Prosecution Insights
Last updated: April 19, 2026
Application No. 18/004,517

ENHANCING IMMUNE RESPONSES THROUGH TARGETED ANTIGEN EXPRESSION

Non-Final OA §102§103§112
Filed
Jan 06, 2023
Examiner
CHEN, STACY BROWN
Art Unit
1672
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Phagenova Bio Inc.
OA Round
1 (Non-Final)
66%
Grant Probability
Favorable
1-2
OA Rounds
3y 2m
To Grant
99%
With Interview

Examiner Intelligence

Grants 66% — above average
66%
Career Allow Rate
605 granted / 914 resolved
+6.2% vs TC avg
Strong +40% interview lift
Without
With
+40.3%
Interview Lift
resolved cases with interview
Typical timeline
3y 2m
Avg Prosecution
40 currently pending
Career history
954
Total Applications
across all art units

Statute-Specific Performance

§101
4.9%
-35.1% vs TC avg
§103
29.3%
-10.7% vs TC avg
§102
17.3%
-22.7% vs TC avg
§112
30.8%
-9.2% vs TC avg
Black line = Tech Center average estimate • Based on career data from 914 resolved cases

Office Action

§102 §103 §112
DETAILED ACTION Election/Restrictions Applicant’s election without traverse of Group I, claims 1-26, species c and species SEQ ID NO: 4 in the reply filed on December 22, 2025 is acknowledged. Further election was required in the election of species requirement dated October 22, 2025, from claims 21-23, but no elections were made in the response of December 22, 2025. In a phone call on February 9, 2026, Applicant elected coronavirus S protein from claim 21, SEQ ID NO: 85 from claim 22, and SEQ ID NO: 84 from claim 23. Specification The disclosure is objected to because of the following informalities: The descriptions of Figures 12 and 13 (see pages 9-10 of the specification) contain amino acid sequences that need to be referenced by a sequence identifier (SEQ ID NO). The figures themselves contain the sequence identifiers, however, the descriptions of the figures also need to recite the sequence identifiers when the amino acid sequences are spelled out. Appropriate correction is required. Claims Summary Claim 1 is directed to an immunogenic composition comprising an effective amount of a therapeutic engineered phage and a pharmaceutically acceptable carrier, wherein the phage comprises one or more fusion polypeptides comprising an antigenic polypeptide and a phage coat protein. The phage coat protein comprises at least one of pIII, pVI, pVII, pVIII, rpVIII and pIX (claim 3). The phage further comprises a fusion polypeptide comprising a tissue-targeting polypeptide and a phage coat protein (claim 2). The tissue-targeting polypeptide targets lung tissue (claim 10), the polypeptide comprising SEQ ID NO: 4 (CAKSMGDIVC). The phage is an AAVP and further comprises a viral gene (claim 20), specifically a coronavirus S protein (elected species, claim 21). The S protein comprises SEQ ID NO: 85 (elected species, claim 22). The viral gene encoding the S protein comprises nucleotide sequence SEQ ID NO: 84 (elected species, claim 23). The phage further comprises a fusion polypeptide comprising an aerosol delivery polypeptide that targets lung tissue and acts as a transcytosis domain and a phage coat protein (claim 24). The aerosol delivery polypeptide comprises SEQ ID NO: 4 (claim 25). The aerosol delivery polypeptide is encoded by SEQ ID NO: 81 (claim 26). Claim Rejections - 35 USC § 112 The following is a quotation of the first paragraph of 35 U.S.C. 112(a): (a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention. The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112: The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention. Claim 24 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. Claim 24 is directed to an immunogenic composition encompassing a large genus of aerosol delivery polypeptides that target lung tissue and act as a transcytosis domain. To provide adequate written description and evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof. In this case, the specification has provided one examples of an aerosol delivery polypeptide that targets lung tissue and act as a transcytosis domain, i.e., SEQ ID NO: 4. This is one structure associated with the claimed function. No other structures appear to have been provided. The one species does not represent the genus. No structure/function correlation appears to have been provided such that one would be able to find other species of the genus. Given that SEQ ID NO: 4 was identified as having the claimed functions through a random peptide library (see Staquicini et al., 2021, Med, 2:321-342) there is no indication of any other structure having the claimed ability to act as a transcytosis domain and aerosol delivery polypeptide. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus. Claim Rejections - 35 USC § 102 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. Claim 1 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by Bachmann et al. (US 2008/0095738 A1, “Bachmann”, cited in the IDS filed 01/06/2023). Bachmann discloses compositions comprising RNA-bacteriophage VLPs comprising a coat protein fused to an antigen, in combination with a pharmaceutically acceptable carrier, for use in immunization (see paragraphs [0021]-[0023], and [0104]). Therefore, claim 1 is anticipated by the prior art. Claims 1-3 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Chen et al. (Chemistry & Biology, 2004, 11:1081-1091, “Chen”). The claims are summarized above and correlated with the teachings of the prior art in bold font. Chen discloses a bifunctional ligand display system for receptor targeting (see abstract). Chen’s engineered phage displays a tissue-targeting ligand from coat protein pIII (a double cyclic peptide), and a cyclic peptide comprising a streptavidin binding sequence from coat protein pVIII (claims 1-3, aspects of engineered phage, antigenic polypeptide, tissue-targeting polypeptide and coat proteins). Thus, Chen’s phage comprises two types of fusion polypeptides: antigen fused to coat protein pIII, and a streptavidin binding sequence fused to coat protein pVIII (claims 1 and 2, aspect of fusion polypeptides). Chen teaches that the phage can be used to deliver therapeutics (abstract) (claim 1, aspect of therapeutic phage). Phage are suspended in PBS, which is a pharmaceutically acceptable carrier (claim 1, aspect of pharmaceutically acceptable carrier). The composition is expected to be immunogenic on some level since it is foreign to its recipient (see pages 1087-1088, bridging paragraph) (claim 1, aspect of immunogenic composition). Therefore, the claimed embodiments are anticipated by the prior art. 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. 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 1-3 and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Hajitou et al. (Nature Protocols, 2007, 2(3):523-531, “Hajitou”) in view of Chen et al. (Chemistry & Biology, 2004, 11:1081-1091, “Chen”). Hajitou discloses a targeted phage that is comprised of a ligand-directed, chimeric adeno-associated virus and phage (AAVP) particles (see abstract) (claim 1, aspect of engineered phage). A tissue-targeting ligand is displayed on the phage coat protein, pIII (see abstract and page 523, right column) (claims 2 and 3, aspect of fusion polypeptide comprising a tissue-targeting ligand fused to a pIII coat protein). Hajitou discloses lung tissue-specific transduction using a homing peptide that binds membrane dipeptidase in lung endothelium (see page 524, right column) (claim 10, aspect of targeting lung tissue). The targeted phage comprises a recombinant AAV (comprising a therapeutic transgene) that is inserted into an intergenomic region of the phage genome. The therapeutic transgene is expressed by the phage upon internalization in a target cell (see Figure 1). Hajitou discloses a composition of phage in PBS, a pharmaceutically acceptable carrier (see page 527, Box 2, last paragraph) (claim 1, aspect of pharmaceutically acceptable carrier). The composition is immunogenic (see page 529, Box 3) (claim 1, aspect of immunogenic). Hajitou does not disclose the presence of a second fusion polypeptide on the AAVP, wherein the polypeptide comprises an antigenic polypeptide fused to a coat protein of the phage. However, it would have been obvious to have engineered Hajitou’s phage to have a functional ligand display system having a second fusion polypeptide on the AAVP, with a reasonable expectation of success. Chen discloses a bifunctional ligand display system for receptor targeting that delivers a therapeutic agent (see abstract). Chen’s engineered phage displays a tissue-targeting ligand from coat protein pIII (a double cyclic peptide), and a cyclic peptide comprising a streptavidin binding sequence from coat protein pVIII. Thus, Chen’s phage comprises two types of fusion polypeptides: antigen fused to coat protein pIII, and a streptavidin binding sequence fused to coat protein pVIII. One would have been motivated to modify Hajitou’s phage to include a second ligand fused to a coat protein to improve receptor targeting without the need for chemical conjugation or coupling of adaptor proteins (see Chen, abstract and page 1, left column, first full paragraph) (claim 1, aspect of an antigenic polypeptide fused to a coat protein of the phage). Therefore, the claimed embodiments would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. Claims 20 and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Hajitou et al. (Nature Protocols, 2007, 2(3):523-531, “Hajitou”) in view of Chen et al. (Chemistry & Biology, 2004, 11:1081-1091, “Chen”) as applied to claim 1 above, and further in view of Baric et al. (US 2016/0238601, “Baric”). The claims are directed to embodiments wherein the engineered phage is an AAVP and further comprises a viral gene, specifically, a coronavirus S protein. The teachings of Hajitou and Chen are outlined above, neither of which suggest a therapeutic gene that encodes a coronavirus S protein. However, it would have been obvious to have expressed a coronavirus S protein from the engineered phage of Hajitou/Chen, with a reasonable expectation of success. Baric discloses coronavirus S proteins for therapeutic administration (see paragraph [0008]), noting that proteins can be expressed/delivered via any known viral vector (see paragraph [0078]). One would have been motivated to use the phage of Hajitou/Chen to express Baric’s coronavirus S protein, given that it would be targeted to lung tissue, where coronavirus replicates as a respiratory pathogen (see paragraph [0004]). Therefore, the claimed embodiments would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. Conclusion No claim is allowed. Claims 11, 22, 23, 25 and 26 are objected to for being dependent on a rejected claim. SEQ ID NO: 4, 81, 84 and 85 are free of the prior art of record. Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. 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. Any inquiry concerning this communication or earlier communications from the examiner should be directed to Stacy B. Chen whose telephone number is 571-272-0896. The examiner can normally be reached on M-F (7:00-4:30). If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Thomas Visone, can be reached on 571-270-0684. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. /STACY B CHEN/Primary Examiner, Art Unit 1672
Read full office action

Prosecution Timeline

Jan 06, 2023
Application Filed
May 19, 2023
Response after Non-Final Action
Jan 13, 2026
Examiner Interview (Telephonic)
Feb 02, 2026
Examiner Interview Summary
Feb 27, 2026
Non-Final Rejection — §102, §103, §112 (current)

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

1-2
Expected OA Rounds
66%
Grant Probability
99%
With Interview (+40.3%)
3y 2m
Median Time to Grant
Low
PTA Risk
Based on 914 resolved cases by this examiner. Grant probability derived from career allow rate.

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