C-terminally fused Cas13-cytidine deaminase fusion protein given teachings for optimization in Yu et al.
Applicant’s Arguments and Examiner’s Response
Applicant’s traverse the rejection of record for the following reasons:
It is asserted the Examiner has ignored or misinterpreted the scope of the patent claims and does not take into consideration that the claims of the ‘896 patent require truncated Cas13 effector proteins.
The Examiner has considered this argument but does not find it convincing because the instant claims are so broad as to encompass any Cas13 protein. Thus, the instant claims are drawn to a genus of Cas13 proteins, the claims of the ‘896 patent are drawn to specific species of a Cas13 protein. The species will necessarily anticipate the genus.
With regard to Applicant’s assertion that a two way distinctness test is required, this is not found convincing. MPEP 804(II)(B)(4) states: Similarly, even if the application under examination has the earlier patent term filing date, only a one-way determination of distinctness is needed to support a double patenting rejection in the absence of a finding: (A) that "the PTO is solely responsible for any delays" in prosecution of that application (In re Hubbell, 709 F.3d 1140, 1150, 106 USPQ2d 1032, 1039 (Fed. Cir. 2013)); and (B) that the applicant could not have filed the conflicting claims in a single (i.e., the earlier-filed) application ( In re Kaplan, 789 F.2d 1574, 229 USPQ 678 (Fed. Cir. 1986)).
Here, Applicant’s have not established: (A) that it was solely the PTO’s responsibility in a delay of examination/prosecution of the patented claims/application and also (B) they could not possibly have filed the conflicting claims in a single application. Thus, the assertion that a two way distinctness test is required is false.
Regarding the one way distinctness test, Applicant’s are correct that the instant claims are so broad as to be drawn to a genus of Cas13 proteins whereas the ‘896 patent are drawn to particular species. As noted in part (A) arguments above, the species necessarily anticipate the genus. See MPEP 804(II)(B)(2) and (3).
Applicant’s traverse the rejection and state there is not a reasonable expectation of success (e.g. Yu et al. teaches making fusion proteins is daunting challenge, etc.) and the secondary reference of Yu et al. away teach from fusion proteins such as the claimed one because of the HEPN at the C-terminus (See Remarks, p. 17).
The Examiner has considered these arguments but does not find them convincing. In the first instance, the claims to the ‘896 patent are broad enough to encompass fusion proteins on either side or anywhere. Said claims, however, do not specifically recite which side the fusion takes place. Applicant’s arguments, however, almost seem to suggest that the claims of the ‘896 patent are not enabled for the breadth of the claimed fusion proteins because: there is no predictability of success, the state of the art suggests it is difficult, there would be a necessity of trial and error work mandated by a skilled artisan which is undue, etc. However, given the claims are patented, they are presumed valid and thus enabled. Claims 9 and 10 of the ‘896 specifically recite that the deaminase is fused to the dCas13 and is fused by a linker. In addition, whether or not the HEPN domain is at the N- or C-terminus (or both) really ultimately does not matter because the Cas13 protein of the ‘896 is already dead/inactive. Thus, it only needs to retain RNA binding not any catalytic function, which makes the expectation of success of adding a fusion partner to either N- or C-terminus all the more significant with regard to expectation of success. While Yu et al. do indicate there are some challenges to making any fusion protein, they also provide sufficient and detailed analysis for achieving success, trying either terminus and finding optimal linkers (See Yu et al. at p. 156, 1st col.). Given the extensive list of successful enzyme fusion proteins as described in Yu et al. (See Custom tailored fusion proteins for multiple applications) along with the strategy for rational design of any fusion protein, then there would be a reasonable expectation of success and the rejection is maintained.
Claims 1-2, 16, 24-26, 73 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 4 of U.S. Patent No. 11739156 in view of Yu et al. (Biotechnology Advances, 2015 – cited previously).
The instant claim in their broadest are drawn to an engineered composition for site directed base editing comprising a Type VI CRISPR system Cas13 protein, or fragment thereof retaining RNA binding activity, a guide molecule and a cytidine deaminase that is fused directly or via a linker to the C-terminus of the Cas13 protein or fragment thereof. Dependent claims 16, 24-26, 73 recite that the engineered composition is found within a population of cells such as T-cells.
The claims to the ‘156 patent in their broadest are drawn to a population of T-cells that have been modified and therefore comprise a CRISPR system comprising dCas13 fused to or otherwise linked to a cytidine deaminase (See claim 1 and 4). It is noted, in construing the scope of the claims (See MPEP 804(II)(B)(1)) of the ‘156 patent, it is ascertained that T-cells must necessarily include guide nucleotide sequences in order to target the dCas13 and cytidine deaminase fusion – See Genetic Modifying Agents section.
The claims of the ‘156 patent, however, do not disclose that the cytidine deaminase is fused directly or with a linker to the C-terminus of the Cas13 protein.
Yu et al. teach at p. 156, 1st col., regarding the Design and Construction of Synthetic Fusion Proteins: “The order of fusion partners in the polypeptide chain is often critical, as the placement of one domain can affect the localization and functionality of the other (Sachdev and Chirgwin, 1998). Hence, in the case of a two component fusion, two sequence combinations should be attempted unless the possible effect of the order is known.” In the same section, Yu et al. also teach of optimization of linkers (e.g. whether to have them or not and if so, finding the optimal linker).
Therefore it would have been obvious to one of ordinary skill in the art to further modify the claims of the ‘156 patent to include to ascertain the optimal order of the fusion protein and determine the best possible order combinations of the cytidine deaminase and Cas13 protein fusions (e.g. N-cytidine deaminase-Cas13-C; AND N-Cas13-cytidine deaminase-C) because it taught this is critical in the design and function for all fusion proteins; which would also provide the motivation and expectation of success (while also optimizing linkers as also detailed in the same cited section of Yu et al). This would be motivation in and of itself for one of ordinary skill in the art wishing to obtain the most optimal Cas13-cytidine deaminase fusion protein. In addition, there would be a reasonable expectation of success in making a C-terminally fused Cas13-cytidine deaminase fusion protein given teachings for optimization in Yu et al.
Applicant’s Arguments and Examiner’s Response
Applicant’s traverse the rejection of record for the following reasons:
With regard to Applicant’s assertion that a two way distinctness test is required, this is not found convincing. MPEP 804(II)(B)(4) states: Similarly, even if the application under examination has the earlier patent term filing date, only a one-way determination of distinctness is needed to support a double patenting rejection in the absence of a finding: (A) that "the PTO is solely responsible for any delays" in prosecution of that application (In re Hubbell, 709 F.3d 1140, 1150, 106 USPQ2d 1032, 1039 (Fed. Cir. 2013)); and (B) that the applicant could not have filed the conflicting claims in a single (i.e., the earlier-filed) application ( In re Kaplan, 789 F.2d 1574, 229 USPQ 678 (Fed. Cir. 1986)).
Here, Applicant’s have not established: (A) that it was solely the PTO’s responsibility in a delay of examination/prosecution of the patented claims/application and also (B) they could not possibly have filed the conflicting claims in a single application. Thus, the assertion that a two way distinctness test is required is false.
Regarding the one way distinctness test, Applicant’s are correct that the instant claims are so broad as to be drawn to a genus of Cas13 proteins whereas the ‘156 patent are drawn to particular species. As noted above, the species necessarily anticipates the genus. See MPEP 804(II)(B)(2) and (3).
Applicant’s traverse the rejection and state there is not a reasonable expectation of success (e.g. Yu et al. teaches making fusion proteins is daunting challenge, etc.) and the secondary reference of Yu et al. away teach from fusion proteins such as the claimed one because of the HEPN at the C-terminus (See Remarks, pp. 19-20).
The Examiner has considered these arguments but does not find them convincing. In the first instance, the claims to the ‘156 patent are broad enough to encompass fusion proteins on either side or anywhere. Said claims, however, do not specifically recite which side the fusion takes place. Applicant’s arguments, however, almost seem to suggest that the claims of the ‘156 patent are not enabled for the breadth of the claimed fusion proteins because: there is no predictability of success, the state of the art suggests it is difficult, there would be a necessity of trial and error work mandated by a skilled artisan which is undue, etc. However, given the claims are patented, they are presumed valid and thus enabled. Claims 4 of the ‘156 patent specifically recite that the deaminase is fused to the either Cas13 enzyme, a nCas13 or dCas13 and is fused to said deaminase. In addition, whether or not the HEPN domain is at the N- or C-terminus (or both) really ultimately does not matter because the Cas13 protein of the ‘156 is not required to be active. Thus, it only needs to retain RNA binding not any catalytic function, which makes the expectation of success of adding a fusion partner to either N- or C-terminus all the more significant with regard to expectation of success. While Yu et al. do indicate there are some challenges to making any fusion protein, they also provide sufficient and detailed analysis for achieving success, trying either terminus and finding optimal linkers (See Yu et al. at p. 156, 1st col.). Given the extensive list of successful enzyme fusion proteins as described in Yu et al. (See Custom tailored fusion proteins for multiple applications) along with the strategy for rational design of any fusion protein, then there would be a reasonable expectation of success and the rejection is maintained.
Claims 1-3, 5-9, 15-16, 24-26, 73, 83-84 and 88 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-34 of U.S. Patent No. 12221636 (previously applied rejection over co-pending US Application No. 16650480) because the combination of claims of the ‘636 patent application would anticipate the instant claims.
The instant claim in their broadest are drawn to an engineered composition for site directed base editing comprising a Type VI CRISPR system Cas13 protein, or fragment thereof retaining RNA binding activity, a guide molecule and a cytidine deaminase that is fused directly or via a linker to the C-terminus of the Cas13 protein or fragment thereof. Dependent claims 16, 24-26, 73 recite that the engineered composition is found within a population of cells such as T-cells.
The claims to the ‘636 patent are drawn to an engineered composition for site directed base editing comprising a Cas13 protein covalently or non-covalently linked to an adenosine deaminase which is modified into a cytidine deaminase and a gRNA (See claims 1, 6-7); and methods of modifying a cytosine in RNA by utilizing the engineered composition (claims 12-15) wherein the fused deaminase can be located either on the N-terminal or C-terminal side of the dCas13 protein (Dependent claim 13).
Thus, when for example, claims 1, 6-7, 12-13 are combined (along with the other overlapping dependent claims), they would necessarily anticipate the instant claims.
Applicant’s Remarks and Examiner’s Rebuttal:
Applicant’s traverse the rejections of record and assert on p. 21, and state the two sets of claims do not overlap because the instant claims are drawn to Cas13 fusions with a cytidine deaminase and the claims of the ‘636 patent are drawn to an a Cas13 protein covalently or non-covalently linked to an adenosine deaminase protein. Thus, because cytidine deaminases and adenosine deaminases are distinct enzymes with different structure, function and substrates the claims of the ‘636 patent cannot anticipate or render obvious the instant claims.
The Examiner has considered these arguments but does not find them convincing because the adenosine deaminase of the ‘636 patent have been functionally and structurally changed and manipulated to have cytidine deaminase activity. This then specifically meets the definition of a “cytidine deaminase” as defined in the instant application:
“[0124] The term “cytidine deaminase” or “cytidine deaminase protein” as used herein refers to a protein, a polypeptide, or one or more functional domain(s) of a protein or a polypeptide that is capable of catalyzing a hydrolytic deamination reaction that converts an cytosine (or an cytosine moiety of a molecule) to an uracil (or a uracil moiety of a molecule), as shown below.”
Given the instant specifications own definition of cytidine deaminase is determined based solely on the function of the protein, then the adenosine deaminase that has been modified to have cytidine deaminase activity and function, meets this definition and the rejection is maintained.
Conclusion
No claim is allowed.
THIS ACTION IS MADE FINAL. 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.
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/SUZANNE M NOAKES/Primary Examiner, Art Unit 1656 12 February 2026