Prosecution Insights
Last updated: April 19, 2026
Application No. 18/273,891

CELL STRAIN FOR PRODUCING BIOSIMILAR DRUG OF USTEKINUMAB AND PRODUCTION METHOD THEREFOR

Non-Final OA §103§112
Filed
Jul 24, 2023
Examiner
VIJAYARAGHAVAN, JAGAMYA NMN
Art Unit
1633
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Qyuns Therapeutics Co. Ltd.
OA Round
1 (Non-Final)
70%
Grant Probability
Favorable
1-2
OA Rounds
3y 9m
To Grant
99%
With Interview

Examiner Intelligence

Grants 70% — above average
70%
Career Allow Rate
19 granted / 27 resolved
+10.4% vs TC avg
Strong +35% interview lift
Without
With
+34.7%
Interview Lift
resolved cases with interview
Typical timeline
3y 9m
Avg Prosecution
52 currently pending
Career history
79
Total Applications
across all art units

Statute-Specific Performance

§101
5.3%
-34.7% vs TC avg
§103
32.0%
-8.0% vs TC avg
§102
16.5%
-23.5% vs TC avg
§112
32.9%
-7.1% vs TC avg
Black line = Tech Center average estimate • Based on career data from 27 resolved cases

Office Action

§103 §112
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 . Priority Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. Acknowledgment is made of applicants' claim for foreign priority to Chinese applications CN 202110099804.1 filed on 01/25/2021. It is noted, however, that applicant has not filed a certified copy of the CN202110099804.1 application as required by 37 CFR 1.55. Information Disclosure Statement The information disclosure statements (IDS) submitted on 09/30/2024 and 08/01/2023 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner. Status of Claims Claims 1-8 are pending and under exam. Claim Interpretation The terms “substantially free of sialylated components” in claim 2 is not given explicit definition in the specification. However [0052] of the specification indicated that “sialylated components of Ustekinumab is between 11.87% and 25.56%, while QX001S expressed by the CHO-S cell line is substantially free of sialylated components.” As such the claim is interpreted to mean that the sialylated components are lower than 11.87%. 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. Claims 3-4 and 6 rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as failing to set forth 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. Claims 3-4 and 6 require a biosimilar drug of Ustekinumab. The term biosimilar is neither expressly defined in the specification, nor does the specification set forth structural, functional or regulatory criteria by which one of ordinary skill in the art could determine whether a given antibody falls within the scope of the claims. As such the metes and bounds of this claim are indefinite. 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. The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action. 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. Claims 1-8 are rejected under 35 U.S.C. 103 as being unpatentable over Pippig et al (WO2018024770A1; Published Feb 8, 2018; hereinafter "Pippig;" See IDS of 08/01/2023), in view of You et al (Appl Microbiol Biotechnol. 2018 Jul; hereinafter "You;" See PTO-892). Regarding claims 1 and 3-4: Pippig taught a method of producing recombinant Ustekinumab antibody drug product, which is a fully humanized monoclonal antibody against a p40 subunit shared by human IL-12 and human IL-23; a heavy chain amino acid sequence of the fully humanized monoclonal antibody comprising instant SEQ ID NO:1, and a light chain amino acid sequence of the fully humanized monoclonal antibody comprising instant SEQ ID NO:3. (See Pippig claim 4). It is also noted that Pippig disclosed that the drug product has heavy chain sequence according to SEQ ID NO: 1 which is 100% identical to instant SEQ ID NO: 1 (See alignment below). Additionally, Pippig disclosed that the light chain has a sequence according to SEQ ID NO: 2, which is 100% identical to instant SEQ ID NO: 3 (See alignment below). It is noted that Pippig did not teach “an expression plasmid that expresses the fully humanized monoclonal antibody against the p40 subunit shared by human IL-12 and human IL-23; the expression plasmid comprises a nucleotide sequence encoding the heavy chain amino acid sequence of the fully humanized monoclonal antibody shown as SEQ ID NO:2, and a nucleotide sequence encoding the light chain amino acid sequence of the fully humanized monoclonal antibody shown as SEQ ID NO:4” as required by the claim. However, Pippig taught “culturing Chinese Hamster Ovary (CHO) host cells, genetically modified to express the heavy chain and the light chain of Ustekinumab, in a suitable culture medium under conditions that allow the cells to express the heavy chain and the light chain and to form the recombinant Ustekinumab antibody” (See Pippig Claim 1a). CHO, genetically modified to express the claimed drug product is interpreted to read on expression plasmid that expresses the fully humanized monoclonal antibody against the p40 subunit shared by human IL-12 and human IL-23. It is noted that the nucleic acid sequence claimed in the instant application: SEQ ID NO: 2 encoding a heavy chain and SEQ ID NO: 4 encoding the light chain was not taught or suggested by Pippig. However, You was directed to producing antibodies with high yield and quality is necessary for clinical applications of antibodies. (See You Abstract). You taught that the yield can be doubled by codon optimization and increased by 50% with the presence of untranslated regions (UTR) specifically for expression in CHO cells. You further taught that the combination of UTR with optimal codon and signal peptide to form an expression vector can result in yield improvement of 150% and correct N-terminal sequences. As such it was known that codon optimization and nucleotide sequence optimization strategies can improve recombinant antibody expression in CHO cells in view of You. It would have been obvious to a person of ordinary skill in the art to optimize the nucleotide sequences encoding the heavy and light chains of an antibody such as Ustekinumab for enhanced expression in CHO cells by modifying codons or other features with a reasonable expectation of success of improving expression without altering the encoded amino acid sequence. It is also noted that codon optimization represents a finite number of predictable solutions and selection of one optimized nucleotide sequence from among synonymous alternatives would have been routine. Query 1 EVQLVQSGAEVKKPGESLKISCKGSGYSFTTYWLGWVRQMPGKGLDWIGIMSPVDSDIRY 60 EVQLVQSGAEVKKPGESLKISCKGSGYSFTTYWLGWVRQMPGKGLDWIGIMSPVDSDIRY Sbjct 1 EVQLVQSGAEVKKPGESLKISCKGSGYSFTTYWLGWVRQMPGKGLDWIGIMSPVDSDIRY 60 Query 61 SPSFQGQVTMSVDKSITTAYLQWNSLKASDTAMYYCARRRPGQGYFDFWGQGTLVTVSSS 120 SPSFQGQVTMSVDKSITTAYLQWNSLKASDTAMYYCARRRPGQGYFDFWGQGTLVTVSSS Sbjct 61 SPSFQGQVTMSVDKSITTAYLQWNSLKASDTAMYYCARRRPGQGYFDFWGQGTLVTVSSS 120 Query 121 STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG 180 STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG Sbjct 121 STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG 180 Query 181 LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGP 240 LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGP Sbjct 181 LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGP 240 Query 241 SVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNS 300 SVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNS Sbjct 241 SVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNS 300 Query 301 TYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDEL 360 TYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDEL Sbjct 301 TYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDEL 360 Query 361 TKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQ 420 TKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQ Sbjct 361 TKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQ 420 Query 421 QGNVFSCSVMHEALHNHYTQKSLSLSPGK 449 QGNVFSCSVMHEALHNHYTQKSLSLSPGK Sbjct 421 QGNVFSCSVMHEALHNHYTQKSLSLSPGK 449 100% identity between SEQ ID NO: 1 of instant application to SEQ ID NO: 1 of WO2018024770A1 Query 1 DRVTITCRASQGISSWLAWYQQKPEKAPKSLIYAASSLQSGVPSRFSGSGSGTDFTLTIS 60 DRVTITCRASQGISSWLAWYQQKPEKAPKSLIYAASSLQSGVPSRFSGSGSGTDFTLTIS Sbjct 17 DRVTITCRASQGISSWLAWYQQKPEKAPKSLIYAASSLQSGVPSRFSGSGSGTDFTLTIS 76 Query 61 SLQPEDFATYYCQQYNIYPYTFGQGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLL 120 SLQPEDFATYYCQQYNIYPYTFGQGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLL Sbjct 77 SLQPEDFATYYCQQYNIYPYTFGQGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLL 136 Query 121 NNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEV 180 NNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEV Sbjct 137 NNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEV 196 Query 181 THQGLSSPVTKSFNRGEC 198 THQGLSSPVTKSFNRGEC Sbjct 197 THQGLSSPVTKSFNRGEC 214 100% identity between SEQ ID NO: 3 of instant application to SEQ ID NO: 2 of WO2018024770A1 Regarding claim 2 and 5: Claim 5 of Pippig indicated that the method of production of Ustekinumab has a sialic acid content of <5%; this reads on substantially free of sialylation. Regarding claims 7-8: The teachings of Pippig in view of You are set forth above. Pippig discloses Ustekinumab or Ustekinumab biosimilar antibodies which bind to p40 subunit of IL-12 and IL-23 using recombinant expression in mammalian cells, including CHO cells. Pippig taught expression constructs comprising nucleotide sequences encoding antibody heavy and light chains, expression vectors containing such sequences and host cells comprising the expression vectors for producing the antibody. While the exact SEQ ID NOs: 2 and 3 are not disclosed in Pippig, You taught that optimization of antibody sequences for CHO cell expression increases antibody expression. You used expression vectors for expressing antibody heavy and light chains. As such the teachings of Pippig in view of You taught that optimized nucleotide sequences encoding a given antibody amino acid sequence can be routinely incorporated into host cells to achieve improved expression with predictable results. Conclusion No claim is allowed. No claim is free art. Any inquiry concerning this communication or earlier communications from the examiner should be directed to JAGAMYA VIJAYARAGHAVAN whose telephone number is (703)756-5934. The examiner can normally be reached 9:00a-5:00p. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Christopher M. Babic can be reached at 571-272-8507. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /JAGAMYA NMN VIJAYARAGHAVAN/ Examiner, Art Unit 1633 /EVELYN Y PYLA/Primary Examiner, Art Unit 1633
Read full office action

Prosecution Timeline

Jul 24, 2023
Application Filed
Jan 08, 2026
Non-Final Rejection — §103, §112 (current)

Precedent Cases

Applications granted by this same examiner with similar technology

Patent 12590136
ENGINEERED T CELLS
2y 5m to grant Granted Mar 31, 2026
Patent 12570987
SYNTHETICALLY EVOLVED DNA CONSTRUCTS FOR REGULATING SIGNAL PEPTIDE PERFORMANCE AS WELL AS VECTORS, HOST CELLS AND RECOMBINANT PROTEINS THEREOF
2y 5m to grant Granted Mar 10, 2026
Patent 12564607
CELL POPULATION COMPRISING MESENCHYMAL CELLS, PHARMACEUTICAL COMPOSITION COMPRISING THE SAME, AND METHOD FOR PRODUCING THE SAME
2y 5m to grant Granted Mar 03, 2026
Patent 12540335
COMPOSITIONS AND METHODS FOR THE TREATMENT OF METABOLIC LIVER DISORDERS
2y 5m to grant Granted Feb 03, 2026
Patent 12527868
MESODERMAL KILLER (MK) CELL
2y 5m to grant Granted Jan 20, 2026
Study what changed to get past this examiner. Based on 5 most recent grants.

AI Strategy Recommendation

Get an AI-powered prosecution strategy using examiner precedents, rejection analysis, and claim mapping.
Powered by AI — typically takes 5-10 seconds

Prosecution Projections

1-2
Expected OA Rounds
70%
Grant Probability
99%
With Interview (+34.7%)
3y 9m
Median Time to Grant
Low
PTA Risk
Based on 27 resolved cases by this examiner. Grant probability derived from career allow rate.

Sign in with your work email

Enter your email to receive a magic link. No password needed.

Personal email addresses (Gmail, Yahoo, etc.) are not accepted.

Free tier: 3 strategy analyses per month