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 .
Claims 136-172 are pending and at issue.
Election/Restrictions
Applicant's election without traverse of the invention of Group II, claims 166-172, drawn to an engineered polymerase of SEQ ID NO:225, in the paper of 5/22/2026, is acknowledged.
Claims 136-165 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
Information Disclosure Statement
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609 A(1) states, "the list may not be incorporated into the specification but must be submitted in a separate paper."
The information disclosure statements filed on 1/19/2025, 2/7/2024, 5/22/2026 and 5/27/2026 are acknowledged and have been considered and initialed as such.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 166-172 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, 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 166 (claims 167-172 dependent on) is indefinite in the recitation “sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glul43Ala” as this recitation is awkward, unclear and confusing because SEQ ID NO:225 does not have a Asp141 and a Glu143. Thus the reference to amino acid substitutions Asp141Ala and Glul43Ala is indefinite as to a reference amino acid sequence. It is recognized that SEQ ID NO:225 comprises the amino acid substitutions Asp141Ala and Glul43Ala relative to SEQ ID NO:1, however, the claim does not contain a reference for the amino acid substitutions Asp141Ala and Glul43Ala.
Appropriate amendment and;/or comment is requested.
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(s) 166-172 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim(s) 166-172 are directed to all possible engineered polymerase comprising: an amino acid sequence that is at least 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase, encompassed by these claims. There is no disclosure of any particular structure to function/activity relationship in the disclosed species. The specification also fails to describe additional representative species of these engineered polymerases by any identifying structural characteristics or properties, for which no predictability of structure is apparent.
Regarding the level of skill and knowledge in the art of amino acid mutation, the reference of Singh et al. (Curr. Protein Pept. Sci. 18:1-11, 2017) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes (see p. 7, column 1, top). Also, the unpredictability associated with amino acid mutations is exemplified by the reference of Zhang et al. (Structure 26:1474-1485, 2018), which discloses that even a mutation of a surface residue that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide (p. 1475, column 1).
Given this lack of additional representative species as encompassed by the claims, Applicants have failed to sufficiently describe the claimed invention, in such full, clear, concise, and exact terms that a skilled artisan would recognize Applicants were in possession of the claimed invention.
Applicant is referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Claim(s) 166-172 are rejected under 35 U.S.C. 112, first paragraph, because the specification, while being enabling for that engineered polymerase comprising: the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase, does not reasonably provide enablement for all possible engineered polymerases comprising: an amino acid sequence that is a mere 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required, are summarized in In re Wands (858 F.2d 731, 8 USPQ 2nd 1400 (Fed. Cir. 1988)) as follows: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claim(s).
Claim(s) 166-172 are so broad as to encompass all possible engineered polymerases comprising: an amino acid sequence that is a mere 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase The scope of the claims is not commensurate with the enablement provided by the disclosure with regard to the extremely large number engineered polymerases and variants broadly encompassed by the claims. The claims rejected under this section of U.S.C. 112, first paragraph, place minimal structural limits on the engineered polymerases encompassed by the claims. Since the amino acid sequence of a protein determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. However, in this case the disclosure is limited to that engineered polymerase comprising: the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase
While recombinant and mutagenesis techniques are known, it is not routine in the art to screen for multiple substitutions or multiple modifications, as encompassed by the instant claims, and the positions within a protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
The specification does not support the broad scope of the claims which encompass any possible engineered polymerase comprising: an amino acid sequence that is a mere 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase, because the specification does not establish: (A) regions of the engineered polymerase which may be modified effecting the polymerase activity, the ability to incorporate a chain terminating nucleotide analog and uracil tolerance; (B) the general tolerance of the engineered polymerases to modification and extent of such tolerance; (C) a rational and predictable scheme for modifying any amino acid residue of an engineered polymerase with an expectation of obtaining the desired biological function; and (D) the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. Because of this lack of guidance, the extended experimentation that would be required to determine which substitutions would be acceptable to retain the required the polymerase activity, ability to incorporate a chain terminating nucleotide analog and uracil tolerance activities and the fact that the relationship between the sequence of a peptide and its tertiary structure (i.e. its activity) are not well understood and are not predictable (e.g., see Ngo et al. in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495; Franceus et al., J. Ind. Microbiol. Biotechnol. Vol 44, pp 687-695, 2017), it would require undue experimentation for one skilled in the art to arrive at the majority of those engineered polymerases comprising: an amino acid sequence that is a mere 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase of the claimed genus.
Thus, applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims broadly including any engineered polymerase comprising: an amino acid sequence that is a mere 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of those engineered polymerases having the desired biological characteristics is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
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.
Claim(s) 166-171 is/are rejected under 35 U.S.C. 103 as being unpatentable over Sorge et al., U.S. Patent No. 8,268,605 and Dombrowski et al., Uniprot Accession No: A0A497RSY7, August 2020.
Sorge et al. teach a number of modified polymerases for improved incorporation of nucleotides and analogues and methods of their use in incorporating nucleotides into polynucleotides, particularly in the context of DNA sequencing. Sorge et al. teach that the modified polymerases are Family B DNA polymerase, JDF-3 which is deficient in 3’ to 5’ exonuclease activity caused by the mutation in the “DXE” motif comprising D141A and E143A. Sorge et al. teach methods of producing the mutant DNA polymerase comprising cloning and mutating the encoding gene and expression in a recombinant host cell. Sorge et al. teach the isolation of the mutated DNA polymerase and its use in DNA synthesis methods comprising contacting the mutated polymerase with a nucleic acid template, nucleic acid primers and nucleotides under conditions that allow the formation of a polymerase complexed with the nucleic acid template and the nucleic acid primer. Sorge et al. teach the above methods of DNA synthesis comprising clonally amplified nucleic acid template/target molecules (linear and circular), comprising primer hybridization to the template molecule and wherein a complexed polymerase is formed comprising a nucleic acid duplex, wherein the duplex comprises one of the nucleic acid template molecules hybridized to a nucleic acid primer.
Dombrowski et al., (Uniprot Accession No: A0A497RSY7, August 2020) teach the protein and encoding DNA sequence of a Family B DNA polymerase from Candidatus Altiarchaeales. The amino acid sequence of the Family B DNA polymerase taught by Dombrowski et al. is 98.5% identical to the amino acid sequence of instant SEQ ID NO:225.
One of skill in the art before the effective filing date would have been motivated to substitute the polymerase taught by Dombrowski et al. (which has 98.5 % sequence identity to instant SEQ ID NO:225) for those taught by Sorge et al. and mutate them as taught by Sorge et al. (D141A and E143A) for their use in methods of DNA synthesis as taught by Sorge et al.. The motivation for substituting the polymerase taught by Dombrowski et al. is that they teach that the polymerase is a family B DNA polymerase and Sorge et al,. teach that any family B DNA polymerase can be mutated with the D141A and E143A substitution to remove 3’ to 5’ exonuclease activity for their use in DNA synthesis methods which allow the incorporating of nucleotide analogs. The obvious methods are those taught by Sorge et al., using the mutated polymerase taught by Dombrowski et al. which are those DNA synthesis methods comprising contacting the mutated polymerase with a nucleic acid template, nucleic acid primers and nucleotides under conditions that allow the formation of a polymerase complexed with the nucleic acid template and the nucleic acid primer. These include the above methods of DNA synthesis comprising clonally amplified nucleic acid template/target molecules (linear and circular), comprising primer hybridization to the template molecule and wherein a complexed polymerase is formed comprising a nucleic acid duplex, wherein the duplex comprises one of the nucleic acid template molecules hybridized to a nucleic acid primer. The expectation of success is high based upon the high level of skill in the art of recombinant DNA technology as exemplified by Sorge et al. and Dombrowski et al.
Thus claim(s) 166-171 is/are rejected under 35 U.S.C. 103 as being unpatentable over Sorge et al., U.S. Patent No. 8,268,605 and Dombrowski et al., Uniprot Accession No: A0A497RSY7, August 2020.
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 §§ 706.02(l)(1) - 706.02(l)(3) 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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
Claims 166-172 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-27 of US 12,139,727. Although the conflicting claims are not identical, they are not patentably distinct from each other, claims 1-27 of US 12,139,727, drawn to method for performing nucleic acid sequencing, comprising: (a) contacting an engineered polymerase with (i) a nucleic acid template molecule and (ii) a nucleic acid primer, wherein said contacting is conducted under a condition suitable for the engineered polymerase to bind to the nucleic acid template molecule and the nucleic acid primer, thereby forming a complexed polymerase, wherein the complexed polymerase comprises an engineered polymerase bound to a nucleic acid duplex, wherein the nucleic acid duplex comprises the nucleic acid template molecule hybridized to the nucleic acid primer, wherein the engineered polymerase comprises an amino acid sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:1 and has amino acid substitutions Asp141Ala and Glu143Ala; (b) contacting the complexed polymerase with a multivalent polymer-nucleotide conjugate to form a multivalent-binding complex, wherein the multivalent polymer-nucleotide conjugate comprises a core attached to multiple nucleotide arms, wherein at least one of the nucleotide arms is attached to a nucleotide unit, wherein said contacting is conducted under a condition suitable for binding the nucleotide unit of at least one of the nucleotide arms of the multivalent polymer-nucleotide conjugate to a corresponding complementary nucleotide base of the nucleic acid template molecule, and inhibiting polymerase-catalyzed extension of the nucleic acid duplex; (c) detecting the multivalent-binding complex; and (d) determining the sequence of the nucleic acid template molecule anticipates/makes obvious instant claims 166-172 drawn to a engineered polymerase comprising: an amino acid sequence that is at least 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase.
Claims 166-172 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-32 of US 12,270,056. Although the conflicting claims are not identical, they are not patentably distinct from each other, because claims 1-32 of US 12,270,056, drawn to a method of forming a complexed polymerase, comprising: contacting an engineered polymerase with (i) a nucleic acid template molecule and (ii) a nucleic acid primer to form a binding or ternary polymerase complex comprising: an engineered polymerase bound to a nucleic acid duplex, wherein the nucleic acid duplex comprises a nucleic acid template molecule hybridized to a nucleic acid primer, wherein the nucleic acid template molecule comprises at least one uracil base in the nucleic acid template molecule, and wherein the engineered polymerase comprises an amino acid sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 1, and has amino acid substitutions Asp141Ala and Glul43 Ala, and wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to the nucleic acid template molecule when compared with the wild type Candidatus Altiarchaeales Family B DNA polymerase anticipates/makes obvious instant claims 166-172 drawn to a engineered polymerase comprising: an amino acid sequence that is at least 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase.
Claims 166-172 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6-8, 10-269, 28-35 of copending Application No. 17/705,011 (reference application, now allowed). Although the conflicting claims are not identical, they are not patentably distinct from each other, Claims 1-4, 6-8, 10-269, 28-35 of copending Application No. 17/705,011, drawn to an engineered polymerase comprising: an amino acid sequence that is at least 90% identical to the amino acid sequence of SEQ ID NO:1 and has amino acid substitutions Asp141Ala and Glul43Ala, and one or more additional amino acid substitutions, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:1, and wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased tolerance for uracil uracil-tolerance in one or more nucleic acid template molecules compared to the wild-type Candidatus Altiarchaeales Family B DNA polymerase of SEQ ID NO: 1. anticipates/makes obvious instant claims 166-172 drawn to a engineered polymerase comprising: an amino acid sequence that is at least 85% identical to the amino acid sequence of SEQ ID NO:225 and has amino acid substitutions Asp141Ala and Glu143Ala, wherein the engineered polymerase has increased ability to incorporate a chain terminating nucleotide analog compared to a wild type polymerase having the amino acid sequence of SEQ ID NO:225, wherein the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance to a nucleic acid template molecule when compared to the wild type Candidatus Altiarchaeales Family B DNA polymerase.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Related ART:
U.S. Patent No. 11,220,707
U.S. Patent No. 10,768,173
Remarks
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to RICHARD G HUTSON whose telephone number is (571)272-0930. The examiner can normally be reached 6-3 EST Mon-Fri.
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rgh
7/18/2026
/RICHARD G HUTSON/Primary Examiner, Art Unit 1652
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