Prosecution Insights
Last updated: October 02, 2026
Application No. 18/193,033

FLUOROARABINO NUCLEIC ACID (FANA) APTAMERS THAT BIND SARS-2 RECEPTOR BINDING DOMAIN AND BLOCK BINDING TO THE ACE2 CELLULAR RECEPTOR

Non-Final OA §102§103§112
Filed
Mar 30, 2023
Priority
Mar 31, 2022 — provisional 63/362,325
Examiner
BRETZ, COREY LANE
Art Unit
1635
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
University of Maryland, College Park
OA Round
1 (Non-Final)
0%
Grant Probability
At Risk
1-2
OA Rounds
0m
Est. Remaining
0%
With Interview

Examiner Intelligence

Grants only 0% of cases
0%
Career Allowance Rate
0 granted / 3 resolved
-60.0% vs TC avg
Minimal +0% lift
Without
With
+0.0%
Interview Lift
resolved cases with interview
Typical timeline
2y 7m
Avg Prosecution
53 currently pending
Career history
36
Total Applications
across all art units

Statute-Specific Performance

§101
5.7%
-34.3% vs TC avg
§103
29.9%
-10.1% vs TC avg
§102
13.3%
-26.7% vs TC avg
§112
18.6%
-21.4% vs TC avg
Black line = Tech Center average estimate • Based on career data from 3 resolved cases

Office Action

§102 §103 §112
DETAILED ACTION 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 . Election/Restrictions Applicant’s election without traverse of Group 1 claims 1-16 and 18 in the reply filed on 11/24/2025 is acknowledged. Claims 17 and 19-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 11/24/2025. Status of Claims Claims 1-20 are pending. Claims 17 and 19-20 are withdrawn. Claims 1-16 and 18 are under examination. 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. Information Disclosure Statement The information disclosure statements (IDSs) submitted on 07/17/2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner. Nucleotide and/or Amino Acid Sequence Disclosures Summary of Requirements for Patent Applications Filed On Or After July 1, 2022, That Have Sequence Disclosures 37 CFR 1.831(a) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.831(b) must contain a “Sequence Listing XML”, as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.831-1.835. This “Sequence Listing XML” part of the disclosure may be submitted: 1. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter “Legal Framework”) in XML format, together with an incorporation by reference statement of the material in the XML file in a separate paragraph of the specification (an incorporation by reference paragraph) as required by 37 CFR 1.835(a)(2) or 1.835(b)(2) identifying: a. the name of the XML file b. the date of creation; and c. the size of the XML file in bytes; or 2. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation by reference statement of the material in the XML format according to 37 CFR 1.52(e)(8) and 37 CFR 1.835(a)(2) or 1.835(b)(2) in a separate paragraph of the specification identifying: a. the name of the XML file; b. the date of creation; and c. the size of the XML file in bytes. SPECIFIC DEFICIENCIES AND THE REQUIRED RESPONSE TO THIS NOTICE ARE AS FOLLOWS: Specific deficiency - Sequences appearing in the drawings are not identified by sequence identifiers in accordance with 37 CFR 1.831(c). Sequence identifiers for sequences (i.e., “SEQ ID NO:X” or the like) must appear either in the drawings or in the Brief Description of the Drawings. Required response – Applicant must provide: Amended drawings in accordance with 37 CFR 1.121(d) inserting the required sequence identifiers; AND/OR A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required sequence identifiers (i.e., “SEQ ID NO:X” or the like) into the Brief Description of the Drawings, consisting of: • A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version); • A copy of the amended specification without markings (clean version); and • A statement that the substitute specification contains no new matter. Figure 2A contains polynucleotide sequences that are more than ten contiguous nucleotides without an accompanying SEQ ID NO either in the figure itself or in the corresponding brief description of the figure. 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. Claims 1-2, 4, 6, 8-11, 13-16, and 18 are 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. Adequate written description support for a claimed genus may be provided by describing sufficient identifying characteristics, describing a representative number of species, actual reduction to practice, disclosure of drawings or structural chemical formulas, complete or partial structure, physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure and any working examples, method of making the claimed invention, level of skill and knowledge in the art as well as predictability in the art are other determinants that are used to analyze whether applicants had possession of the claimed genus. The present specification fails to meet these requirements for the following reasons. REGARDING CLAIMS 1, 8-10, 14-16, and 18 Claim 1 is directed to a broad genus of FANA aptamers functionally defined as aptamers that bind either the SARS-CoV-2 receptor binding domain (RBD) or the S1 domain of SARS-CoV-2 and thereby block binding of SARS-CoV-2 to ACE2 expressed on the surface of a host cell. Claims 8-10, 14-16, and 18 depend from or otherwise further recite subject matter based upon the FANA aptamer of claim 1 and therefore encompass the same broad genus of functionally defined FANA aptamers. The specification, however, does not describe this genus with sufficient identifying characteristics, representative species, or a disclosed structure-function correlation to reasonably convey possession of the full scope of the claimed genus as of the filing date. Although the specification describes a number of particular FANA aptamer sequences, including FANA-R8-3, FANA-R8-5, FANA-R8-7, FANA-R8-9, FANA-R8-15, FANA-R8-17, and FANA-R8-22 (see [0007] and table 1), the specification does not establish that these particular sequences are representative of the full scope of FANA aptamers encompassed by claim 1. The specification itself explains that the RBD was selected as the target because aptamers that directly block S protein-ACE2 interactions were desired, rather than aptamers that bind to other portions of the S protein see [0103]. The specification further states that the RBD constitutes only a portion of the S1 subunit, see [0103]. Thus, the disclosure of aptamers selected against the RBD does not, without more, establish possession of the entire genus of FANA aptamers that bind any portion of S1 and possess the claimed ACE2-blocking function. The specification demonstrates substantial functional variation among aptamers in Table 1. The specification reports that the seven tested FANA sequences exhibited different apparent equilibrium dissociation constants for the RBD and S1 proteins. For example, FANA-R8-3 exhibited a reported in table 1 RBD KDapp, FANA-R8-3 exhibited 68.1 nM, FANA-R8-5 exhibited 26.4 nM, FANA-R8-7 exhibited 62.8 nM, FANA-R8-9 exhibited 23.5 nM, FANA-R8-15 exhibited 43.3 nM, FANA-R8-17 exhibited 29.5 nM, and FANA-R8-22 exhibited 21.3 nM. The specification further reports that FANA-R8-9, FANA-R8-22, and FANA-R8-17 differed in their ability to block ACE2 binding, with FANA-R8-17 being approximately threefold weaker than FANA-R8-9 in the reported ACE2-blocking assay, see [0106]. Thus, the disclosed sequences do not exhibit a uniform or predictable functional behavior merely by virtue of being FANA aptamers obtained from the same selection. The specification further expressly acknowledges the unpredictability associated with producing aptamers, stating that making aptamers is a “hit-or-miss” proposition and that there are no guarantees that aptamers having improved binding affinity can be found, see [0110]. The specification additionally recognizes that aptamers may bind the larger S1 domain without necessarily exhibiting the same RBD-binding characteristics, see [0110]. In particular, the specification discusses a previously reported aptamer that bound S1 but not strongly to the RBD, and further notes that an aptamer binding S1 outside the RBD can nevertheless exhibit antiviral activity without directly blocking binding to ACE2, see [0111]. Accordingly, the specification itself does not establish a predictable relationship between the sequence of an arbitrary FANA aptamer, the portion of S1 to which the aptamer binds, its ability to bind the RBD, and its ability to block ACE2 binding. The state of the art teaches that retention of aptamer activity following sequence variation depends upon the particular nucleotide and structural context of the aptamer. For example, Miyakawa S, et al., (US20100004432A1) explains that nucleotide substitutions may be tolerated when the nucleotide is not involved in direct binding to the target molecule and that replacement of a base pair may retain activity when the overall structure is maintained, see [0055]. However, Miyakawa also teaches that such substitutions depend upon whether the affected nucleotide participates in target binding and whether the alterations change the overall steric structure, and reports experimentally that particular deletions and structural variations can substantially reduce or eliminate activity. Thus, Miyakawa does not establish that sequence identity itself is predictive of retained aptamer function; rather, Miyakawa established that particular structural and functional characteristics to any particular aptamer must be considered in determining whether a sequence variant retains activity. The present specification does not identify the nucleotide positions within the disclosed FANA aptamers that may be varied while retaining RBD or S1 binding and ACE2-blocking activity, does not identify which substitutions are tolerated at those positions, and does not provide a structure-function correlation that would permit the skilled artisan to predict a FANA aptamer having any nucleotide sequence. Rather, the specification provides particular FANA sequences that bind the SARS-CoV-2 RBD and/or S1. The disclosure therefore does not reasonably convey possession of the full scope of claim 1 at the time of filing. Claims 8-10, 14-16, and 18 do not cure this deficiency. Claim 8 merely requires a modification that increases stability, without identifying the structural or sequence characteristics of the aptamers encompassed by claim 1 that would retain the claimed binding and ACE2-blocking functions following such modification. Claim 9 similarly does not provide a structural definition of the claimed aptamer sufficient to overcome the deficiency of claim 1. Claims 10, 14, and 15 merely recite a pharmaceutical composition, intranasal formulation, or nanoparticle association containing the FANA aptamer of claim 1, and claim 16 merely recites use of the FANA aptamer for treatment or prevention of SARS-CoV-2 infection. Claim 18 similarly recites a kit comprising the pharmaceutical composition of claim 10. None of these additional limitations supplies the missing description of the broad genus of FANA aptamers encompassed by claim 1 or establishes a sufficient structure-function correlation for the claimed genus. Accordingly, claims 1, 8-10, 14-16, and 18 lack adequate written description support under 35 U.S.C. 112(a). REGARDING CLAIMS 2, 4, 6, 11, and 13 Claims 2 and 6 recite broad sequence-based genera encompassing FANA aptamers having as little as 90% sequence identity to the specified SEQ ID NOS, while retaining the functional limitations of claim 1. Claim 4 further encompasses corresponding sequence variants of the recited primer regions, and claims 11 and 13 depend from claims 2 and 4, respectively. Although the specification expressly recites sequence-identity ranges extending down to 90%, mere recitation of a percentage identity range does not, by itself, demonstrate possession of every sequence within that range that also possesses the claimed functional characteristics. The specification identifies particular FANA aptamer sequences and reports functional testing of a limited number of those sequences. However, the specification does not identify which nucleotide positions may be substituted while retaining the claimed RBD or S1 binding and ACE2-blocking activity, does not establish a structure-function correlation that would permit prediction of which 90%-identity variants retain those functions, and does not provide a representative number of species spanning the full sequence space encompassed by the claims. This is particularly significant because the claimed genus extends from the specifically disclosed sequences to variants containing potentially numerous substitutions while still being required to perform the claimed biological functions. The state of the art demonstrates that the functional consequences of sequence variation in aptamers depend upon the particular sequence and structural context. For example, Miyakawa S, et al., (US20100004432A1) experimentally evaluated numerous altered forms of an aptamer and reported materially different inhibitory activities among the altered forms. Miyakawa reports in Table 3-1and 3-2 relative activities ranging from 0 to 130 for different altered forms, while Table 3-2 reports activities ranging from 0 to 78 for additional altered forms. The reference further reports that replacement of an internal loop retained activity, deletion of A19 retained activity, deletion of G18 caused a substantial decrease in activity, and deletion of a C-G base pair caused a change in secondary structure and loss of inhibitory activity. See Table 3-1, Table 3-2, and the accompanying discussion. Thus, the reference demonstrates that particular nucleotide and structural alterations can have materially different effects on aptamer activity and that functional equivalence cannot be established merely from the fact that a variant is derived from, or remains substantially similar to, a parent aptamer. Similarly, Levay et al., (Identifying high-affinity aptamer ligands with defined cross-reactivity using high-throughput guided SELEX,” Nucleic Acids Research, 2015, 43(12), e82) reports that individual nucleotide substitutions within an aptamer produced differing effects on target binding, including increased affinity, unchanged affinity, and reduced or disrupted binding, see page e82. The authors further reported that mapping the mutations to predicted secondary structure did not adequately explain the differing effects of the mutations, see figure 4C and page e28. Thus, the prior art supports the conclusion that the functional consequences of individual sequence changes in aptamers depend upon particular nucleotide and structural context. In view of the above, the specification’s disclosure of particular FANA aptamer sequences and a generic statement that sequences having at least 90% identity are contemplated does not reasonably convey possession of the entire genus of 90%-identity variants (much less a fragment thereof as claimed) encompassed by claims 2 and 6 (and dependent claims) that also satisfy the functional limitations of claim 1 from which they depend. The disclosure does not identify the permissible sequence variation throughout the claimed genus or provide an adequate structure-function correlation from which the skilled artisan could reasonably conclude that the full scope of the claimed variants was possessed at the time of filing. Claim 4 additionally encompasses variants of the fixed primer regions having sequence identity extending down to 90%. However, claim 4 depends from claim 2 and therefore retains the broad 90%-identity genus of the FANA aptamer itself in addition to the sequence variation of the primer regions. The additional primer limitation does not provide written description support for the claimed functional variants of the aptamer. Claims 11 and 13 likewise depend from the deficient genera of claims 2 and 4 and therefore are not separately cured by their pharmaceutical-composition limitations. 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. Claims 1-7 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Irani Alves Ferreira-Bravo I, DeStefano JJ. (Xeno-Nucleic Acid (XNA) 2'-Fluoro-Arabino Nucleic Acid (FANA) Aptamers to the Receptor-Binding Domain of SARS-CoV-2 S Protein Block ACE2 Binding. Viruses. 2021 Oct 2;13(10):1983, in IDS, - also published in BioRxiv Jul 14, 2021). Regarding claim 1, Alves teaches a 2'-fluoro-arabinonucleic acid (FANA) aptamer that binds to a SARS-CoV-2 receptor binding domain or S1 domain of SARS-CoV-2 and thereby blocks binding of SARS-CoV-2 to the angiotensin-converting enzyme 2 (ACE2) expressed on the surface of a host cell, see abstract, results, discussion, and figures 1-6 particularly FANA-R8-9. Regarding claims 2-7, Alves teaches the aptamer FANA-R8–9, which has 100% sequence identity to instant SEQ ID NO: 12, see Table 1, figure 2, and alignment below: PNG media_image1.png 210 620 media_image1.png Greyscale Alves further teaches “only the ~40 nt random regions of the ~79 nt aptamers are shown. In the full aptamer, this would be flanked by 5′-AAAAGGTAGTGCTGAATTCG-3′ at the 5′ end and, and 5′-UUCGCUAUCCAGUUGGCCU-3′ at the 3′ end,” see table 1, figure 2, and section 2.2.2. Alignment of each of these 5’ and 3’ flanking sequences align with 100 and 95 percent identity to instant SEQ ID NOs 19 and 20, respectively, see alignments below: PNG media_image2.png 200 620 media_image2.png Greyscale , and PNG media_image3.png 203 628 media_image3.png Greyscale Alves teaches the 40-nucleotide central random regions are flanked at the 5′ end by 20 nucleotides of fixed sequence DNA (5′-AAAAGGTAGTGCTGAATTCG-3′), and at the 3′ end by 19 nucleotides of fixed FANA sequence (5′-UUCGCUAUCCAGUUGGCCU-3’) (i.e., 5′-AAAAGGTAGTGCTGAATTCG(N)40UUCGCUAUCCAGUUGGCCU-3’); thus, Alves teaches the structure of the aptamers represented by instant SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, and 17. When aligning the 5’ fixed, the FANA-R8-9, and the 3’ fixed sequences in this structure as taught by Alves, it produces an aptamer with 100% identity so instant SEQ ID NO: 11, see alignment below: PNG media_image4.png 288 620 media_image4.png Greyscale . 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. Claims 1, 8-10, 14-16, and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Sun M, et al., (Aptamer Blocking Strategy Inhibits SARS-CoV-2 Virus Infection. Angew Chem Int Ed Engl. 2021 Apr 26;60(18):10266-10272, in IDS) in view of Dahma MJ, et al., (US20090131352A1). Regarding claims 1 and 16, Sun teaches “an aptamer blocking strategy by engineering aptamers’ binding to the region on SRBD that directly mediates ACE2 receptor engagement, leading to block SARS‐CoV‐2 infection,” and that “with aptamer selection against SRBD and molecular docking, aptamer CoV2‐6 was identified and applied to prevent, compete with, and substitute ACE2 from binding to SRBD,” see abstract. Sun teaches that “compared to neutralizing antibodies, aptamers show several distinct advantages for SARS‐CoV‐2 treatment,” and that “aptamers with the ability to inhibit SARS‐CoV‐2 infection may provide an effective therapeutic and prophylactic solution to complement existing treatment and protection measures,” see introduction. Sun further teaches that “CoV2‐6C3 aptamer replaced more than 55.91 % ACE2 bound to SRBD, indicating its potential for the treatment of infected patients,” see Aptamer Characterization section. Regarding claim 8, Sun teaches “CoV2‐6 was further shortened and engineered as a circular bivalent aptamer CoV2‐6C3 (cb‐CoV2‐6C3) to improve the stability, affinity, and inhibition efficacy,” and that “cb‐CoV2‐6C3 is stable in serum for more than 12 h and can be stored at room temperature for more than 14 days,” see abstract. Overall, Sun reports “cb‐CoV2‐6C3 binds to SRBD with high affinity (K d=0.13 nM) and blocks authentic SARS‐CoV‐2 virus with an IC50 of 0.42 nM,” see abstract. Regarding claim 9. Sun teaches “circular aptamers are resistant to exonuclease degradation, helping them to retain sequence integrity, even after storage at room temperature for 14 days, incubation with 95 % human plasma for 12 hours, and cell media (containing 10 % FBS) for 48 hours, while the monovalent CoV2‐6C3 was easily degraded after incubation with cell media (containing 10 % FBS) for 6 hours,” see section: Design and Characterization of Circularly Bivalent Aptamer, and Figures 3B-C. Regarding claim 14, Sun teaches “the smaller sizes of aptamers (2–3 nm compared to >10 nm for an antibody) allow them to be directly delivered into the respiratory system through intranasal administration or nebulization, see introduction. Regarding claim 15, Sun teaches “aptamers are emerging as highly programmable building blocks for the design of versatile molecular nanodevices with specific structures and functions,” see introduction. Sun does not teach FANA aptamers, pharmaceutical acceptable carriers, or kits. Dahma teaches “nucleic acid ligands (or aptamers) that form a G-tetrad containing at least one arabinose modified nucleotide,” wherein “the arabinose modified nucleotide is 2′-deoxy-2′-fluoroarabinonucleotide (FANA) nucleotide,” see abstract and claim set. Dahma teaches using FANA to increase at least one of nuclease stability or selective binding of an aptamer, see claims 20-21. Dahma teaches combining the FANA aptamers with a pharmaceutically acceptable carrier to create a pharmaceutical composition, see claims 28-31. Dahma teaches creating a commercial package (i.e., a kit absent evidence to the contrary) comprising the FANA aptamer in a pharmaceutical composition and instructions for its use. It would have been obvious to a person having ordinary skill in the art (PHOSITA) before the effective filing date to employ FANA in the engineering aptamers’ binding to the region on SRBD of Sun and combine with a pharmaceutical acceptable carrier to create pharmaceutical compositions that can be included in a kit/commercial package. A PHOSITA would have been motivated to do so in order to increase nuclease stability and/or selective binding of an aptamer, and to have a convenient and acceptable composition to deliver the engineered aptamer to a patient. A PHOSITA would have had a reasonable expectation of success because these were standard methodologies in the art that were shown to work as intended with proven benefits. Claims 1-7 and 11-13 are rejected under 35 U.S.C. 103 as being unpatentable over Irani Alves Ferreira-Bravo I, DeStefano JJ. (Xeno-Nucleic Acid (XNA) 2'-Fluoro-Arabino Nucleic Acid (FANA) Aptamers to the Receptor-Binding Domain of SARS-CoV-2 S Protein Block ACE2 Binding. Viruses. 2021 Oct 2;13(10):1983, in IDS, also published in BioRxiv Jul 14, 2021) as applied to claims 1-7 above, and further in view of Dahma MJ, et al., (US20090131352A1). The teachings of Alves are incorporated herein by reference to the 102 rejection above. Alves does not teach combining the FANA aptamers with pharmaceutically acceptable carriers. Dahma teaches combining the FANA aptamers with a pharmaceutically acceptable carrier to create a pharmaceutical composition, see claims 28-31. Dahma teaches creating a commercial package (i.e., a kit absent evidence to the contrary) comprising the FANA aptamer in a pharmaceutical composition and instructions for its use. It would have been obvious to a person having ordinary skill in the art (PHOSITA) before the effective filing date to employ the FANA aptamers in a pharmaceutical composition comprising a pharmaceutical acceptable carrier. A PHOSITA would have been motivated to do so in order to create a suitable composition for administering to a patient. A PHOSITA would have had a reasonable expectation of success because this is well known and routinely practice in the art. Conclusion No claims are allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to COREY LANE BRETZ whose telephone number is (571)272-7299. The examiner can normally be reached M-F 7:30am - 6:30pm. 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, Ram Shukla can be reached at (571) 272-0735. 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. /COREY LANE BRETZ/Examiner, Art Unit 1635 /RAM R SHUKLA/Supervisory Patent Examiner, Art Unit 1635
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Prosecution Timeline

Mar 30, 2023
Application Filed
Apr 01, 2026
Response Filed
Sep 21, 2026
Non-Final Rejection mailed — §102, §103, §112 (current)

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Prosecution Projections

1-2
Expected OA Rounds
0%
Grant Probability
0%
With Interview (+0.0%)
2y 7m (~0m remaining)
Median Time to Grant
Low
PTA Risk
Based on 3 resolved cases by this examiner. Grant probability derived from career allowance rate.

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