CTFR 18/183,815 CTFR 99463 DETAILED ACTION Notice of Pre-AIA or AIA Status 07-03-aia AIA 15-10-aia The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. Withdrawal of Rejections The response and amendments filed on 03/18/2026 are acknowledged. Any previously applied minor objections and/or minor rejections ( i.e., formal matters), not explicitly restated here for brevity, have been withdrawn necessitated by Applicant’s formality correction and/or amendments. For the purposes of clarity of the record, the reasons for the Examiner’s withdrawal, and/or maintaining, if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner’s Response to Arguments section. Briefly, the previous claim rejections under 35 U.S.C. 112(b) for indefiniteness have been withdrawn necessitated by Applicant’s amendments; however, new grounds of rejection have been set forth below. The previous claim rejections under 35 U.S.C. 112(a) for written description have been withdrawn for claim 52, as it pertains to generally claiming peptides, necessitated by Applicant’s amendments. The previous claim rejections under 35 U.S.C 102 for anticipation have been withdrawn necessitated by Applicant’s amendments. The previous claim rejections under 35 U.S.C. 103 for obviousness have been withdrawn necessitated by Applicant’s amendments; however, new grounds of rejection are set forth below. The following rejections and/or objections are either reiterated or newly applied. They constitute the complete set presently being applied to the instant application. Maintained Objections Drawing Objections 06-22 AIA The drawings are objected to because higher quality images/figures are requested for all figures filed on 05/24/2023, as these figures are low quality and the Examiner cannot discern certain structures and labels that are being displayed . Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance. Examiner’s Response to Arguments Regarding Applicant’s arguments that the Examiner did not explain why the drawings are objected to (remarks, page 5), this argument is not persuasive because the Examiner informed the Applicant that the figures are low quality and the structures and labels for all the figures cannot be discerned. More specifically, all figures are blurry, and for example, the labels for the protein conformation/folding images cannot be discerned because the images are too blurry. It is requested that Applicant submit new, higher resolution figures and images. 12-256 AIA New Grounds of Rejection Necessitated by Amendments Claim Rejections - 35 USC § 112(b), Indefiniteness 07-103 AIA The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action. Claims 52, 55, 58-59, and 61-62 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 52 recites that the Cap2 enzymes has a target recognition motif and then goes on to recite that the Cap2 enzyme ligates the first peptide to the target peptide, forming a fusion peptide. It is unclear if the Cap2 enzyme is directly coupled to the target peptide since the Cap2 enzyme has a target recognition motif, or if the target peptide is directly coupled to the first peptide because the claim recites that the Cap2 enzyme ligates the first peptide to the target peptide, forming a fusion peptide. Furthermore, the order by which the peptides are ligated together is unclear because the claim recites that the Cap2 enzyme has a target recognition motif, which one of ordinary skill in the art would understand means that the Cap2 enzyme binds to the target peptide; however, the claim then goes on to recite that the Cap2 enzyme ligates the first peptide to the target peptide. For the purpose of applying prior art, the Examiner has interpreted this to mean that the target peptide is indirectly ligated to the first peptide, wherein the CD- NTase and Cap2 proteins are separating the target peptide and first peptide to make a fusion protein. Claim 52 recites “cGAS/DncV”; however, the instant specification does not completely recite what the cGAS/DncV abbreviation stands for; therefore, there can be multiple interpretations for what cGAS/DncV is. Moreover, abbreviations should be completely spelled out upon first use, especially when they are not defined in the instant specification. For the purposes of applying prior art, the Examiner has interpreted cGAS/DncV to be cyclic GMP-AMP synthase/dinucleotide cyclase. Claim 52 recites “a first peptide having an intermediary peptide recognition motif comprising a cGAS/DncV-like nucleotidyltransferase (CD-NTase) recognition motif”; however, it is unclear if the first peptide has an intermediary peptide recognition motive and a CD-NTase recognition motif, or if the first peptide has an intermediary peptide recognition motif, which is a CD-NTase recognition motif. For the purposes of applying prior art, the Examiner has interpreted the intermediary peptide recognition motif to be the CD-NTase recognition motif. Examiner’s Response to Arguments Regarding Applicant’s arguments pertaining to the 35 U.S.C. 112(b) rejection (remarks, page 5), as stated above, these rejections have been withdrawn; however, new grounds of rejection have been set forth necessitated by Applicant’s amendments. Therefore, Applicant’s arguments are moot. 12-256 AIA New Grounds of Rejection Necessitated by Amendments Claim Rejections - 35 USC § 112(a), Written Description 07-103 AIA The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action. 07-31-01 Claims 52, 55, 58-59, and 61-62 are rejected under 35 U.S.C. 112(a) 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. Claims 52-53 recites a “recognition motif” for the Cap2 enzyme and first enzyme. The instant Specification defines “recognition motif” as “an antibody, or antibody fragment thereof, configured to bind to and couple a target peptide. In alternative embodiments, target recognition motif of the invention may include an engineered protein binding motif configured to bind to and couple a target peptide” ( see, e.g., instant Specification, pg. 15, lines 4-7). However, the instant Specification does not recite what these target recognition motifs are, such as specific sequences, or structures. Therefore, the Examiner has interpreted this to mean that there are multiple sequences and/or structure that can be recognition motifs for these peptides. As such, the scope of the claimed recognition motifs encompasses a large number of sequences and/or structures that are needed to perform the activity of the protein binding to a target peptide. Claim 58 recites “wherein said Cap2 enzyme is selected from SEQ ID NO.’s 1-2, 13 or 16, or a fragment or variant thereof”. Claim 59 recites “wherein said target recognition motif comprises an antibody, or fragment thereof”. The instant Specification defines a “fragment” as “one that substantially retains at least one biological activity normally associated with that polypeptide” and “substantially retains all of the activities possessed by the unmodified peptide” ( see, e.g., instant Specification, pg. 23, lines 12-16). Additionally, the instant Specification defines “variant” as “a member of a set of similar proteins that perform the same or similar biological roles. For example, fragments and variants of the disclosed polynucleotides and amino acid sequences of the invention encoded thereby are also encompassed by the present invention. By "fragment" is intended a portion of the polynucleotide or a portion of the amino acid sequence” ( see, e.g., instant Specification, pg. 24, lines 25-29). The Examiner has interpreted these phrase to mean that there is no necessary core structure and/or sequence needed for the polypeptide or fragment to exhibit enzymatic activity, or activity in general. As such, the scope of the claimed polypeptide, fragment, or variant encompasses a large array of polypeptides without any necessary core structure and/or sequence that would be needed in order for the polypeptide to exhibit the claimed activity. The Specification does not teach fragment or variants of the Cap2 enzyme sequence ( i.e., SEQ ID NO: 1), the CD-NTase peptide sequence ( i.e., SEQ ID NO: 5), or the antibody sequence that comprises the target recognition motif. Therefore, the instant Specification fails to set forth a representative number of species, such as structures and/or sequences, for fragments or variants of the Cap2 enzyme sequence ( i.e., SEQ ID NO: 1), the CD-NTase peptide sequence ( i.e., SEQ ID NO: 5), or the antibody sequence that comprises the target recognition motif. Moreover, it is unclear which core structures or core residues are required within SEQ ID NOs: 1 and 5 for enzyme activity to be maintained. Thus, the specific embodiments taught in the instant Specification are not sufficient for the skilled artisan to envisage what constitutes a cores structure and/or sequence for a peptide, fragment, or variant to exhibit the required activity. Moreover, in regards to the recognition motifs, there are probably undiscovered recognition motifs that can be used to bind proteins to target peptides, which the claimed invention encompasses. Therefore, the specific embodiments taught in the instant Specification, in regards to the recognition motifs, are not sufficient for the skilled artisan to envisage what constitutes the recognition motif for protein-peptide binding. Examiner’s Response to Arguments Regarding Applicant’s arguments pertaining to the 35 U.S.C. 112(a), written description rejection (remarks, pages 5-6), as previously stated above, the 35 U.S.C 112(a), written description rejection has been withdrawn for claim 52, as it pertains to generally claiming peptides. However, Applicant has not provided arguments and has not amended claims to overcome the 35 U.S.C. 112(a), written description rejections as it pertains to recitation of “fragments” or “variants” in claims 55 and 58-59, nor does Applicant provide arguments and amendments to overcome the rejections pertaining to the recognition motifs. Therefore, these rejections have been maintained. 12-256 AIA New Grounds of Rejection Necessitated by Amendments Claim Rejections - 35 USC § 103, Obviousness 07-103 AIA The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action. 07-21-aia AIA Claim s 52, 55, and 58-59 are rejected under 35 U.S.C. 103 as being unpatentable over Kranzusch (cGAS and CD-NTase enzymes: structure, mechanism, and evolution; 2019 – previously cited) in view of Whiteley (WO 2020/051197; Date of Publication: March 12, 2020 – previously cited), Murphy (The Genome Sequence of Enterobacter cloacae UCI 50; 2014 – previously cited), and Trier (Peptides, Antibodies, Peptide Antibodies and More; 2019 – newly cited) . Kranzusch ’s general disclosure relates to cGAS/DncV signaling in human cells to control immune-sensing of cytosolic DNA ( see, e.g., Kranzusch, abstract). Moreover, Kranzusch discloses “cGAS and DncV homologs comprise a family of cGAS/ DncV-like nucleotidyltransferase (CD-NTase) enzymes that synthesize noncanonical RNA signals including cyclic dinucleotides, cyclic trinucleotides, and linear oligonucleotides” ( see, e.g., Kranzusch, abstract). Furthermore, Kranzusch discloses that “CD-NTase enzymes function as nucleic acid and chemical sensors, allowing animal and bacterial cells to respond to changing environmental conditions and rapidly initiate signaling responses” ( see, e.g., Kranzusch, “cGAS and CD-NTase enzymes as chemical sensors”, pg. 179). Regarding claim 52 pertaining to the first peptide, Kranzusch teaches that folate-like metabolites can bind to CD-NTase and inactivate the enzymatic activity of the CD-NTase ( see, e.g., Kranzusch, Figure 1, pg. 179). One of ordinary skill in the art would understand that if the folate-like metabolites bind to CD-NTase, then these metabolites have a CD-NTase recognition motif. However, Kranzusch does not teach : a CD-NTase-associated protein 2 (Cap2) having a target recognition motif ( claim 52 ); or a target peptide ( claim 52 ); or an intermediary peptide comprising a CD-NTase peptide coupling the first peptide and said Cap2 enzyme ( claim 52 ); or wherein said Cap2 enzyme ligates said first peptide to said target peptide forming a fusion peptide ( claim 52 ); or wherein said CD-NTase peptide is SEQ ID NO: 5 ( claim 52 ); or wherein said Cap2 enzyme is SEQ ID NO: 1 ( claim 58 ); or wherein said target recognition motif comprises an antibody, or a fragment thereof, or an engineered protein binding motif ( claim 59 ). Whiteley ’s general disclosure relates to “the discovery and characterization of the CD-NTase family of proteins, as well as compositions comprising CD-NTases ( see, e.g., Whiteley, abstract). Furthermore, Whiteley discloses “A series of crystal structures establish CD-NTas es as a structurally conserved family and reveal key contacts in the active-site lid that direct purine or pyrimidine selection. CD-NTas e products are not restricted to CDNs and also include an unexpected class of cyclic trinucleotide compounds. Biochemical and cellular analysis of these novel nucleotide second messengers demonstrated that these signals active distinct host receptors and modulate the interaction of both pathogenic and commensal microbiota with their animal and plant hosts” ( see, e.g., Whiteley, pg. 19, lines 5-11). Regarding claims 52 and 55 pertaining to the CD-NTase, Whiteley teaches SEQ ID NO: 112, which encodes a CD-NTase with 100% sequence identity to instant SEQ ID NO: 5 ( see, e.g., Office Action Appendix). Murphy ’s general disclosure relates to a submitted Uniprot sequence of the Enterobacter cloacae UCI 50 genome, wherein this sequence contains a sequence encoding the Cap2 enzyme ( see, e.g., Murphy, Uniprot website and sequence). Regarding claim 52 and 58 pertaining to the Cap2 enzyme, Murphy teaches a sequence within the genome of Enterobacter cloacae , which has 100% sequence identity to instant SEQ ID NO: 1 ( see, e.g., Office Action Appendix). Trier ’s general disclosure relates to peptides and antibodies in molecular biology, as well as development of new peptide and antibodies for therapy and prevention of disease ( see, e.g., Trier, Introduction, pg. 1). Furthermore, Trier discloses the use of polyclonal, monoclonal, recombinant, and peptide antibodies for treatment of different diseases and interactions with different target molecules ( see, e.g., Trier, Sections 3-4, pgs. 4-11). Regarding claims 52 and 59 pertaining to the target recognition motif and the target peptide, Trier teaches that recombinant antibodies can be produced that are bispecific ( see, e.g., Trier, Section 3.5, pg. 8); therefore, one of ordinary skill in the art would readily understand that the antibody can be generated to bind to both CD-NTase and the target peptide. Trier teaches that the generated recombinant antibody can be produced with pre-determined properties and a specific purpose ( see, e.g., Trier, Sections 3.4-3.5, pg. 8). Furthermore, Trier teaches peptide antibodies can be targeted to any peptide and “Peptide Abs are usually of high specificity and affinity, and have the advantage that the antigenic target is already well-defined” ( see, e.g., Trier, Section 4.1, pg. 9). Therefore, one of ordinary skill in the art would readily understand that a target peptide can be generated to interact with an peptide antibody, based on the teachings of Trier. Furthermore, the Examiner has interpreted the target peptide to be any peptide since the claims do not further limit what the target peptide is; therefore, based on the teachings of Trier, peptide antibodies can be directed to any peptide, and can be specifically directed to post-translational modifications, conserved regions, intra-cellular or extra-cellular domains, cleavage sites, tags, and specific conformations ( see, e.g., Trier, section 4.1, pg. 9), of the target peptide. It would have been first obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine Kranzusch’s first peptide, which can be a folate-like metabolite, with CD-NTase, as taught by Whiteley. One would have been motivated to do so because Whiteley teaches that CD-NTases are capable of nucleotide second messenger synthesis ( see, e.g., Whiteley, pg. 32, lines 21-23). Moreover, Kranzusch teaches that CD-NTase is on and active in the absence of inactivating ligands, such as folate metabolites ( see, e.g., Kranzusch, Figure 1). Therefore, it would be obvious to one of ordinary skill in the art that the first peptide can be used as a “molecular switch” to turn on and off the activity of CD-NTase, such as secondary messenger synthesis, within the fusion peptide. One would have expected success because Kranzusch and Whiteley both teach CD-NTase signaling. It would have been secondly obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine Kranzusch’s first peptide bound to CD-NTase and Cap2, as taught by Whiteley and Murphy, respectively, with an antibody as the target recognition motif bound to a target protein, as taught by Trier. One would have been motivated to do so because Trier teaches peptide antibodies can be targeted to any peptide and “Peptide Abs are usually of high specificity and affinity, and have the advantage that the antigenic target is already well-defined” ( see, e.g., Trier, Section 4.1, pg. 9). Moreover, Trier teaches recombinant antibodies can be produced that are bispecific ( see, e.g., Trier, Section 3.5, pg. 8); therefore, one of ordinary skill in the art would readily understand that the antibody can be generated to bind to both CD-NTase and the target peptide. Trier teaches that the generated recombinant antibody can be produced with pre-determined properties and a specific purpose ( see, e.g., Trier, Sections 3.4-3.5, pg. 8). Therefore, Trier teaches that antibodies can be generated that can bind to multiple targets at the same time (i.e., bivalent), such as the Cap2 protein and the target protein, and can be produced to bind to a wide variety of peptide target. Moreover, Whiteley teaches detecting the presence of a polypeptide in a sample by using an antibody which binds to the polypeptide ( see, e.g., Whiteley, pg. 6, lines 7-12). Additionally, Whiteley teaches modulating the expression of the polypeptide bound to the antibody ( see, e.g., Whiteley, pg. 7, lines 13-25), and Kranzusch teaches activation and inactivation of CD-NTase by binding of specific ligands, such as folate metabolites, to CD-NTase ( see, e.g., Kranzusch, Figure 1). Therefore, one of ordinary skill in the art would readily understand that activation and inactivation of the target peptide could come from the first peptide interacting with the CD- NTase protein. One would have expected success because Kranzusch, Whiteley, Murphy, and Trier all teach proteins for binding and activation of molecular pathways. Regarding claim 52 pertaining to Cap2 ligating the first peptide and target peptide, this is a product-by-process limitation ( see, e.g., MPEP 2113); therefore, patentability is based on the product itself and not on the process of making; however, the combination of Kranzusch, Murphy, Whitely, and Trier teaches a first peptide ligated to CD-NTase ( see, e.g., Kranzusch, Figure 1, pg. 179), wherein CD-NTase ( see, e.g., Whitely & Office Action Appendix) is ligated to Cap2 ( see, e.g., Murphy & Office Action Appendix), and Cap2 is ligated to an antibody that can bind to a target peptide ( see, e.g., Trier, pgs. 8-9). Therefore, the combined prior art teaches that the first peptide is indirectly fused to the target peptide via CD-NTase and Cap2 . 07-22-aia AIA Claim 61 is rejected under 35 U.S.C. 103 as being unpatentable over Kranzusch , Murphy , Whiteley , and Trier as applied to claim s 52, 55, and 58-59 above, and further in view of Chen (Fusion Protein Linkers: Property, Design and Functionality; 2012 – previously cited) . The combined teachings of Kranzusch, Murphy, Whiteley, and Trier, herein referred to as modified-Kranzusch-Murphy-Whiteley-Trier, are discussed above as it pertains to generating a composition comprising a first peptide, a Cap2 enzyme, a target peptide, and an intermediary peptide. Regarding claim 61 pertaining to the first and target peptides, modified-Kranzusch-Murphy-Whiteley-Trier teaches a first peptide, such as a folate-like metabolite that can bind to CD-NTase ( see, e.g., Kranzusch, Figure 1, pg. 179), and modified-Kranzusch-Murphy-Whiteley-Trier teaches a target peptide that can bind to the target recognition motif antibody ( see, e.g., Trier, pgs. 8-9). However, modified-Kranzusch-Murphy-Whiteley-Trier does not teach : wherein the amino acid sequence of the first and target peptides are preserved in said fusion protein ( claim 61 ). Chen ’s general disclosure relates to a review pertaining to the “current knowledge of fusion protein linkers and summarizes examples for their design and application. The general properties of linkers derived from naturally-occurring multi-domain proteins can be considered as the foundation in linker design. Empirical linkers designed by researchers are generally classified into 3 categories according to their structures: flexible linkers, rigid linkers, and in vivo cleavable linkers. Besides the basic role in linking the functional domains together (as in flexible and rigid linkers) or releasing the free functional domain in vivo (as in in vivo cleavable linkers), linkers may offer many other advantages for the production of fusion proteins, such as improving biological activity, increasing expression yield, and achieving desirable pharmacokinetic profiles ( see, e.g., Chen, abstract). Regarding claim 61 pertaining to preservation of the fusion peptide, Chen teaches fusion protein linkers that can be implemented between peptides within a fusion protein, wherein these protein linkers are “critical to preserve the stability or bioactivity of the fusion proteins” ( see, e.g., Chen, Section 3.2, pg. 6). Moreover, Chen teaches that “Direct fusion of functional domains without a linker may lead to many undesirable outcomes, including misfolding of the fusion proteins” ( see, e.g., Introduction, pg. 2). Therefore, based on the teachings of Chen, one of ordinary skill in the art would understand that implementing linkers within the fusion protein would preserve the peptides and their structure within the fusion protein. It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce modified-Kranzusch-Murphy-Whiteley-Trier fusion protein, wherein the peptides are preserved through implementation of protein linkers between the peptides, as taught by Chen. One would have been motivated to do so because Chen teaches that “Direct fusion of functional domains without a linker may lead to many undesirable outcomes, including misfolding of the fusion proteins” ( see, e.g., Introduction, pg. 2), and it would be obvious to one of ordinary skill in the art that misfolding does not preserve the peptides within the fusion protein. Additionally, Chen teaches that protein linkers preserve the stability and bioactivity of the fusion protein ( see, e.g., Chen, Section 3.2, pg. 6). Moreover, modified-Kranzusch-Murphy-Whiteley-Trier teaches production of a fusion protein comprising a first peptide, which can be a folate-like metabolite ( see, e.g., Kranzusch, Figure 1, pg. 179), CD-NTase ( see, e.g., Whiteley, abstract & Office Action Appendix), Cap2 ( see, e.g., Murphy, Office Action Appendix), and Trier ( see, e.g., Trier, pgs. 8-9). Therefore, based on the teachings of modified-Kranzusch-Murphy-Whiteley-Trier and Chen, it would be obvious to implement protein linkers between the peptides in a Cap2 fusion protein in order to preserve the structure and function of the fusion protein. One would have expected success because modified-Kranzusch-Murphy-Whiteley-Trier and Chen both teach generation of fusion proteins. Examiner’s Response to Arguments Regarding Applicant’s arguments pertaining to the 35 U.S.C 102 rejection and 35 U.S.C 103 rejection, as it pertains to the teachings of Peche (remarks, pages 6-), as discussed above, these rejections have been withdrawn and Peche was not relied upon in the newly presented rejection above due to Applicant’s amendments. Therefore, Applicant’s arguments are moot. Conclusion Claims 52, 55, 58-59, and 61-62 are rejected. However, claim 62 appears free from the art because prior to the effective filing date of the claimed invention, the structure of Cap2 was not determined and, due to this, the prior art does not teach that Cap2 is a homodimer. No claims are allowed. 07-39 AIA THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a). A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action. Correspondence Information Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE IANNUZO whose telephone number is (703)756-5559. The examiner can normally be reached Mon - Fri: 8:30-6:00 EST. 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, Sharmila Landau can be reached at (571) 272-0614. 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. /NATALIE IANNUZO/Examiner, Art Unit 1653 /SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653 Application/Control Number: 18/183,815 Page 2 Art Unit: 1653 Application/Control Number: 18/183,815 Page 3 Art Unit: 1653 Application/Control Number: 18/183,815 Page 4 Art Unit: 1653 Application/Control Number: 18/183,815 Page 5 Art Unit: 1653 Application/Control Number: 18/183,815 Page 6 Art Unit: 1653 Application/Control Number: 18/183,815 Page 7 Art Unit: 1653 Application/Control Number: 18/183,815 Page 8 Art Unit: 1653 Application/Control Number: 18/183,815 Page 9 Art Unit: 1653 Application/Control Number: 18/183,815 Page 10 Art Unit: 1653 Application/Control Number: 18/183,815 Page 11 Art Unit: 1653 Application/Control Number: 18/183,815 Page 12 Art Unit: 1653 Application/Control Number: 18/183,815 Page 13 Art Unit: 1653 Application/Control Number: 18/183,815 Page 14 Art Unit: 1653 Application/Control Number: 18/183,815 Page 15 Art Unit: 1653 Application/Control Number: 18/183,815 Page 16 Art Unit: 1653 Application/Control Number: 18/183,815 Page 17 Art Unit: 1653
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