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 .
Detailed Action
This action is in response to the papers filed January 14, 2026.
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 01/14/2026 has been entered.
Claim Amendments
Applicant’s amendment to the claims filed on 12/30/2025 is acknowledged.
Claims 57-58, 60-64, 69-72, and 76 are pending and under examination.
Election/Restrictions
The following is a summary of the restriction/election requirements in the application. See the Requirement for Restriction/Election mailed 01/02/2025.
Applicant elected without traverse Group 1, drawn to a chimeric receptor comprising an extracellular domain of G-CSFR, and a nucleic acid encoding thereof, an expression vector comprising thereof, a cell comprising thereof, and a kit comprising thereof, in the reply filed 04/01/2025.
Applicant further elected without traverse a chimeric receptor comprising a G-CSFR extracellular domain according to SEQ ID NO: 5 (amino acid sequence) and SEQ ID NO: 6 (nucleic acid sequence), a G-CSFR transmembrane domain according to SEQ ID NO: 8 (amino acid sequence) and SEQ ID NO: 12 (nucleic acid sequence), a G-CSFR intracellular domain according to SEQ ID NO: 20 (amino acid sequence), and an IL-2Rβ intracellular domain according to SEQ ID NO: 21 (amino acid sequence). The elected construct corresponds to the “G2R-3” construct as described in the specification and depicted in Figure 4:
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Priority
The instant application 17/767,687 was filed on 04/08/2022. This application is a national stage of international application PCT/CA2020/051346 filed 10/08/2020, claiming priority based on U.S. Provisional Application 62/912,223 filed 10/08/2019.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 01/14/2026 has been considered.
Withdrawal of Prior Rejections/Objections
Rejections and/or objections not reiterated from the previous Office action mailed 10/31/2025 are hereby withdrawn. The following rejections and/or objections are either newly applied or are reiterated and are the only rejections and/or objections presently applied to the instant application.
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.
Claims 57-58, 60-63, 69-72, and 76 are rejected under 35 U.S.C. 103 as being unpatentable WO 94/22914 to Greenberg et al., in view of US 2019/0292533 A1 to Nager et al.; and US 2018/0044399 A1 to Rajpal et al.
This rejection is newly applied, necessitated by amendment. A response to applicant’s traversal follows this rejection.
As discussed above in this action, applicant’s elected chimeric receptor corresponds to the “G2R-3” construct as described in the specification and depicted in Figure 4:
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Prior to the effective filing date of the instantly claimed invention, Greenberg describes chimeric cytokine receptors which enable lymphocytes to proliferate in response to an alternative cytokine, preferably a cytokine that is expressed in the lymphocyte at elevated levels in response to cognate antigen stimulation, or a cytokine that could be administered with reduced toxicity relative to, e.g., IL-2. The chimeric cytokine receptor comprises an extracellular domain of one receptor A-R fused, via a transmembrane domain, to an intracellular (cytoplasmic) domain of a second receptor B-R, thereby lessening the growth dependency of the lymphocyte on cytokine B in the presence of cytokine A. See, e.g., Abstract; pg. 5, ll. 11-18; pg. 6, ll. 20-28; and Figure 1:
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In particular, Greenberg teaches the extracellular domain is derived from G-CSFR, and the intracellular (cytoplasmic) domain is derived from IL-2Rβ. See, e.g., pg. 12, ll. 2-15. Furthermore, Greenberg discloses that suitable transmembrane domains exhibit characteristics such as hydrophobicity that promote their stable incorporation into the cellular membrane. Logically, a convenient source of such a transmembrane domain would be the transmembrane domains of receptors A-R or B-R. Preferably, therefore, the transmembrane domain is derived from cytokine receptor A-R or, more preferably, from receptor B-R. See, e.g., pg. 7, ll. 5-12; pg. 11, ll. 15-18. Accordingly, Greenberg fairly suggests that the transmembrane domain is derived from G-CSFR or IL-2Rβ.
Greenberg further discloses a nucleic acid encoding the chimeric receptor, and host cells comprising the nucleic acid. See, e.g., pg. 12, ll. 16-33.
For these reasons, Greenberg is found to teach or fairly suggest a chimeric receptor comprising the extracellular domain of G-CSFR, the intracellular domain of IL-2Rβ, and the transmembrane domain of G-CSFR or IL-2Rβ. Such a chimeric cytokine receptor comprising the intracellular domain of IL-2Rβ, as found in Greenberg, comprises the intracellular signaling domains of IL-2Rβ, including the Jak-binding regions (Box 1 and Box 2 motifs), adaptor protein SHC region, and STAT5 region.
The claimed invention recites that the chimeric receptor comprises a Box 1 region and a Box2 region of G-CSFR. Accordingly, the difference between the claimed invention and that of Greenburg is that the Jak-binding regions (Box 1 and Box 2 motifs) are derived from the receptor of the intracellular domain, IL-2Rβ, in Greenburg’s invention; whereas, the Jak-binding regions (Box 1 and Box 2 motifs) are derived from the receptor of the extracellular domain, G-CSFR, in the claimed invention.
However, prior to the effective filing date of the instantly claimed invention, Nager is considered relevant prior art for teaching chimeric cytokine receptors for improving the functional activities of immune cells, such as T cells. The chimeric cytokine receptor comprises a dimerization domain, a tyrosine activating domain, and a tyrosine effector domain; wherein the dimerization domain is an extracellular domain of a cytokine receptor; wherein the tyrosine activating domain is a transmembrane domain and a Jak-binding domain (Box 1 and Box 2 motifs) derived from a protein; wherein the tyrosine effector domain is a STAT-activation domain of a receptor. See, e.g., Abstract; par. 7-8, 10, 19, 220, 236.
Furthermore, Nager discloses that the dimerization domain may comprise the extracellular domain of G-CSFR (see, e.g., par. 20, 34, 223), the tyrosine activating domain may comprise a transmembrane domain and a Jak-binding domain of G-CSFR (see, e.g., par. 22, 25, 34, 238-239, 248), and the tyrosine effector domain may comprise a cytoplasmic tail (cytotail) of IL-2Rβ containing the STAT-activation domains thereof (see, e.g., par. 31, 252-255, 258).
Nager further describes the innovation as an improvement over the “traditional approach” to engineering cytokine receptors. While the traditional approach (Figure 10C) fuses only the extracellular domain (ectodomain) of receptor A to the transmembrane domain, Jak-binding domain and “cytotail” domain (i.e., the region after the JAK-binding domain) of receptor B, Nager’s improved approach (Figure 10D) fuses the extracellular domain (ectodomain), transmembrane domain and Jak-binding domain of receptor A to the cytotail domain of receptor B. In a working example, chimeric cytokine receptors based on the new approach showed a greater magnitude of downstream signaling relative to the traditional approach. See, e.g., Example 5C, par. 430-435; and Figures 10C-10F.
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Accordingly, Greenburg’s design of a G-CSFR/IL-2Rβ chimera follows the “traditional approach” (Figure 10C, above) described by Nager, and the claimed invention may therefore be viewed as applying Nager’s improved approach (Figure 10D, above) to designing a G-CSFR/IL-2Rβ chimera. Therefore, prior to the effective filing date of the instantly claimed invention, it would have been prima facie obvious to one of ordinary skill in the art to modify the G-CSFR/IL-2Rβ chimera of Greenburg (a design following the “traditional approach”), by retaining the transmembrane domain and Jak-binding domains (Box 1 and Box 2 motifs) of the receptor of the extracellular domain, G-CSFR, in view of the teachings of Nager (improved approach), with a reasonable expectation of success because, Nager found that chimeric cytokine receptors based on the improved approach showed a greater magnitude of downstream signaling relative to the traditional approach (par. 435, Figure 10F). Moreover, as outlined above, Nager broadly teaches that G-CSFR provides suitable extracellular, transmembrane, and Jak-binding domains for a chimeric receptor, and IL-2Rβ provides a suitable cytotail (i.e., the region after the JAK-binding domain) for a chimeric receptor.
Claim 57 further recites “wherein the chimeric receptor homodimerizes upon contact with G-CSF.” As instructed by MPEP 2111.04, claim scope is not limited by claim language that does not limit a claim to a particular structure. In this case, the recitation is directed to a functional property of the claimed chimeric receptor but does not clearly or necessarily further limit the structure thereof. Accordingly, since the prior art structure is capable of performing the recited function, the prior art meets the claim. Moreover, Greenburg expressly recognizes that G-CSFR undergoes homodimerization (pg. 11, ll. 27-29), and Nager expressly teaches that the chimeric receptors undergo dimerization (par. 20, 220, 223, 486), as claimed. For these reasons, the limitation “wherein the chimeric receptor homodimerizes upon contact with G-CSF” is not found to necessarily result in a structural difference which patentably distinguishes the claimed chimeric receptor from that of the prior art.
Sequence identifiers (SEQ ID NOs):
Claim 57 further recites the that (a)the G-CSFR transmembrane domain comprises the amino acid sequence of SEQ ID NO: 8; (b) the G-CSFR Box 1 and Box2 region comprises the amino acid sequence of SEQ ID NO: 20; and (c) the IL-2Rβ intracellular domain comprises the amino acid sequence of SEQ ID NO: 21.
(a) Nager discloses that the “tyrosine kinase activating domain” (transmembrane and Jak-binding domains) of G-CSFR comprises the amino acid sequence according to SEQ ID NO: 95 (pg. 20, Table 1B), which comprises the amino acid sequence of instant SEQ ID NO: 8. See alignment:
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(b) Nager discloses that the “tyrosine kinase activating domain” (transmembrane and Jak-binding domains) of G-CSFR comprises the amino acid sequence according to SEQ ID NO: 95 (pg. 20, Table 1B), which is 96.5% identical to instant SEQ ID NO: 20. See alignment:
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The difference between Nager’s SEQ ID NO: 95 and the instantly claimed sequence is that Nager’s SEQ ID NO: 95 does not include the last two amino acid residues (positions 61-62) of instant SEQ ID NO: 20. However, Rajpal discloses the N-terminal flanking regions of immunoreceptor tyrosine-based inhibitory motif- (ITIM-) containing intracellular domains for naturally-occurring receptors, including G-CSFR according to SEQ ID NO: 350 (Table 3, pg. 43). Rajpal’s SEQ ID NO: 350 is a sequence comprising the amino acid sequence according to instant SEQ ID NO: 20, as instantly claimed. See alignment:
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Therefore, prior to the effective filing date of the instantly claimed invention, it would have been prima facie obvious to one of ordinary skill in the art to modify the invention of Greenberg and Nager combined such that the G-CSFR domain comprises the amino acid sequence of instant SEQ ID NO: 20, as found in Rajpal, with a reasonable expectation of success because the claimed sequence corresponds to the known, naturally-occurring sequence of G-CSFR, and therefore this sequence would have been suitable to construct the chimeric receptor of the prior art references.
(c) Nager discloses that the “tyrosine effector domain” (cytotail domain) of IL-2Rβ comprises the amino acid sequence according to SEQ ID NO: 135 (pg. 21, Table 1B), which comprises the amino acid sequence according to instant SEQ ID NO: 21. See alignment:
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For these reasons, claim 57 would have been prima facie obvious over the prior art.
Dependent claims:
Regarding claim 58, Greenburg discloses that G-CSFR undergoes homodimerization (pg. 11, ll. 27-29) and induces cellular proliferation upon activation by binding of its ligand, G-CSF (pg. 5, ll. 12-18; pg. 25, ll. 12-23; claim 17). Nager discloses that the chimeric receptors undergo dimerization (par. 20, 220, 223, 486) and induces proliferation, persistence, STAT activation, cytotoxicity upon activation by binding of its ligand (par. 52-57).
Regarding claims 60-62, Greenberg discloses expression of the chimeric receptor in lymphocytes, such as T cells and B cells. See, e.g., Abstract; pg. 4, ll. 30-33; pg. 7, ll. 29-32. Greenberg further discloses that cytotoxic T cells can be isolated from cancer patients (pg. 2, ll. 31-34), which reads on primary cells. Nager discloses expression of the chimeric receptor in immune cells, such as T cells, B cells, NK cells, NKT cells, macrophages, and dendritic cells. The immune cell may also be derived from a stem cell. See, e.g., Abstract; par. 42, 186. Nager further discloses that the cells may be obtained from a number of sources, including peripheral blood, of the subject (par. 293), which reads on primary cells.
Regarding claims 63, 69-72, Greenburg discloses that the chimeric receptor is encoded by a retroviral vector or a plasmid, and introduced into a host cell. See, e.g., pg. 8, ll. 24-28; pg. 9, ll. 4-10; pg. 14-17. Nager discloses that the chimeric receptor is encoded by a plasmid, lentivirus, retrovirus or adenovirus, and introduced into a host cell. See, e.g., par. 189, 317, 321.
Regarding claim 76, Nager discloses “kits” comprising one or more containers comprising an isolated immune cells comprising one or more polynucleotides encoding the chimeric cytokine receptor, and instructions for use. See, e.g., par. 339-342.
Response to arguments:
Applicant’s remarks filed 12/30/2025 have been carefully considered but are not found persuasive for the following reasons:
Applicant argues that the prior art does not teach or fairly suggest the limitation “wherein the chimeric receptor homodimerizes upon contact with G-CSF,” as claimed, and such activity would have been an unexpected result prior to the effective filing date of the instantly claimed invention. See, pg. 6-10 of applicant’s reply.
As instructed by MPEP 2111.04, claim scope is not limited by claim language that does not limit a claim to a particular structure. In this case, the recitation “wherein the chimeric receptor homodimerizes upon contact with G-CSF” is directed to a functional property of the claimed chimeric receptor but does not clearly or necessarily further limit the structure thereof. Accordingly, since the prior art structure is capable of performing the recited function, the prior art meets the claim. Moreover, Greenburg expressly recognizes that G-CSFR undergoes homodimerization (pg. 11, ll. 27-29), and Nager expressly teaches that the chimeric receptors undergo dimerization (par. 20, 220, 223, 486), as claimed. For these reasons, the limitation “wherein the chimeric receptor homodimerizes upon contact with G-CSF” is not found to necessarily result in a structural difference which patentably distinguishes the claimed chimeric receptor from that of the prior art.
Homodimerization and binding with the corresponding ligands would have been expected results of the claimed cytokine receptor. In addition to the teachings of Greenburg and Nager (as outlined in the preceding paragraph), Morella et al. (1995) "The Action of Interleukin-2 Receptor Subunits Defines a New Type of Signaling Mechanism for Hematopoietin Receptors in Hepatic Cells and Fibroblasts" Journal of Biological Chemistry, 270(14), 8298-8310, of record, discloses chimeric cytokine receptors comprising an extracellular domain of G-CSFR, and the transmembrane and intracellular domains of IL-2Rβ, γc or gp130. See, e.g., Abstract, Table 1, and Receptor an JAK3 Expression Vectors on page 8299. As depicted in Figure 13, wild-type G-CSFR undergoes homodimerization upon binding of its corresponding ligand (GCSF) to the extracellular domain of the receptor, and this homodimerization activity is retained when the transmembrane and intracellular domains are substituted with those of IL-2Rβ to form a chimeric receptor. (The figure further shows that G-CSFR+IL-2Rβ chimera may also undergo heterodimerization with a G-CSFR+IL-2Rγc chimera, if present, as taught by Greenburg and identified in applicant’s remarks).
Figure 13 is reproduced, below:
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See also, Horan et al. (1996) “Dimerization of the extracellular domain of granulocyte-colony stimulating factor receptor by ligand binding: a monovalent ligand induces 2:2 complexes” Biochemistry, 35(15), 4886-4896, which further provides experimental evidence that G-CSFR homodimerization is mediated through ligand binding to the extracellular domain thereof. In particular, deletion of the transmembrane and intracellular domains of G-CSFR did not eliminate homodimerization activity, but rather homodimerization may occur only through the extracellular domain of the receptor (see, e.g., Abstract). Since the extracellular domain of G-CSFR is retained in the claimed chimeric receptor, retention of the homodimerization activity would have been expected.
For these reasons, and those stated in the new grounds of rejection, applicant’s traversal is found unpersuasive.
Claim 64 is rejected under 35 U.S.C. 103 as being unpatentable Greenberg, Nager, and Rajpal, as applied to claims 57-58, 60-63, 69-72, and 76 above; in further view of WO 2005/072340 A2 to Ayalon-Soffer et al.
This rejection is newly applied, necessitated by amendment. Applicant’s traversal is for the same reasons addressed above.
Regarding claim 64, the claim recites that the extracellular domain (ECD) of G-CSFR comprises the amino acid sequence set forth in SEQ ID NO: 5. This limitation is not taught by Greenberg, Nager, and Rajpal.
Prior to the effective filing date of the instantly claimed invention, Ayalon-Soffer provides an amino acid sequence for wild-type, human G-CSFR according to SEQ ID NO: 183. See, e.g., Fig. 106. This sequence comprises the amino acid sequence of instant SEQ ID NO: 5, as instantly claimed. See alignment:
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Therefore, prior to the effective filing date of the instantly claimed invention, it would have been prima facie obvious to one of ordinary skill in the art to modify the invention of Greenberg such that the G-CSFR domain comprises the amino acid sequence of instant SEQ ID NO: 5, as found in Ayalon-Soffer, with a reasonable expectation of success because the claimed sequence corresponds to the known, wild-type sequence of human G-CSFR, and therefore this sequence would have been suitable to construct Greenberg’s chimeric receptor comprising the ECD of G-CSFR.
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 57-58, 60, 63, 69, 71-72, and 76 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over the claims of copending U.S. Application No. 18/286,045 (reference to claim listing filed 04/02/2024). Although the claims at issue are not identical, they are not patentably distinct from each other because the copending claims anticipate the instant claims. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
This rejection is newly applied, necessitated by amendment.
The copending claims a chimeric receptor comprising an extracellular domain (ECD) of G-CSFR, a transmembrane domain (TMD) of G-CSFR, and an intracellular domain (ICD) comprising at least one signaling molecule binding site from an ICD of a cytokine receptor; wherein the at least one signaling molecule binding site is a SHC binding site and/or STAT5 binding site of IL-2Rβ; wherein the ICD of the chimeric receptor further comprises at least one Box 1 and Box 2 region of G-CSFR. See, e.g., claims 311, 314.
The copending claims further recite that the TMD comprises a sequence set forth in SEQ ID NO: 88. See, e.g., claim 314. This sequence is identical to instant SEQ ID NO: 8. See alignment:
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The copending claims further recite that the ICD comprises an amino acid sequence of SEQ ID NO: 90. See, e.g., claim 314. This sequence is identical to instant SEQ ID NO: 20. See alignment:
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The copending claims further recite that the ICD comprises an amino acid sequence of SEQ ID NO: 91. See, e.g., claim 314. This sequence is identical to instant SEQ ID NO: 21. See alignment:
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The copending claims further recite that the activated form of the chimeric receptor forms a homodimer, and, optionally, activation of the chimeric receptor causes a cellular response comprising at least one of proliferation, viability, persistence, cytotoxicity, cytokine secretion, memory, and enhanced activity of a cell expressing the receptor, and, optionally, the chimeric receptor is activated upon contact with a G-CSF (claim 312). Therefore, the limitation of instant claim 57 “wherein the chimeric receptor homodimerizes upon contact with G-CSF” is met by the copending claims.
For these reasons, instant claim 57 is anticipated by the copending claims.
Regarding instant claim 58, the copending claims recite that the activated form of the chimeric receptor forms a homodimer, and, optionally, activation of the chimeric receptor causes a cellular response comprising at least one of proliferation, viability, persistence, cytotoxicity, cytokine secretion, memory, and enhanced activity of a cell expressing the receptor, and, optionally, the chimeric receptor is activated upon contact with a G-CSF (claim 312). Further, the G-CSF is a wild-type G-CSF, and the extracellular domain of the G-CSFR is a wild-type extracellular domain (claim 313).
Regarding instant claims 60, 63, 69, 71-72, the copending claims further recite a nucleic acid encoding the chimeric receptor (claims 320), and a vector comprising thereof (claim 321), and expression vectors comprising thereof (claims 319-321). The chimeric receptor is also expressed in a cell, preferably an immune cell (claims 314 and 316).
Regarding instant claim 76, the copending claims recite a “kit” comprising cells, preferably immune cells, comprising one or more chimeric receptors, or one or more expression vectors encoding thereof, instructions for use, and at least one cytokine that binds the chimeric receptor, or one or more expression vectors encoding thereof (claim 319).
Claims 61-62 and 70 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over the claims of copending U.S. Application No. 18/286,045 (reference to claim listing filed 04/02/2024), as applied to claims 57-58, 60, 63, 69, 71-72, and 76 above; in view of WO 94/22914 to Greenberg et al. Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims would have been prima facie obvious over the copending claims and secondary references. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
This rejection is newly applied, necessitated by amendment.
The teachings of Greenberg have been discussed above.
The copending claims recite the chimeric receptor is expressed in a cell, preferably an immune cell. See, e.g., claims 314 and 316. The copending claims do not recite that the immune cell is a T cell, an NK cell, an NKT cell, a B cell, a plasma cell, a macrophage, or a dendritic cell, as instantly claimed in claim 61.
However, Greenberg discloses expression of the chimeric receptor in lymphocytes, such as T cells and B cells. See, e.g., Abstract; pg. 4, ll. 30-33; pg. 7, ll. 29-32. Such cells are useful for treating cancer. See, e.g., pg. 2, ll. 28-35; pg. 16, ll. 23-34; pg. 17, ll. 10-21.
Therefore, prior to the effective filing date of the instantly claimed invention, it would have been prima facie obvious to one of ordinary skill in the art to modify the invention of the copending claims by selecting a T cell, as found in Greensburg, with a reasonable expectation of success because the copending claims (e.g., claim 318) recites treating a cancer in a subject by administration of an immune cell expressing the chimeric receptor, and T cells were known in the art as therapeutically useful cell types for treating cancer in a subject, as suggested by Greenberg.
Regarding instant claim 62, Greenberg further discloses that T cells can be isolated from cancer patients (pg. 2, ll. 31-34), which reads on primary cells.
Regarding instant claim 70, Greenburg discloses that the chimeric receptor is encoded by a retroviral vector or a plasmid for introduction into a T cell. See, e.g., pg. 8, ll. 24-28; pg. 9, ll. 4-10; pg. 14-17.
Claim 64 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over the claims of copending U.S. Application No. 18/286,045 (reference to claim listing filed 04/02/2024), as applied to claims 57-58, 60, 63, 69, 71-72, and 76 above; in view of WO 2005/072340 A2 to Ayalon-Soffer et al. Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims would have been prima facie obvious over the copending claims and secondary references. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
This rejection is newly applied, necessitated by amendment.
Regarding instant claims 64, the claim recites that the extracellular domain (ECD) of G-CSFR comprises the amino acid sequence set forth in SEQ ID NO: 5. The copending claims do not recite this limitation.
Prior to the effective filing date of the instantly claimed invention, Ayalon-Soffer provides an amino acid sequence for wild-type, human G-CSFR according to SEQ ID NO: 183. See, e.g., Fig. 106. This sequence comprises the amino acid sequence of instant SEQ ID NO: 5, as instantly claimed. See alignment, provided above.
Therefore, prior to the effective filing date of the instantly claimed invention, it would have been prima facie obvious to one of ordinary skill in the art to modify the invention of the copending claims such that the G-CSFR domain comprises the amino acid sequence of instant SEQ ID NO: 5, as found in Ayalon-Soffer, with a reasonable expectation of success because the instantly claimed sequence corresponds to the known, wild-type sequence of human G-CSFR, and therefore this sequence would have been suitable to construct the chimeric receptor of the copending claims.
Noncompliance with CFR 1.111(b):
Applicant’s remarks field 12/30/2025 have been carefully considered. Applicant indicated that any action regarding the NSDP rejections will be deferred until the pending claims are otherwise allowable. See, pg. 10 of applicant’s reply. As instructed by MPEP 804, a complete response to a NSDP rejection is either a reply by applicant showing that the claims subject to the rejection are patentably distinct from the reference claims or the filing of a terminal disclaimer in accordance with 37 CFR 1.321. Such a response is required even when the nonstatutory double patenting rejection is provisional. Accordingly, applicant’s reply filed 12/30/2025 is not in compliance with 37 CFR 1.111(b), which requires a complete reply to every ground of objection and rejection set forth in the prior Office action. Applicant is respectfully reminded to provide a complete reply to every ground of objection and rejection, as required by 37 CFR 1.111(b), in order to avoid delays prosecution.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JAMES J GRABER whose telephone number is (571)270-3988. The examiner can normally be reached Monday-Thursday: 9:00 am - 4:00 pm.
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/JAMES JOSEPH GRABER/Examiner, Art Unit 1631