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 – 20 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 Claims 13 – 20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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, a gene encoding an Fc region of an antibody, and a gene encoding a target protein. 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 Interpretation
17. For the purpose of applying prior art, claim 1 is interpreted as a vector comprising a hepatocyte-specific expressed gene, a gene encoding an Fc region of an antibody, and a gene encoding a target protein and not a method of constructing a vector.
18. For the purpose of applying prior art, a gene encoding a complete antibody such as an immunoglobulin is interpreted to meet the limitations of “a gene encoding an Fc region of an antibody, and a gene encoding a target protein” of claim 1 because immunoglobulins contain an Fc region and because Applicant’s Figure 1A shows human IgGFc region as one unit of the plasmid.
19. 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.
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.
20. Claim(s) 1 – 4 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, a gene encoding an Fc region of an antibody, and a gene encoding a target protein are introduced.
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 antibody (“a gene encoding an Fc region of an antibody, and a gene encoding a target protein” of claim 1) (page 104, para. 0802 – 0803; Figure 4; page 2, para. 0017).
Therefore, Ballance anticipates claims 1 – 4.
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.
21. Claim(s) 1 – 6 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 Kim (Kim, Young Min, et al. Biomaterials 167 (2018): 58-68.), hereinafter Kim as evidenced by NCBI (ALB albumin [Gallus gallus (chicken)], NCBI, https://www.ncbi.nlm.nih.gov/gene/396197; Accessed 04/27/2025) in view of Sharma (Sharma, Rajiv, et al. Blood, The Journal of the American Society of Hematology 126.15 (2015): 1777-1784.), hereinafter Sharma.
Ballance anticipates claims 1 – 4 as set forth above.
Regarding claim 6, Ballance teaches preparation of a vector encoding a albumin-fusion protein where the cDNA for a therapeutic protein is modified at the 5’ end to encode the last amino acids of albumin (page 96 – 97, para. 0744). 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). Ballance teaches vectors encoding bifunctional albumin-fusion proteins where a nucleic acid encoding a second protein of interest is inserted in frame downstream from the first albumin-fusion after removal of stop codons (page 99, para. 0767; Figure 8). Thus, Ballance teaches for expression of a albumin-fusion protein where the HA is expressed N-terminal to the target protein, the albumin does not include a stop codon.
Ballance does not teach human IgG of claim 5. However, Ballance teaches the fusion proteins may be useful for the treatment of hematopoietic related disorders such as leukemia and non-Hodgkin’s lymphoma (page 67, para. 0463; page 121, para. 1024). Ballance teaches construction of albumin fusion proteins can be made using the human Fc portion of the IgG molecule for cloning into the vector and Ballance teaches a sequence of the human IgG Fc region in SEQ ID NO: 36 (page 103, para. 0798 – 0799). Ballance teaches fusion of albumin to a therapeutic protein may be achieved by genetic manipulation such that the DNA coding for albumin is joined to the DNA coding for the therapeutic protein (page 1, para. 0005). Ballance teaches transforming or transfecting a suitable host with the fusion and expression of the fusion in vivo from a transgenic organism (page 1, para. 0005). Ballance teaches an embodiment of administration of albumin fusion proteins to an animal including a chicken to produce increased quantities of one or more antibodies including IgG (page 65, para. 0430; page 93, para. 0693).
Regarding “human immunoglobulin G” of claim 5, Kim teaches a vector for expression of CD20 mAb in chickens comprising a nucleic acid sequence encoding human IgG (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 transgenic chickens contained the CD20 mAb transgene on chromosomes 4 and 33 (page 61, left col. para. 1; Figure 1b – d; page 62, right col. para. 3 – 4). The albumin gene is located on chromosome 4 in chickens as evidenced by NCBI (page 1, Location). Kim teaches the CD20 mAb was strongly expressed in oviduct tissue (page 63, left col. para. 1). Kim teaches stable Fab-binding affinity among batches is an indicator of mAb quality and stability and is required for evaluation of the biological activity of therapeutic antibodies (page 64, left col. para. 2). Kim teaches the binding affinity for Raji cells of the CD20 mAb produced in chickens was not significantly different from that of rituximab (page 64, left col. para. 2). Kim teaches cell apoptosis due to antibody binding is an important feature of therapeutic antibodies and the CD20 mAb produced in chickens has similar Fab-binding affinity and a greater ability to induce apoptosis compared to rituximab (page 64, left col. last para. and right col. para. 1; page 66, right col. last para.). 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). One would have been motivated to combine the teachings of Ballance and Kim in a vector comprising an albumin-CD20 mAb fusion for producing the recombinant mAb in chickens for treating leukemias as Ballance teaches the fusion proteins may be useful for the treatment of hematopoietic related disorders such as leukemia and non-Hodgkin’s lymphoma and Kim teaches the CD20 mAb and 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.
Sharma teaches integration of human Factor IX gene at the mouse albumin locus in vivo where the mice exhibited high circulating human factor IX levels and stable expression levels were observed beyond 1 year (Figure 1; page 1780, left col. last para. and right col. para. 1). Sharma teaches albumin was chosen as the genomic safe harbor because of its very high expression level and the tractability of liver for gene delivery and in vivo editing relative to other tissues (page 1777, right col. para. 3). Sharma teaches the albumin gene structure is well suited for transgene targeting into intronic sequences because its first exon encodes a secretory peptide that is cleaved from the final protein product (page 1777, right col. para. 3). Sharma teaches a typical genome editing approach is to target the disease locus itself; however, the proportion of alleles successfully edited may not express sufficient levels of protein to alleviate the disease phenotype (page 1777, right col. para. 2). Sharma teaches integration into a locus with high transcriptional activity (safe harbor) would address this limitation and provide a versatile platform for expressing various proteins, substituting the donor for each respective therapeutic transgene (page 1777, left col. para. 2).
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 human albumin and an antibody with the teachings of Kim regarding a vector encoding CD20 antibody containing human IgG to produce transgenic chickens expressing CD20 mAb where the transgene was found on chromosomes 4 and 33 with the teachings of Sharma regarding the albumin locus is a genomic safe harbor because of its very high expression level and it is well suited for transgene targeting to arrive at the claimed vector wherein the hepatocyte specific expressed gene is chicken albumin and the gene encoding a target protein is CD20 mAb that contains human IgG and an Fc region and chicken albumin does not include a stop codon. One would have been motivated to combine the teachings of Ballance, Kim, and Sharma in a vector to produce high levels of albumin-CD20 mAb fusion in transgenic chickens and transgenic chicken eggs for treating leukemia as Ballance teaches the fusion proteins may be useful for the treatment of hematopoietic related disorders such as leukemia and non-Hodgkin’s lymphoma and Ballance teaches an embodiment of administration of HA fusion proteins to an animal including a chicken to produce increased quantities of one or more antibodies including IgG 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 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 and Sharma teaches albumin was chosen as the genomic safe harbor because of its very high expression level and the tractability of liver for gene delivery and Sharma teaches the albumin gene structure is well suited for transgene targeting into intronic sequences because its first exon encodes a secretory peptide that is cleaved from the final protein product. One would have a reasonable expectation of success in combining the teachings as Kim teaches the transgene was located on chromosome 4, which is the chromosome chicken albumin is located and Kim teaches the transgenic chicken bioreactor allows post-translational modifications in Abs with superior Fc-effector functions and these characteristics were maintained in successive generations and Kim teaches this germline transgenic chicken bioreactor system is suitable for the production of anti-cancer antibodies.
22. Claim(s) 7 – 12 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 Kim (Kim, Young Min, et al. Biomaterials 167 (2018): 58-68.), hereinafter Kim as evidenced by NCBI (ALB albumin [Gallus gallus (chicken)], NCBI, https://www.ncbi.nlm.nih.gov/gene/396197; Accessed 04/27/2025) in view of Sharma (Sharma, Rajiv, et al. Blood, The Journal of the American Society of Hematology 126.15 (2015): 1777-1784.), hereinafter Sharma as applied to claims 1 – 6 above, and further in view of Patterson (Patterson, James T., et al. Bioconjugate chemistry 27.10 (2016): 2271-2275.), hereinafter Patterson in view of Chng (Chng, Jake, et al. MAbs. Vol. 7. No. 2. Taylor & Francis, 2015), hereinafter Chng in view of Hache (Haché RJ, et. al. J Biol Chem. 1983 Apr 10;258(7):4556-64), hereinafter Hache.
Ballance anticipates claims 1 – 4 as set forth above and Ballance in view of Kim make obvious the limitations of claims 5 and 6 as set forth above.
Regarding claim 10, Kim teaches the lysozyme signal peptide sequence is upstream of the sequence encoding the mAb (page 59, right col. para. 3). Kim does not teach a gene encoding a 2A peptide or that the nucleotide sequence encoding the lysozyme signal peptide is downstream of a 2A peptide. However, Kim teaches the mAbs are successfully deposited in the chicken body and are secreted into the egg white (page 63, left col. para. 2).
Regarding claim 11, Sharma teaches albumin is fused to the N-terminus of the human gene in Figure 1A. Sharma does not teach genes encoding a 2A peptide, or secretory signal peptide.
Regarding claim 12, Sharma teaches the albumin gene structure is well suited for transgene targeting into intronic sequences because its first exon encodes a secretory peptide that is cleaved from the final protein product (page 1777, right col. last para.). Sharma teaches in Figure 1A that albumin exon 1 is fused to the human gene. Sharma teaches one of the main advantages of the targeting strategy is that it allows production of any secretable protein without the need to change the nuclease used for making the transgenic animal (page 1780, right col. last para.). Sharma teaches the liver can secrete large amounts of protein into the blood (page 1782, left col. para. 2). Sharma teaches the fusion resulted in the secretion of protein in an active form (page 1782, left col. para. 2). Sharma does not teach SEQ ID NO: 1.
Ballance, Kim, and Sharma do not teach the vector further comprises “a gene encoding a 2A peptide between the hepatocyte-specific expressed gene and a gene encoding a target protein” of claim 7 or “the 2A peptide consists of 10 to 22 amino acid sequences” of claim 8, or “the 2A peptide” is T2A of claim 9 or the secretory signal peptide is downstream of the gene encoding the 2A peptide of claim 10 or the order of the genes in the vector of claim 11 or the secretory signal peptide amino acid sequence is SEQ ID NO: 1 of claim 12. However, Kim teaches the mAb produced by transgenic chickens has superior Fc-effector functions and ADC activity due to the N-glycosylation pattern (page 67, left col. para. 2 – 3).
Patterson teaches a vector encoding albumin fused to the mAb trastuzumab and chemical conjugation of albumin to trastuzumab (page S5, para. 2; Abstract). Patterson teaches a marginal decrease in binding by the albumin-Ab fusion was noted and that the fusion protein may potentially occlude important interactions depending on fusion orientation (page 2272, left col. para. 2). Patterson does not teach “a gene encoding a 2A peptide between the hepatocyte-specific expressed gene and a gene encoding a target protein” of claim 7 or “the 2A peptide consists of 10 to 22 amino acid sequences” of claim 8, or “the 2A peptide” is T2A of claim 9. One would have been motivated to combine the teachings of Ballance, Kim, and Patterson to remove the albumin fusion to maintain the superior functioning of the mAb produced in transgenic chickens because Patterson teaches the albumin-Ab fusion may potentially occlude important interactions depending on fusion orientation.
Regarding claims 7 – 9, Chng teaches a vector encoding a mAb 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 F2A, E2A, P2A, and T2A have been widely used in biomedical research (page 404, left col. para. 3). Chng teaches T2A exhibited the highest cleavage efficiency (Abstract). One would have been motivated to combine the teachings of Ballance, Kim, Patterson, and Chng to include a nucleic acid encoding a 2A peptide between the chicken albumin gene and the nucleic acid encoding the mAb to produce a mAb without albumin fused in vivo because Patterson teaches the albumin-Ab fusion may potentially occlude important interactions depending on fusion orientation and Chng teaches 2A linked genes are translated in one open reading frame and self-cleavage occurs co-translationally.
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).
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 human albumin and an antibody with the teachings of Kim regarding a vector encoding CD20 antibody containing human IgG and a secretory signal peptide to produce transgenic chickens expressing CD20 mAb in the body and eggs where the transgene was found on chromosomes 4 and 33 with the teachings of Sharma regarding a fusion of the first exon of albumin that encodes a secretory peptide with a human gene for transgenic expression of the human gene with the teachings of Patterson regarding albumin fused to mAbs could affect important interactions with the teachings of Chng regarding 2A linked genes are cleaved co-translationally with the teachings of Hache regarding the sequence of the signal peptide sequence of the first exon of chicken albumin to arrive at the claimed vector further comprising a gene encoding a 2A peptide between the hepatocyte-specific expressed gene and the gene encoding the target protein wherein vector is configured in the order the hepatocyte-specific expressed gene-the gene encoding a 2A peptide-the gene encoding a secretory signal peptide-the gene encoding the antibody. One would have been motivated to combine the teachings of Ballance, Kim, Sharma, Patterson, Chng, and Hache in a vector to produce high levels of secreted CD20 mAb without albumin fusion in transgenic chickens and transgenic chicken eggs for treating leukemia as 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 Patterson teaches the albumin-Ab fusion may potentially occlude important interactions depending on fusion orientation. One would have a reasonable expectation of success in combining the teachings as Chng teaches self-cleavage of the 2A linked genes occurs co-translationally and Kim teaches the transgenic chicken bioreactor allows post-translational modifications in Abs with superior Fc-effector functions and these characteristics were maintained in successive generations and Kim teaches this germline transgenic chicken bioreactor system is suitable for the production of anti-cancer antibodies.
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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