The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 5-5-2025 has been entered.
The amendment filed on 5-5-2025 is acknowledged. Claims 21- 22 have been added. Claims 2-22 are pending. Claims 3-4, 9-13 and 16-19 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Claims 2, 5-8, 14-15 and 20 are currently under examination. It should be noted that claims 3-4, 9-13 and 16-19 have improper claim status identifiers as claims are either “withdrawn” or “previously presented”. Said status identifiers must be corrected in any response this action in order to be considered fully responsive.
Claim Objections Maintained
Claims 2, 7-8 and 21 are objected to for reciting claim language drawn to non-elected inventions is maintained for the reasons set forth in the previous Office action in the objection of claims 2 and 7-8.
Claim Rejections Maintained
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 2, 5-8, 14-15 and 21 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 8-10, 14-15, 21 and 24-25 of copending Application No. 18/028,477 (reference application) for the reasons set forth in the previous Office action in the rejection of claims 2, 5-8 and 14-15
Contrary to Applicant’s assertion, this rejection is not the only remaining rejection. As outlined previously, although the claims at issue are not identical, they are not patentably distinct from each other because the LukA variants of the reference application (SEQ ID NO:1, 2, 4, 7-8 and 25) are encompassed by LukA variants of the rejected claims. SEQ ID NO:1 has 99.2% identity to SEQ ID NO:2 of the rejected claims; SEQ ID NO:2 has 88.2% identity to SEQ ID NO:2 of the rejected claims; SEQ ID NO:4 has 87.2% identity to SEQ ID NO:2 of the rejected claims; SEQ ID NO:7 has 97.6% identity to SEQ ID NO:2 of the rejected claims; SEQ ID NO:8 has 86.9% identity to SEQ ID NO:2 of the rejected claims; and SEQ ID NO:25 has 99.5% identity to SEQ ID NO:2 of the rejected claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
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 2, 5-8, 14-15 and 20-21 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.
Applicant argues:
1. The Present Application includes a sequence alignment containing the amino acid sequence of a majority LukA sequence (designated as SEQ ID NO: 1), and the wildtype LukA variant polypeptides from thirteen (13) different but structurally similar strains of S. aureus to which it corresponds (designated as SEQ ID NOs: 2-14).
2. The specification of the Present Application includes a corresponding description in paragraph [0033] of natural variability at 59 positions (two or three tolerated residues per position) in the mature LukA sequences. In particular, the Present Application notes that a LukA consensus sequence, based on SEQ ID NOs: 2-14 (which are not exhaustive with respect to native S. aureus LukA) would thus include variability at a minimum of 64 positions of LukA.
3. The Present Application provides evidence of the natural variation among wildtype LukA proteins (SEQ ID NOs: 1-14) by way of the alignments presented in FIG. 1 and the analysis of those variants at paragraphs [0031]- [0033]. As noted above, those natural LukA variants encompass amino acid changes at 59 positions within the mature LukA proteins (i.e., aa 28-351).
4. As shown in Exhibit A, a multiple sequence alignment comparison of SEQ ID NOs: 2-14 shows a percent identity above 85% between all the sequences of SEQ ID NOs: 2-14. Consequently, the specification as originally filed fully supports the "at least 85% sequence identity" limitation as used to define the LukA polypeptide variants within the scope of claim 1.
5. The Present Application exemplifies this embodiment with the disclosure of a non-cytotoxic LukA analog comprising a C-terminal deletion. However, the disclosure is in no way limited to that one particular non-cytotoxic LukA analog. The specification further teaches various assays (e.g., membrane damage assay and cell cytotoxicity assay) that can be readily employed to determine whether any one or more substitutions produce a suitable LukA analog.
6. a-LukA polyclonal antibody that neutralizes the effect of LukAB still recognizes LukA lacking the C-terminal extension (rLukAA10C). Thus, the Present Application demonstrates that the LukA C-terminal amino acids can be altered without disrupting the neutralizing epitopes on LukA.
7. The results reported in the post filing '255 Publication (WO 2022/067255) confirm that compositions containing LukA variants having the features recited in claims 2, 5-8, 14, 15, and 20 can be used as (noncytotoxic) monomers to induce a neutralizing immune response and, when used together with wildtype LukB or LukB variants, can form useful LukAB toxoids that induce a broad neutralizing immune response while exhibiting significantly reduced toxicity.
8. The LukA variants described in the '255 Publication contain a number of amino acid variations compared to wildtype LukA amino acid sequences. These are described in Table 1 of the '255 Publication. See Exhibit B at Table 1. In particular, Table 1 of the '255 Publication shows the wild-type LukA CC8 amino acid sequence (SEQ ID NO: 1)1; the wild- type LukA CC45 amino acid sequence (SEQ ID NO: 2) and LukA variants having the sequence of SE ID NO:3-11.
9. The evidence presented in the Present Application, together with the post-filing date evidence, confirms that leukocidin A (LukA) variant polypeptides having an amino acid sequence having at least 85% sequence identity to the amino acid sequence of (i) amino acid residues 28-351 of any one of SEQ ID NOs: 1-3 and 7-14, or (ii) amino acid residues 28-350 of any one of SEQ ID NOs: 4-6 are useful alone, as monomers, or in combination with a LukB polypeptide, which form a LukAB toxoid having a reduction in cytotoxicity against primary phagocytes compared to a LukAB toxin formed with wildtype LukA and LukB polypeptides.
Applicant’s arguments have been fully considered and deemed non-persuasive.
With regard to Points 1-14, the rejected claims are not limited to the encompass variants having at least 85% sequence identity to residues 28-351 of SEQ ID NO:2 wherein said variant polypeptides variant polypeptide, when in combination with a LukB polypeptide, forms a LukAB toxoid having a reduction in cytotoxicity against primary phagocytes compared to a LukAB toxin formed with wildtype LukA and LukB polypeptides and comprising a variant LukA polypeptide comprising an amino acid sequence with at least 90% sequence identity to residues 28-351 of SEQ ID NO:2 wherein said variant polypeptides variant polypeptide, when in combination with a LukB polypeptide, forms a LukAB toxoid having a reduction in cytotoxicity against primary phagocytes compared to a LukAB toxin formed with wildtype LukA and LukB polypeptides and induces a neutralizing immune response against wildtype LukA or the LukAB toxin, Satisfactory disclosure of a "representative number" depends on whether one of skill in the art would recognize that the inventor was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. See, e.g., Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are "representative of the full variety or scope of the genus," or by the establishment of "a reasonable structure-function correlation." Such correlations may be established "by the inventor as described in the specification," or they may be "known in the art at the time of the filing date." See AbbVie, 759 F.3d at 1300-01, 111 USPQ2d 1780, 1790-91 (Fed. Cir. 2014). Description of a representative number of species does not require the description to be of such specificity that it would provide individual support for each species that the genus embraces. Given the claimed 15% or 10% sequence variation, the claimed genus encompasses 2.4 x 1064 and 8.32 x 1040 substitution mutants, respectively. Considering the claimed genus also encompasses insertional and deletion mutants (as well as fragments), the claimed genus is much larger. As set forth in the rejection, while the skilled artisan would be able to envision LukA with a variant sequence of SEQ ID NO:2, they would not be able to predict which variant LukA proteins would have the ability to form a LukAB toxoid having a reduction in cytotoxicity against primary phagocytes compared to a wildtype LukAB toxin when combined with a LukB polypeptide. Consequently, there is no correlation between structure and function as required by the written description requirement.
With regard to Point 5, as noted by Applicant the claims are not limited to variants with a C-terminal deletion. Moreover, Applicant is reminded that adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
With regard to Point 6, the claims are not limited variants with a C-terminal deletion. Moreover, contrary to Applicant’s assertion, the disclosure of a single variant LukA (i.e. rLubAA10C) that maintains the ability to induce neutralizing antibodies does not provide description of the vast genus of variants of LukA encompassed by claim 21. While the skilled artisan may be able to envision variant LukA polypeptides with a sequence variation up to 10%, they would not be able to predict which of those variant LukA polypeptides would have the claimed biological and immunological characteristics.
With regard to Points 7, 8 and 9, written description is based on whether or not Applicant had possession the claimed invention at the time of filing established "by the inventor as described in the specification," or what may be "known in the art at the time of the filing date." See AbbVie, 759 F.3d at 1300-01, 111 USPQ2d 1780, 1790-91 (Fed. Cir. 2014). Applicant cannot rely on post filing references to provide support for variants that were not properly described in the specification.
With regard to Point 9, while the disclosure of the specification would allow the skilled artisan would be able to envision LukA with a sequence with up to 15% variance to the sequence of SEQ ID NO:2, it does not allow them to predict which of said variant LukA proteins would have the claimed biological and immunological characteristics. Consequently, there is no correlation between structure and function as required by the written description requirement.
As outlined previously, the rejected claim is drawn to compositions comprising a variant LukA polypeptide comprising an amino acid sequence with at least 85% sequence identity to residues 28-351 of SEQ ID NO:2 wherein said variant polypeptides variant polypeptide, when in combination with a LukB polypeptide, forms a LukAB toxoid having a reduction in cytotoxicity against primary phagocytes compared to a LukAB toxin formed with wildtype LukA and LukB polypeptides and comprising a variant LukA polypeptide comprising an amino acid sequence with at least 90% sequence identity to residues 28-351 of SEQ ID NO:2 wherein said variant polypeptides variant polypeptide, when in combination with a LukB polypeptide, forms a LukAB toxoid having a reduction in cytotoxicity against primary phagocytes compared to a LukAB toxin formed with wildtype LukA and LukB polypeptides and induces a neutralizing immune response against wildtype LukA or the LukAB toxin (claim 21).
To fulfill the written description requirements set forth 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, the specification must describe at least a substantial number of the members of the claimed genus, or alternatively describe a representative member of the claimed genus, which shares a particularly defining feature common to at least a substantial number of the members of the claimed genus, which would enable the skilled artisan to immediately recognize and distinguish its members from others, so as to reasonably convey to the skilled artisan that Applicant has possession the claimed invention. To adequately describe the claimed genus of variant LukA polypeptides, Applicant must adequately describe the sequence of the LukA polypeptide that possess the recited biological characteristics.
However, the specification does not disclose distinguishing and identifying features of a representative number of members of the genus of variant LukA polypeptides to which the claims are drawn, such as a correlation between the structure of the polypeptide (e.g. sequence) and its recited function (combining with a given LukB polypeptide to form a LukAB toxoid which has a reduction in cytotoxicity against primary phagocytes compared to a LukAB toxin formed with wildtype LukA and LukB polypeptides and optionally induce a neutralizing immune response against wildtype LukA polypeptide or the LukAB toxin), so that the skilled artisan could immediately envision, or recognize at least a substantial number of members of the claimed genus of pharmaceutical compositions. Moreover, the specification fails to disclose which amino acid residues are essential to a given function of the LukA polypeptide or which amino acids might be replaced so that the resultant immunoepitope retains the activity of its parent, or by with which other amino acids the essential amino acids might be replaced so that the resultant immunoepitope retains the activity of its parent. Therefore, since the specification fails to adequately describe at least a substantial number of members of the genus of variant LukA sequences on which the claims are based and therefore fails to adequately describe at least a substantial number of members of the claimed genus of variant LukA polypeptides capable of combining with a given LukB polypeptide to form a LukAB toxoid which has a reduction in cytotoxicity against primary phagocytes compared to a LukAB toxin formed with wildtype LukA and LukB polypeptides.
MPEP § 2163.02 states, “[a]n objective standard for determining compliance with the written description requirement is, 'does the description clearly allow persons of ordinary skill in the art to recognize that he or she invented what is claimed' ”. The courts have decided:
The purpose of the “written description” requirement is broader than to merely explain how to “make and use”; the applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the “written description” inquiry, whatever is now claimed.
See Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1563-64, 19 USPQ2d 1111, 1117 (Federal Circuit, 1991). Furthermore, the written description provision of 35 USC § 112 is severable from its enablement provision; and adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
MPEP 2163.02 further states, “[p]ossession may be shown in a variety of ways including description of an actual reduction to practice, or by showing the invention was 'ready for patenting' such as by disclosure of drawings or structural chemical formulas that show that the invention was complete, or by describing distinguishing identifying characteristics sufficient to show that the applicant was in possession of the claimed invention” See, e.g., Pfaff v. Wells Elecs., Inc., 525 U.S. 55, 68, 119 S.Ct. 304, 312, 48 USPQ2d 1641, 1647 (1998); Regents of the Univ. of Cal. v. Eli Lilly, 119 F.3d 1559, 1568, 43 USPQ2d 1398, 1406 (Fed. Cir. 1997); Amgen, Inc. v. Chugai Pharm., 927 F.2d 1200, 1206, 18 USPQ2d 1016, 1021 (Fed. Cir. 1991) (one must define a compound by "whatever characteristics sufficiently distinguish it"). Moreover, because the claims encompass a genus of variant species, an adequate written description of the claimed invention must include sufficient description of at least a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics sufficient to show that Applicant was in possession of the claimed genus. However, factual evidence of an actual reduction to practice has not been disclosed by Applicant in the specification; nor has Applicant shown the invention was “ready for patenting” by disclosure of drawings or structural chemical formulas that show that the invention was complete; nor has Applicant described distinguishing identifying characteristics sufficient to show that Applicant were in possession of the claimed invention at the time the application was filed.
Additionally, MPEP 2163 states:
"A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed." In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004)”
And:
For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. See, e.g., Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are "representative of the full variety or scope of the genus," or by the establishment of "a reasonable structure-function correlation." Such correlations may be established "by the inventor as described in the specification," or they may be "known in the art at the time of the filing date." See AbbVie, 759 F.3d at 1300-01, 111 USPQ2d 1780, 1790-91 (Fed. Cir. 2014) (Holding that claims to all human antibodies that bind IL-12 with a particular binding affinity rate constant (i.e., koff) were not adequately supported by a specification describing only a single type of human antibody having the claimed features because the disclosed antibody was not representative of other types of antibodies in the claimed genus, as demonstrated by the fact that other disclosed antibodies had different types of heavy and light chains, and shared only a 50% sequence similarity in their variable regions with the disclosed antibodies.).
As evidenced by the teachings of Skolnick et al., the art is unpredictable. Skolnick et al. (Trends in Biotechnology 18: 34-39, 2000) discloses the skilled artisan is well aware that assigning functional activities for any particular protein or protein family based upon sequence homology is inaccurate, in part because of the multifunctional nature of proteins (see, e.g., the abstract; and page 34, Sequence-based approaches to function prediction). Even in situations where there is some confidence of a similar overall structure between two proteins, only experimental research can confirm the artisan's best guess as to the function of the structurally related protein (see, in particular, the abstract and Box 2). Thus, one skilled in the art would not accept the assertion, which is based only upon an observed similarity in amino acid sequence that a variant of a given polypeptide would necessarily have a given biological activity. Moreover, protein chemistry is probably one of the most unpredictable areas of biotechnology. Consequently, the effects of sequence dissimilarities upon protein structure and function cannot be predicted. Bowie et al (Science, 1990, 257:1306-1310) teach that an amino acid sequence encodes a message that determines the shape and function of a protein and that it is the ability of these proteins to fold into unique three-dimensional structures that allows them to function and carry out the instructions of the genome and further teaches that the problem of predicting protein structure from sequence data and in turn utilizing predicted structural determinations to ascertain functional aspects of the protein is extremely complex (see column 1, page 1306). Bowie et al further teach that while it is known that many amino acid substitutions are possible in any given protein, the position within the protein's sequence where such amino acid substitutions can be made with a reasonable expectation of maintaining function are limited. Certain positions in the sequence are critical to the three-dimensional structure/function relationship and these regions can tolerate only conservative substitutions or no substitutions (column 2, page 1306). The sensitivity of proteins to alterations of even a single amino acid in a sequence are exemplified by Burgess et al (J. of Cell Bio. 111:2129-2138, 1990) who teach that replacement of a single lysine reside at position 118 of acidic fibroblast growth factor by glutamic acid led to the substantial loss of heparin binding, receptor binding and biological activity of the protein and by Lazar et al. (Molecular and Cellular Biology, 1988, 8:1247-1252) who teach that in transforming growth factor alpha, replacement of aspartic acid at position 47 with alanine or asparagine did not affect biological activity while replacement with serine or glutamic acid sharply reduced the biological activity of the mitogen. These references demonstrate that even a single amino acid substitution will often dramatically affect the biological activity and characteristics of a protein. Clearly, variant proteins based on the sequence of SEQ ID NO:2 that maintained the recited biological characteristics could not be predicted. Additionally, Bork (Genome Research, 2000,10:398-400) clearly teaches the pitfalls associated with comparative sequence analysis for predicting protein function because of the known error margins for high-throughput computational methods. Bork specifically teaches that computational sequence analysis is far from perfect, despite the fact that sequencing itself is highly automated and accurate (p. 398, column 1). One of the reasons for the inaccuracy is that the quality of data in public sequence databases is still insufficient. This is particularly true for data on protein function. Protein function is context dependent, and both molecular and cellular aspects have to be considered (p. 398, column 2). Conclusions from the comparison analysis are often stretched with regard to protein products (p. 398, column 3). Further, although gene annotation via sequence database searches is already a routine job, even here the error rate is considerable (p. 399, column 2). Most features predicted with an accuracy of greater than 70% are of structural nature and, at best, only indirectly imply a certain functionality (see legend for table 1, page 399). As more sequences are added and as errors accumulate and propagate it becomes more difficult to infer correct function from the many possibilities revealed by database search (p. 399, paragraph bridging columns 2 and 3). The reference finally cautions that although the current methods seem to capture important features and explain general trends, 30% of those features are missing or predicted wrongly. This has to be kept in mind when processing the results further (p. 400, paragraph bridging cols 1 and 2). Clearly, given not only the teachings of Bowie et al., Lazar et al. and Burgess et al. but also the limitations and pitfalls of using computational sequence analysis and the unknown effects of alternative splicing, post translational modification and cellular context on protein function as taught by Bork, the functional variants of the polypeptide of SEQ ID NO:2 cannot be predicted. Clearly, it could not be predicted that a polypeptide that is a “variant” of a given SEQ ID NO: will function in a given manner. Reasonable correlation must exist between structure and function.
Conclusion
No claim is allowed.
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/ROBERT A ZEMAN/Primary Examiner, Art Unit 1645 January 16, 2026