NOTE: THIS NON-FINAL REJECTION IS A RE-ISSUE OF THE NON-FINAL REJECTION MAILED 04/29/2026 BECAUSE APPLICANT’S AMENDMENT FILED 03/02/2026 WAS NOT PROPERLY SPLIT SUCH THAT THE AMENDED CLAIMS WERE NOT LISTED AS THE MOST RECENT CLAIM SET AND THEREFORE WERE NOT CONSIDERED.
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 .
1. Claims 1 – 4 and 6 – 21 are pending.
Election/Restrictions
2. Applicant’s election of Group I (claims 1 – 12) in the reply filed on 03/02/2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
3. Claims 13 – 21 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 03/02/2026.
4. Applicant has elected the following species: albumin as the hepatocyte-specific expressed gene; human immunoglobulin G as the target protein; T2A peptide as the 2A peptide in the reply filed on 03/02/2026.
Priority
5. This application claims domestic benefit to application PCT/KR2021/005510 filed 04/30/2021 and foreign priority to application KR10-2021-0042615 filed 04/01/2021.
6. Should applicant desire to obtain the benefit of foreign priority under 35 U.S.C. 119(a)-(d) prior to declaration of an interference, a certified English translation of the foreign application must be submitted in reply to this action. 37 CFR 41.154(b) and 41.202(e).
Failure to provide a certified translation may result in no benefit being accorded for the non-English application.
Information Disclosure Statement
7. The information disclosure statement (IDS) submitted on 09/25/2023 is acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Drawings
8. The drawings are objected to because of the following informalities: there is description of color in the Specification of Figure 4 on page 8, para. 3, and the various colors cannot be distinguished from each other since the figures are in black and white.
Color photographs and color drawings are not accepted in utility applications unless a petition filed under 37 CFR 1.84(a)(2) is granted. Any such petition must be accompanied by the appropriate fee set forth in 37 CFR 1.17(h), one set of color drawings or color photographs, as appropriate, if submitted via the USPTO patent electronic filing system or three sets of color drawings or color photographs, as appropriate, if not submitted via the via USPTO patent electronic filing system, and, unless already present, an amendment to include the following language as the first paragraph of the brief description of the drawings section of the specification:
The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee.
Color photographs will be accepted if the conditions for accepting color drawings and black and white photographs have been satisfied. See 37 CFR 1.84(b)(2).
Specification
9. The use of the term pGEM-T, ABI Prism 3730XL, HyBond, ECL, HiLoad, Superdex, Acquity UPLC, Empower, which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Claim Objections
10. Claim 1 is objected to because the claim recites both “a vector” (product) and “are introduced” (a method). A suggested wording of claim 1 is the following: A vector comprising a hepatocyte-specific expressed gene and a gene encoding a target protein, wherein the target protein is at least one selected from the group consisting of human immunoglobulin G (hIgG), a CD20 antibody, a HER2 antibody, an EGFR antibody, a TNF-alpha antibody, an Fc region of an antibody and Fc region-fused proteins. The objection does not rise to a 112(b) rejection because it is clear Applicant is claiming a vector based on Applicant’s specification at page 17 – 18 regarding construction of donor plasmid and Figure 1A (left).
11. Claim 7 is objected to because of the following informalities: in line 2 – 3, “and a gene encoding a target protein” should read “and the gene encoding the target protein” to clarify that the gene encoding the target protein of claim 7 is the same as that recited in claim 1. Appropriate correction is required.
12. Claim 8 is objected to because of the following informalities: in line 3, “amino acid sequences” should read “amino acids” to clarify that 2A peptide consists of a sequence of 18 to 22 amino acids and not multiple sequences. Appropriate correction is required.
13. Claim 10 is objected to because of the following informalities: in line 2 – 3, “a gene encoding a 2A peptide” should read “the gene encoding the 2A peptide” to clarify that the gene encoding the 2A peptide of claim 10 is the same as that recited in claim 7. Appropriate correction is required.
14. Claim 11 is objected to because of the following informalities: in line 2, “in the order the” should read “in the order of”. Appropriate correction is required.
15. Claim 11 is objected to because of the following informalities: in line 2, “the gene encoding a” should read “the gene encoding the”; in line 3, “a secretory signal peptide” should read “the secretory signal peptide”; in line 3, “an Fc” should read “the Fc”; in line 4, “a target protein” should read “the target protein” to clarify that the recited gene are the same as those recited in claims 1 and 10. Appropriate correction is required.
16. Claim 12 is objected to because of the following informalities: in line 2, “wherein the secretory signal peptide is a amino acid sequences set forth SEQ ID NO: 1” should read “wherein the gene encoding the secretory signal peptide encodes the sequence set forth in SEQ ID NO: 1” to clarify that the gene sequence encoding the secretory signal peptide encodes SEQ ID NO: 1 and not any amino acid sequence in SEQ ID NO: 1. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
17. Claim 11 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
18. It is unclear if claim 11 is further requiring “the gene encoding an Fc region of an antibody” or is an error because of the amendment to claim 1 to delete requirement of this gene and its inclusion in the Markush group.
Claim Interpretation
19. For the purpose of applying prior art, claim 1 is interpreted as a vector comprising a hepatocyte-specific expressed gene and a gene encoding a target protein, wherein the target protein is at least one selected from the group consisting of human immunoglobulin G (hIgG), a CD20 antibody, a HER2 antibody, an EGFR antibody, a TNF-alpha antibody, an Fc region of an antibody and Fc region-fused proteins and not a method of constructing a vector.
20. For the purpose of applying prior art, “human immunoglobulin G (hIgG)” of claim 1 is interpreted as hIgG Fc based on Applicant’s specification at page 7 – 8, page 17, last para., and Figure 1, 2A, and 3.
21. For the purpose of applying prior art, claim 4 is interpreted as the vector of claim 1 because the elected claims are drawn to a vector and not a method.
22. For the purpose of applying prior art, claim 11 is interpreted as the vector of claim 10, wherein the vector is configured in the order of the hepatocyte-specific expressed gene-the gene encoding the 2A peptide-the gene encoding the secretory signal peptide-the gene encoding the target protein because Applicant has amended claim 1 to delete “a gene encoding an Fc region of an antibody” and instead include it in the Markush group of claim 1.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
23. Claim(s) 1 – 4 and 6 is/are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Ballance (US-20180200346-A1; Filed 12/21/2017; Published 07/19/2018), hereinafter Ballance.
Claim 1 is drawn to a vector into which a hepatocyte-specific expressed gene, and a gene encoding a target protein are introduced, wherein the target protein is at least one selected from the group consisting of human immunoglobulin G (hIgG), a CD20 antibody, a HER2 antibody, an EGFR antibody, a TNF-alpha antibody, Fc region of antibody and Fc region-fused proteins.
Regarding claims 1 – 4, Ballance teaches a vector comprising a gene encoding human serum albumin (“a hepatocyte-specific expressed gene” of claim 1 and 4; “albumin” of claims 2 and 3) and human IgG (“human immunoglobulin G (hIgG)” of claim 1) (page 103, para. 0798 - 0801; Figure 4; page 2, para. 0017).
Regarding claim 6, Ballance teaches that the polynucleotide encoding the fusion protein is cloned without a stop codon, otherwise a Fc containing-fusion protein will not be produced (page 103, para. 0800).
Therefore, Ballance anticipates claims 1 – 4 and 6.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
24. Claim(s) 1 – 4 and 6 – 9 is/are rejected under 35 U.S.C. 103 as being unpatentable over Ballance (US-20180200346-A1; Filed 12/21/2017; Published 07/19/2018), hereinafter Ballance in view of Chng (Chng, Jake, et al. MAbs. Vol. 7. No. 2. Taylor & Francis, 2015), hereinafter Chng.
Ballance anticipates claims 1 – 4 and 6 as set forth above. Ballance does not teach a 2A peptide between albumin and human IgG of claim 7 that consists of 18 to 22 amino acids of claim 8 that is T2A of claim 9. However, Ballance teaches the albumin fusion proteins may include a linker peptide between the fused portions to provide greater physical separation between the moieties and thus maximize the accessibility of the therapeutic protein portion, for instance, for binding to its cognate receptor (page 30, para. 0125). Ballance teaches the linker sequence may be cleavable by a protease and the albumin fusion proteins may have the following formula R1-L-R2 or R2-L-R1 where R1 is a therapeutic protein, peptide or polypeptide and L is a linker, and R2 is a serum albumin sequence (page 30, para. 0127). Ballance teaches a plasmid DNA coding for the fusion of albumin to the therapeutic protein is transfected into a suitable host so that the host including eukaryotic cells or a transgenic organism expresses the fusion polypeptide (page 1, para. 0005). Ballance teaches therapeutic proteins in their native state or when recombinantly produced are typically labile molecules exhibiting short shelf-lives and when formulated for administration they must be lyophilized and refrigerated at all times during storage rendering the molecules difficult to transport and/or store (page 1, para. 0006). Ballance teaches therapeutic proteins are formulated in combination with large proportion of albumin carrier molecule, though this is an undesirable and expensive feature of the formulation (page 1, para. 0006). Ballance teaches there is a need for stabilized, long lasting formulations of proteinaceous therapeutic molecules that are easily dispensed, preferably with a simple formulation requiring minimal post-storage manipulation (page 1, para. 0007). Ballance teaches that the albumin fusion proteins comprising a therapeutic protein such as a polypeptide or antibody or fragments and variants thereof is sufficient to prolong the shelf life of the therapeutic protein, and/or stabilize it, and/or its activity in solution in vitro and/or in vivo (page 1, para. 0009).
Regarding claims 7 – 9, Chng teaches a vector encoding an antibody and a 2A peptide (claim 7) that is 18 amino acids (claim 8) that is T2A (claim 9) (Figure 1). Chng teaches 2A linked genes are translated in one open reading frame and self-cleavage occurs co-translationally (page 404, left col. para. 2). Chng teaches transfection of the vector into CHO cells and the T2A sequence enhanced mAb expression by 2.6-fold compared to other 2A peptides (page 404, right col. last para; Figure 2; page 406, left col. last para.; page 408, left col. para. 1). Chng teaches T2A had the highest mAb titers in stably transfected CHO cells (page 406, right col.; Figure 3A). Chng teaches purified products from T2A had more correctly cleaved products and contained relatively lower levels of aggregates compared to the other 2A peptides (page 407, left col. para. 2). Chng teaches IgG monoclonal antibodies are the best-selling class of biopharmaceuticals on the market (page 403, left col.). Chng teaches 2A linked genes are translated in one open reading frame and self-cleavage occurs co-translationally to give equal amounts of the co-expressed proteins (page 404, left col. para. 2). Chng teaches CHO cells are the dominant host for producing mAb because of their capacity to perform proper folding, assembly, and human-like glycosylation (page 403, left col.).
It would have been obvious prior to the effective filing date of the invention as claimed for the person of ordinary skill in the art to combine the teachings of Ballance regarding a vector encoding an albumin-human IgG Fc fusion that may also contain a linker peptide between the fused portions where the linker peptide may be cleaved by a protease with the teachings of Chng regarding a vector encoding an antibody and a T2A peptide for cleavage increased expression of the antibody and a purified antibody with less aggregates to arrive at the claimed vector further comprising a gene encoding a 2A peptide between the hepatocyte-specific expressed gene and a gene encoding a target protein. One would have been motivated to combine the teachings of Ballance and Chng to include a nucleic acid encoding a 2A peptide between the albumin gene and the nucleic acid encoding the human IgG to increase the stability and expression of the fusion as Ballance teaches there is a need for stabilized, long lasting formulations of proteinaceous therapeutic molecules that are easily dispensed, preferably with a simple formulation requiring minimal post-storage manipulation and Chng teaches IgG monoclonal antibodies are the best-selling class of biopharmaceuticals on the market. One would have a reasonable expectation of success in combining the teachings as Ballance teaches the linked sequence may be cleavable by a protease and the albumin fusion proteins may have the following formula R1-L-R2 or R2-L-R1 where R1 is a therapeutic protein, peptide or polypeptide and L is a linker, and R2 is a serum albumin sequence and Ballance teaches that the albumin fusion proteins comprising a therapeutic protein such as a polypeptide or antibody or fragments and variants thereof is sufficient to prolong the shelf life of the therapeutic protein, and/or stabilize it, and/or its activity in solution in vitro and/or in vivo and Chng teaches the T2A sequence enhanced mAb expression by 2.6-fold compared to other 2A peptides and Chng teaches T2A had the highest mAb titers in stably transfected CHO cells and Chng teaches purified products from T2A had more correctly cleaved products and contained relatively lower levels of aggregates compared to the other 2A peptides.
25. Claims 10 – 12 are rejected under 35 U.S.C. 103 as being unpatentable over Ballance (US-20180200346-A1; Filed 12/21/2017; Published 07/19/2018), hereinafter Ballance in view of Chng (Chng, Jake, et al. MAbs. Vol. 7. No. 2. Taylor & Francis, 2015), hereinafter Chng as applied to claims 1 – 4 and 6 – 9 above, and further in view of Kim (Kim, Young Min, et al. Biomaterials 167 (2018): 58-68.), hereinafter Kim in view of Hache (Haché RJ, et. al. J Biol Chem. 1983 Apr 10;258(7):4556-64), hereinafter Hache as evidenced by Compere (Compere, Sally J., et. al. European Journal of Biochemistry 116.3 (1981): 437-440), hereinafter Compere.
Ballance anticipates claims 1 – 4 and 6 as set forth above and Ballance in view of Chng make obvious claims 7 – 9 as set forth above.
Regarding claim 10, Ballance teaches the polynucleotide encoding an albumin fusion protein may contain a secretory signal sequence that facilitates secretion of the protein (page 60, para. 0378). Ballance teaches typically, the signal sequence is positioned in the coding region of the polynucleotide to be expressed towards or at the 5’ end of the coding region (page 60, para. 0378) but does not teach the secretory signal peptide is downstream of the gene encoding a 2A peptide of claim 10 or the configuration of the vector of claim 11 or SEQ ID NO: 1 of claim 12. However, Ballance teaches the linker sequence may be cleavable by a protease and the albumin fusion proteins may have the following formula R1-L-R2 or R2-L-R1 where R1 is a therapeutic protein, peptide or polypeptide and L is a linker, and R2 is a serum albumin sequence (page 30, para. 0127).
Regarding claims 10 and 11, Kim teaches a vector for expression of CD20 mAb in chickens comprising a nucleic acid sequence encoding human IgG and the lysozyme signal peptide sequence upstream of the sequence encoding the mAb (page 59, right col. para. 3; Figure 1a). Kim teaches the vector was used to produce transgenic chickens expressing the antibody (page 62, right col. para. 3). Kim teaches the mAbs were strongly expressed in oviduct tissue and secreted into the egg white (page 63, left col. para. 1 – 2). Kim teaches the CD20 mAb produced in chickens has enhanced Fc-effector functions including CDC and ADCC compared to rituximab and the Fc-effector function were consistent irrespective of generation and integration pattern (page 65, right col. para. 1; page 67, left col. para. 1). Kim teaches this enhanced CDC and ADCC activity may be due to the high level of terminal galactose residues in its N-glycans and high mannose N-glycoform, respectively (page 67, left col. para. 1 – 3). Kim teaches the N-glycosylation of therapeutic antibodies is an important parameter from the perspective of functionality and efficacy because of its role in activation of immune Fc-effector functions (page 66, right col., para. 1). Kim teaches the general N-glycosylation pattern of recombinant proteins produced in transgenic chickens has high mannose, a core afucosylated form, and terminal galactosylation that are believed to enhance the Fc-effector functions of antibodies (page 59, left col. para. 3; page 64, left col. para. 1; page 66, right col., para. 1). Kim teaches the results suggest the potential of the germline-competent transgenic chicken bioreactor, as its capacity to allow post-translational modifications in Abs with superior Fc-effector functions and these characteristics were maintained in successive generations (page 67, left col. last para.). Kim teaches this germline transgenic chicken bioreactor system is suitable for the production of anti-cancer antibodies (page 67, left col. last para.). Kim teaches chicken is the most efficient animal bioreactor for the production of anti-cancer antibodies because of its relatively short generation time, plentiful reproductive capacity, and daily deposition in the egg white (Abstract). Kim teaches recombinant mAbs such as rituximab is used to treat non-Hodgkin’s lymphoma, chronic lymphocytic leukemia, and rheumatoid arthritis (page 58, left col.). Kim teaches the US FDA has approved a recombinant protein-based drug produced by transgenic hens (page 59, left col. para. 3). Kim teaches a signal peptide of chicken lysozyme but does not teach SEQ ID NO: 1 of claim 12. One would have been motivated to combine the teachings of Ballance, Chng, and Kim as all are directed to methods of producing therapeutic antibodies.
Regarding SEQ ID NO: 1 of claim 12, Hache teaches the sequence flanking the first exon of chicken serum albumin gene includes SEQ ID NO: 1 in Figure 5 (page 4558, left col. para. 4 and right col. para. 1), which is a secretory signal peptide as evidenced by Compere (Abstract; page 437, left col., para. 1; page 440, left col. para. 1 and right col. para. 1).
It would have been obvious prior to the effective filing date of the invention as claimed for the person of ordinary skill in the art to combine the teachings of Ballance regarding a vector encoding an albumin-human IgG Fc fusion that may also contain a linker peptide between the fused portions where the linker peptide may be cleaved by a protease and the vector may also encode secretory signal sequence that facilitates secretion of the protein where typically, the signal sequence is positioned in the coding region of the polynucleotide to be expressed towards or at the 5’ end of the coding region with the teachings of Chng regarding a vector encoding an antibody and a T2A peptide for cleavage increased expression of the antibody and a purified antibody with less aggregates with the teachings of Kim regarding a vector encoding a lysozyme signal peptide sequence upstream of the sequence encoding the mAb encoding human IgG to produce mAb in chickens with the teachings of Hache as evidenced by Compere regarding a secretory signal peptide of chicken albumin that is an amino acid sequence set forth in SEQ ID NO: 1 to arrive at the claimed vector further comprising a secretory signal peptide downstream of the gene encoding the 2A peptide wherein the vector is configured in the order of the albumin gene-the gene encoding the T2A peptide-the gene encoding the secretory signal peptide-the gene encoding human IgG and wherein the secretory signal peptide is an amino acid sequence set forth in SEQ ID NO: 1. One would have been motivated to combine the teachings of Ballance, Chng, Kim, and Hache to produce therapeutic human IgG in chickens as Kim teaches this germline transgenic chicken bioreactor system is suitable for the production of anti-cancer antibodies and Kim teaches chicken is the most efficient animal bioreactor for the production of anti-cancer antibodies because of its relatively short generation time, plentiful reproductive capacity, and daily deposition in the egg white and Kim teaches recombinant mAbs such as rituximab is used to treat non-Hodgkin’s lymphoma, chronic lymphocytic leukemia, and rheumatoid arthritis. One would have a reasonable expectation of success in combining the teachings as Kim teaches the mAbs were strongly expressed in the chicken and Kim teaches the US FDA has approved a recombinant protein-based drug produced by transgenic hens.
Conclusion
No claims allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ZANNA M BEHARRY whose telephone number is (571)270-0411. The examiner can normally be reached Monday - Friday 8:45 am - 5:45 pm.
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/ZANNA MARIA BEHARRY/Examiner, Art Unit 1632
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