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 .
Response to Amendment
The reply filed on 06/17/2026 has been entered. Claims 46, 192-195, and 198-209 are pending and examined.
Response to Arguments
The rejections and objections of claims not repeated in this Action are withdrawn because of either Applicant’s persuasive arguments or amendments to the claims.
With respect to Lockridge in view of Lin, Stadheim, or Coskun, Applicant argues that there is no motivation to link the claimed IL-10 protein to an Fc portion because Lockridge does not teach the function of the protein and neither Lin, Stadheim, Coskun, nor Garokhad remedies that deficiency.
In response to Applicant’s argument that there is no teaching, suggestion, or motivation to combine the references, the examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007).
In this case, Lockridge teaches that the cloned gene encodes an IL-10 homolog (see Fig. 2 on page 276 and also on page 277), which is involved in immune functions. Lockridge reasonably suggests that the cloned Il-10 homolog would function in host immune regulation. See the Discussion section starting page 276, right column.
With respect to Davison, Applicant states that the claim is amended. This argument has been fully considered but found unpersuasive because the previous Office action stated that Davison’s polypeptide and instant SEQ ID NO:125 are identical. In addition, the IL-10 taught by Lockridge is same as the claimed polypeptide in claim 46.
With respect to the amended base claim 46 and its dependent claims, the new ground of rejection is based previously applied references.
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.
Claims 46, 192, 198-205, 208, and 209 are rejected under 35 U.S.C. 103 as being unpatentable over Lockridge (PTO-892; page 1, Reference U) in view of US 20250367255 A1 (PTO-892; page 1, Reference B; "Lin”) and of US 9187552 B2 (PTO-892; page 1, Reference E, “Stadheim”) and US 8557769 B2 (PTO-892; page 1, Reference D, “Coskun”).
The claimed invention is drawn to a fusion protein comprising SEQ ID NO: 125 linked to a Fc portion.
In the previous Office action, Lockridge was cited teaching a viral homolog of IL-10 which is 98.2% sequence identical between reference amino acids 27-185 to instant SEQ ID NO: 125 and the protein was recognized a the host immune system (Lockridge; page 275, right column, paragraph 2). Lockridge teaches the IL-10-like gene to be compatible with the known functions of cIL-10 such as decreasing antigen-specific CD4+ T cell proliferation by reducing the expression of MHC II molecules on antigen-presenting cells (Lockridge; page 277, right column, paragraph 2).
Lockridge does not teach a Fc structures claimed in the instant claims 198-204 or Fc functions in claim 205.
However, Lin does teach a fusion protein using a Fc structure and the fusion protein with Fc exhibited an effect function recited in the instant claim 205.
Stadheim also teaches a beneficial effect of a Fc such as (ADCC) (Stadheim; page 37, column 1, lines 22-25).
Coskun teaches a GLP-1 fusion protein containing an Fc portion which is derived from human IgG4 but comprises one or more substitutions compared to the wild-type sequence as shown in SEQ ID NO:5 (Reference SEQ ID NO:5 is 100% sequence identical to instant SEQ ID NOs:33-34) (Cuskon; page 2-3, column 2-3, lines 66 and 1-2). Coskun teaches the Fc portion can include the hinge region and extend through the CH2 and CH3 domains and can further include one or more glycosylation sites (Cuskon; page 3, column 4, lines 19-22).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date, to have modified the fusion polypeptide containing IL-10-like ORF of Lockridge with the human Ig Fc constant region with half-life enhancing alterations of Lin with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to combine the fusion polypeptide containing IL-10-like ORF of Lockridge with the human Ig Fc constant region with half-life enhancing alterations of Lin to increase the fusion protein’s duration.
Therefore, it would have been obvious to one of ordinary skill in the art to combine the fusion polypeptide containing the IL-10-like ORF of Lockridge with the human Ig Fc constant region with half-life enhancing alterations of Lin to yield predictable results of extending the fusion protein’s duration within a target specimen.
It would have been prima facie obvious to one of ordinary skill, in the art before the effective filing date, to have modified the fusion polypeptide containing IL-10-like ORF of Lockridge with the human IgG1 or IgG4 Fc constant regions as shown in reference SEQ ID NOs: 2 and 6 of Lin with the Fc constant regions as shown in reference SEQ ID NO:19 of Stadheim with the Fc constant regions as shown in reference SEQ ID NO:5 of Cuskon with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to operably connect the IL-10-like ORF of Lockridge with a heterologous polypeptide containing a human IgG1 or IgG4 Fc constant region of Lin, Stadheim, and Cuskon to recruit effecter immune cells such as NK cells to destroy and kill a cell expressing hIL-10R.
Therefore, it would have been obvious to a person of ordinary skill in the art to
combine the fusion polypeptide containing the IL-10-like ORF of Lockridge with the IgG1 or IgG4 Fc constant regions of Lin, Stadheim, and Cuskon to yield a fusion protein that specifically binds hIL-10R to induce an effective immune response against a cell expressing hIL-10R.
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date, to have modified the fusion polypeptide containing IL-10-like ORF of Lockridge with the human IgG1 or IgG4 Fc constant regions with one or no more than 10 amino acid variations of Lin, Stadheim, and Cuskon with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to combine the fusion polypeptide containing the IL-10-like ORF of Lockridge with the IgG1 or IgG4 human Fc regions with one or no more than ten amino acid variations of Lin, Stadheim, and Cuskon in order to modify ADCC, Fc dimer stability, glycosylation, and half-life extension while retaining Fc receptor binding.
Therefore, it would have been obvious to a person of ordinary skill in the art to combine the fusion polypeptide containing the IL-10-like ORF of Lockridge with the IgG1 or IgG4 Fc constant regions with one to no more than ten amino acid variations of Lin, Stadheim, and Cuskon to yield predictable results of altered ADCC and enhance destruction and killing of the target cell.
The invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the references, especially in the absence of evidence on the contrary.
Claims 193-195 are rejected under 35 U.S.C. 103 as being unpatentable over Davison of record in view of Lin of record, Stadhein of record, and Coskun of record.
Davison teaches a viral interleukin-10 (IL-10) homolog encoded by simian cytomegalovirus where it plays a role in regulating host immune response. The reference viral IL-10 homolog is 100% identical to instant SEQ ID NO:125 between reference amino acids 27-185; reference amino acids 1-26 represent the heterologous polypeptide sequence operably connected to instant SEQ ID NO:125).
Davison does not teach Fc.
However, the combination of Lin, Stadhein, and Coskun teaches why one of ordinary skill in the art would have been motivated to make a fusion protein of Fc connected to Davison’s viral IL-10 protein. See above 103 rejection.
Claims 46, and 206-207 are rejected under 35 U.S.C. 103 as being unpatentable over Lockridge of record, in view of Lin of record ”) and Stadheim and Coskun of record., as applied to claim 46 above, and further in view of Farokhzad of record.
The combined references above teach the claimed fusion protein.
The combined references do not teach a nanoparticle carrier.
However, as stated in the previous Office action, Farokhzad teaches compositions and methods of using lipid nanoparticles as carriers for therapeutic agents (Farokhzad; Abstract; [2]). Farokhzad teaches that nanotechnology provides a means of improved methods for delivery of biomolecules with nanoparticles being effective platforms for protein delivery due to the possibility of fine-tuning their biophysiochemical properties and their ability to protect and release proteins in a controlled manner (Farokhzad; [2]). Farokhzad teaches that nanoparticles allow for the efficient delivery of labile biomolecules using an organic-solvent-free polymer thermoexpansion mechanism with clinical potential, capable of effectively delivering a molecule such as IL-10 in a sustained manner with minimal or no loss of bioactivity, and an improved half-life and in vivo efficacy compared with administration of the therapeutic agent alone (Farokhzad; [3]). Farokhzad also teaches the nanoparticles to delivery organic molecules such as Fc fusion proteins that can offer stability or selective targeting of a cell or tissue type (Farokhzad; [65]).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date, to combine the fusion polypeptide of Lockridge with the lipid nanoparticle carrier of Farokhzad with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to combine the fusion polypeptide of Lockridge with the lipid nanoparticle carrier of Farokhzad in order to improve the half-life and in vivo efficacy of the fusion protein with minimal to no loss of bioactivity.
Therefore, it would have been obvious to a person of ordinary skill in the art to combine the fusion polypeptide Lockridge with the lipid nanoparticle carrier of Farokhzad to yield predictable results of improving the half-life and in vivo efficacy of the fusion protein with minimal to no loss of bioactivity.
The invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the references, especially in the absence of evidence on the contrary.
Farokhzad does teach compositions and methods of using lipid nanoparticles as carriers for therapeutic agents (Farokhzad; Abstract; [2]). Farokhzad teaches that nanotechnology provides a means of improved methods for delivery of biomolecules with nanoparticles being effective platforms for protein delivery due to the possibility of fine-tuning their biophysiochemical properties and their ability to protect and release proteins in a controlled manner (Farokhzad; [2]). Farokhzad teaches that nanoparticles allow for the efficient delivery of labile biomolecules using an organic-solvent-free polymer thermoexpansion mechanism with clinical potential, capable of effectively delivering a molecule such as IL-10 in a sustained manner with minimal or no loss of bioactivity, and an improved half-life and in vivo efficacy compared with administration of the therapeutic agent alone (Farokhzad; [3]). Farokhzad also teaches the nanoparticles to delivery organic molecules such as Fc fusion proteins that can offer stability or selective targeting of a cell or tissue type (Farokhzad; [65]).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date, to combine the fusion polypeptide of Davison with the lipid nanoparticle carrier of Farokhzad with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to combine the fusion polypeptide of Davison with the lipid nanoparticle carrier of Farokhzad in order to improve the half-life and in vivo efficacy of the fusion protein with minimal to no loss of bioactivity.
Therefore, it would have been obvious to a person of ordinary skill in the art to combine the fusion polypeptide Davison with the lipid nanoparticle carrier of Farokhzad to yield predictable results of improving the half-life and in vivo efficacy of the fusion protein with minimal to no loss of bioactivity.
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 46, 192-195, and 198-209 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 120, 259, 264, 269, 272, 282, 287, and 289-290 of copending Application No. 19/267,934 (reference application) in view of US 20250367255 A1 (PTO-892; page 1, Reference B; "Lin”) in further view of US 9187552 B2 (PTO-892; page 1, Reference E, “Stadheim”) in further view of US 8557769 B2 (PTO-892; page 1, Reference D, “Coskun”).
‘934 teaches in reference claim 1 a fusion protein comprising a fusion protein comprising any two or more of (a) a protein comprising an amino acid sequence at least about 85%-100% identical to the amino acid sequence set forth in any one of SEQ ID NOs:34-386 (Reference SEQ ID NO: 40 is 100% identical to instant SEQ ID NO:125 between reference amino acids 27-185; Reference SEQ ID NO:165 is 98.1% identical to instant SEQ ID NO:125 between reference amino acids 27-185; Reference SEQ ID NO:218 is 100% sequence identical to instant SEQ ID NO:125; Reference SEQ ID NO:340 is 98.1% sequence identical to instant SEQ ID NO:125); (b) a protein comprising an amino acid sequence of at least 85%-100% identical to amino acid sequence set forth in any one of SEQ ID NOs:387-576.
However, ‘934 does not teach instant claims the second heterologous protein to further comprise a half-life extension polypeptide; an immunoglobulin (Ig) Fc region; wherein the Ig Fc region comprises at least a portion of a hinge domain, a CH2 domain, and a CH3 domain; wherein the Ig Fc region comprises a hinge domain, a CH2 domain, and a CH3 domain; wherein the Ig Fc region is a human IgG (hIgG); wherein the hIgG is hIgG1 or hIgG4; wherein the amino acid sequence of the heterologous polypeptide comprises the amino acid sequence of any one of SEQ ID NOs:16-21 or 27-34; wherein the amino acid sequence of the heterologous polypeptide comprises or consists of the amino acid sequence of any one of SEQ ID NOs: 16-21 or 27-34, comprising no more than 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid variations; wherein the lg Fc region comprises one or more amino acid substitutions relative to a reference lg Fc region that reduces or abolishes one or more of the following effector functions relative to the reference Fc region: antibody dependent cell mediated cytotoxicity (ADCC), complement dependent cytotoxicity (CDC), and/or affinity to one or more Fc receptor.
However, Lin teaches a CD47 blocking agent comprising a form of human SIRPalpha that binds CD47, and incorporate a region of its extracellular domain linked with a particularly useful form of an IgG1-based Fc region or an IgG4-based Fc region wherein the SIRPalpha protein is fused directly or indirectly with an antibody constant region, of Fc region, having at least some effector function (i.e. SIRPalpha is an Fc fusion) (Lin; [0003]; [0068]). The Fc component “having an effector function” is an Fc component having at least some contribution for instance to antibody-dependent cellular cytotoxicity (ADCC) or some ability to fix complement (Lin; [0068]). Lin teaches the preferred embodiment of the instant invention wherein the Fc region is based on human antibodies of the IgG1 or IgG4 isotope which also includes the hinge-CH2-CH3 domains (Lin; [0068]; [0072]). Lin teaches the IgG1 constant region has the amino acid sequence as shown in reference SEQ ID NO:2 (Reference SEQ ID NO:2 comprises 100% of instant SEQ ID NO:16 between reference amino acids 9-227; comprises 100% of instant SEQ ID NO:17 between reference amino acids 8-226; comprises 100% of instant SEQ ID NO:18 between reference amino acids 5-227; and comprises 100% of instant SEQ ID NO:19 between reference amino acids 5-226) (Lin; [0069]). Lin additionally teaches the IgG4 constant region has the amino acid sequence as shown in reference SEQ ID NO:6 (Reference SEQ ID NO:6 is 100% sequence identical to instant SEQ ID NOs:31-32; Reference SEQ ID NO:6 comprises 100% of instant SEQ ID NO:27 between reference amino acids 13-229; comprises 100% of instant SEQ ID NO:28 between reference amino acids 13-228; comprises 100% of instant SEQ ID NO:29 between reference amino acids 7-229; comprises 100% of instant SEQ ID NO: 30 between reference amino acids 7-228) (Lin; [0072]). Lin teaches the Fc region to incorporate 1-, or 10 amino acid alterations including alterations that affect certain Fc properties such as Fc dimer stability, glycosylation, and half-life extension while retaining Fc receptor binding (Lin; [0073]).
Stadheim teaches Fc containing polypeptides which are useful as human and animal therapeutic agents (Stadheim; page 37, column 1, lines 5-9). Stadheim teaches the variable region of a monoclonal antibody recruits effecter cells such as natural killer (NK) cells and NK cells bind to the constant region (Fc) of the antibody and destroy cells to which the antibody is bound which is known as antibody-dependent cell cytotoxicity (ADCC) (Stadheim; page 37, column 1, lines 22-25). Stadheim teaches ADCC depends on N-glycosylation of the Fc region and structures that lack N-glycosylation still bind antigens but do not mediate ADCC (Stadheim; page 376, column 1, lines 25-34). Stadheim teaches that modification of specific amino acids in the Fc region of an antibody to modify the effector function is desirable (Stadheim; page 37, column 1, lines 47-50). Furthermore, Stadheim teaches the Fc region of an antibody to comprise reference SEQ ID NO:19 (Reference SEQ ID NO:19 is 100% sequence identical to instant SEQ ID NOs:20-21) (Stadheim; page 38, column 4, lines 34-36).
Coskun teaches a GLP-1 fusion protein containing an Fc portion which is derived from human IgG4 but comprises one or more substitutions compared to the wild-type sequence as shown in SEQ ID NO:5 (Reference SEQ ID NO:5 is 100% sequence identical to instant SEQ ID NOs:33-34) (Cuskon; page 2-3, column 2-3, lines 66 and 1-2). Coskun teaches the Fc portion can include the hinge region and extend through the CH2 and CH3 domains and can further include one or more glycosylation sites (Cuskon, page 3, column 4, lines 19-22).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date, to have modified the fusion polypeptide containing SEQ ID NO: 40, 165, 218, or 340 operably connected to a second protein of ‘934 with the human Ig Fc constant region with half-life enhancing alterations of Lin with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to swap the second protein of ‘934 with human Ig Fc constant region with half-life enhancing alterations of Lin to increase the fusion protein’s duration.
Therefore, it would have been obvious to one of ordinary skill in the art to combine the fusion polypeptide containing SEQ ID NO: 40, 165, 218, or 340 operably connected to a second protein of ‘934 with the human Ig Fc constant region with half-life enhancing alterations of Lin to yield predictable results of extending the fusion protein’s duration within a target specimen.
It would have been prima facie obvious to one of ordinary skill, in the art before the effective filing date, to have modified fusion polypeptide containing SEQ ID NO: 40, 165, 218, or 340 operably connected to a second protein of ‘934 with the human IgG1 or IgG4 Fc constant regions as shown in reference SEQ ID NOs: 2 and 6 of Lin with the Fc constant regions as shown in reference SEQ ID NO:19 of Stadheim with the Fc constant regions as shown in reference SEQ ID NO:5 of Cuskon with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to operably connect the fusion polypeptide containing SEQ ID NO: 40, 165, 218, or 340 of ‘934 with a heterologous polypeptide containing a human IgG1 or IgG4 Fc constant region of Lin, Stadheim, and Cuskon to recruit effecter immune cells such as NK cells to destroy and kill a cell expressing hIL-10R.
Therefore, it would have been obvious to a person of ordinary skill in the art to
combine the fusion polypeptide containing SEQ ID NO: 40, 165, 218, or 340 of ‘934 with the IgG1 or IgG4 Fc constant regions of Lin, Stadheim, or Cuskon to yield a fusion protein that specifically binds hIL-10R to induce an effective immune response against a cell expressing hIL-10R.
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date, to have combine the fusion polypeptide containing SEQ ID NO: 40, 165, 218, or 340 of ‘934 with the human IgG1 or IgG4 Fc constant regions with one or no more than 10 amino acid variations of Lin, Stadheim, and Cuskon with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to combine the fusion polypeptide containing the fusion polypeptide containing SEQ ID NO: 40, 165, 218, or 340 of ‘934 with the IgG1 or IgG4 human Fc regions with one or no more than ten amino acid variations of Lin, Stadheim, and Cuskon in order to modify ADCC, Fc dimer stability, glycosylation, and half-life extension while retaining Fc receptor binding.
Therefore, it would have been obvious to a person of ordinary skill in the art to combine the fusion polypeptide containing the fusion polypeptide containing SEQ ID NO: 40, 165, 218, or 340 of ‘934 with the IgG1 or IgG4 Fc constant regions with one to no more than ten amino acid variations of Lin, Stadheim, and Cuskon to yield predictable results of altered ADCC and enhance destruction and killing of the target cell.
Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the references, especially in the absence of evidence on the contrary.
This is a provisional nonstatutory double patenting rejection.
Claims 46, 134, and 206-207 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1, 120, 264, and 287 of copending Application No. 19/267,934 in view of US 10272050 B2 (PTO-892; page 1, Reference A; "Farokhzad").
'934 has been discussed above. The claimed invention differs from '934 with respect to instant claims 134 and 206-207, wherein a carrier comprises the isolated an isolated polypeptide comprising an amino acid sequence at least 85%-100% identical to SEQ ID NO:125 and wherein a carrier comprises the fusion protein of claim 46 wherein the carrier is a lipid nanoparticle. However, Farokhzad does teach compositions and methods of using lipid nanoparticles as carriers for therapeutic agents (Farokhzad; Abstract; [2]). Farokhzad teaches that nanotechnology provides a means of improved methods for delivery of biomolecules with nanoparticles being effective platforms for protein delivery due to the possibility of fine-tuning their biophysiochemical properties and their ability to protect and release proteins in a controlled manner (Farokhzad; [2]). Farokhzad teaches that nanoparticles allow for the efficient delivery of labile biomolecules using an organic-solvent-free polymer thermoexpansion mechanism with clinical potential, capable of effectively delivering a molecule such as IL-10 in a sustained manner with minimal or no loss of bioactivity, and an improved half-life and in vivo efficacy compared with administration of the therapeutic agent alone (Farokhzad; [3]). Farokhzad also teaches the nanoparticles to delivery organic molecules such as Fc fusion proteins that can offer stability or selective targeting of a cell or tissue type (Farokhzad; [65]).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date, to combine the fusion polypeptide of ‘934 with the lipid nanoparticle carrier of Farokhzad with reasonable expectation of success.
One of ordinary skill in the art would have been motivated to combine the fusion polypeptide of ‘934 with the lipid nanoparticle carrier of Farokhzad in order to improve the half-life and in vivo efficacy of the fusion protein with minimal to no loss of bioactivity.
Therefore, it would have been obvious to a person of ordinary skill in the art to combine the fusion polypeptide ‘934 with the lipid nanoparticle carrier of Farokhzad to yield predictable results of improving the route of administration of the fusion polypeptide and improve the half-life and in vivo efficacy of the fusion protein with minimal to no loss of bioactivity.
Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the references, especially in the absence of evidence on the contrary.
This is a provisional nonstatutory double patenting rejection.
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 Misook Yu whose telephone number is (571)272-0839. The examiner can normally be reached M-Th, 7-5pm.
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/MISOOK YU/Supervisory Patent Examiner, Art Unit 1641
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