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 .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 11/12/2025 has been entered.
Applicant’s amendment of claims 1, 2, 33, and the addition of new claims 35-38, in the paper of 11/12/2025, is acknowledged. Applicants' arguments filed on 11/12/2025, have been fully considered and are deemed to be persuasive to overcome some of the rejections previously applied. Rejections and/or objections not reiterated from previous office actions are hereby withdrawn. Claims 1-40 are pending and at issue.
Election/Restrictions
Applicant's election without traverse of the invention of the following species:
Species Group I:
" (1) wherein at least one of the nucleotide polymerization initiation sites comprises
a nucleic acid primer that hybridizes to a portion of one of the nucleic acid template
molecules,
Species Group II:
" Claim 13: The composition of claim 9, wherein the composition comprises
a plurality of multivalent molecules including the multivalent molecule of claim 9, wherein the plurality of multivalent molecules comprise the same type of nucleotide unit selected from a group consisting of dATP, dGTP, dCTP, dTTP and dUTP;
Species Group III:
linear nucleic acid molecule
Species Group IV:
a copy of a target sequence of interest;
Species Group V:
the same target of interest sequence target of interest sequences;
Species Group VI:
an oligo ethylene glycol chain having 2-6 subunits;
Species Group VII:
" Claim 17: wherein the one or more nucleotide units comprises one type of
nucleotide unit selected from a group consisting of dATP, dGTP, dCTP, dTTP and
dUTP;
Species Group VIII:
" Claim 19: wherein the one or more nucleotide units comprises one type of
nucleotide unit selected from a group consisting of dATP, dGTP, dCTP, dTTP and
dUTP;
Species Group IX:
the one or more complexed polymerases further comprises a plurality of non-catalytic divalent cations that inhibit polymerase-catalyzed nucleotide incorporation (Claim 22);
in the paper of 1/8/2025, is acknowledged.
Claims 14, 18, 20 and 23 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
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 33-40 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.
Claims 33-38 and 40 each recite the limitation "the composition of" in claim 1. There is insufficient antecedent basis for this limitation in the claim. Claim 39 depends from claim 33 which is why claim 39 is included in this rejection. Claims 33-40 are interpreted as if they were drawn to “the engineered polymerase of”.
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) 34 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim(s) 34 is directed to the composition of claim 1, wherein the engineered polymerase further comprises at least one substitution that confers increased uracil-tolerance compared to the wild-type Candidatus Altiarchaeales Family B DNA polymerase of SEQ ID NO: 1. Applicants only teach the substitutions Aspl41Ala and Glul43Ala encompassed by these substitutions. The specification also fails to describe additional representative species of these substitution that confers increased uracil-tolerance compared to the wild-type Candidatus Altiarchaeales Family B DNA polymerase of SEQ ID NO: 1, 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; cited on the attached Form PTO-892) 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; cited on the attached Form PTO-892), 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 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) 1-8, 24-29, 31 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.
This rejection was stated in the previous office action as it applied to the previous claims 1-8, 24-29. In response to the rejection applicants have minorly amended the claims and argue the rejection as it applies to the newly amended claims. For applicants convenience the original rejection is repeated herein.
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. Smith 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 from Candidatus Altiarchaeales taught by Dombrowski et al. is 100% identical to instant SEQ ID NO:1.
One of skill in the art before the effective filing date would have been motivated to substitute the polymerase taught by Dombrowski et al. for those taught by Smith et al. and mutate them as taught by Smith et al. (D141A and E143A) for their use in methods of DNA synthesis as taught by Smith 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 Smith 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.
Applicants Response:
Applicants continue to traverse the rejection on much of the same basis as in applicants previous response. Applicants reference to Dombrowski-1 or Dombrowski-2 in their traversal is acknowledged, however, it is noted that the rejection is based upon over Sorge et al., U.S. Patent No. 8,268,605 and Dombrowski et al., Uniprot Accession No: A0A497RSY7, August 2020. It is further noted that Dombrowski-1 appears to be the same as the Dombrowski et al., Uniprot Accession No: A0A497RSY7, August 2020.
Applicants submit that in relying upon the theory of inherency, the examiner must provide a basis in fact and/or technical reasoning to reasonably support the determination that the allegedly inherent characteristic necessarily flows from the teachings of the applied prior art." Ex parte Levy, 17 USPQ2d 1461, 1464 (Bd. Pat. App. & Inter. 1990).
Applicants submit the Examiner has failed to provide evidence or reasoning to show inherency under 35 U.S.C. 103 that increased uracil tolerance in a Candidatus Altiarchaeales Family B DNA polymerase compared to the wild type polymerase of SEQ ID NO: 1 necessarily flows from the combination of the natural result of the combination of elements in Sorge in view of Dombrowski-1 or Dombrowski-2.
Applicants submit the claims 1 and 2 are amended to recite that the engineered polymerase is a uracil-tolerant polymerase that exhibits increased uracil-tolerance compared to the wild-type Candidatus Altiarchaeales Family B DNA polymerase of SEQ ID NO: 1. Applicants submit this element of uracil tolerance of the engineered polymerase compared to the wild-type Candidatus Altiarchaeales Family B DNA polymerase of SEQ ID NO: 1, is a functional phenotype of the engineered polymerase that results in the ability of the engineered polymerase to replicate through uracil-containing templates without stalling or degradation. This functional phenotype is not taught or suggested by Sorge alone or in combination with Dombrowski-1 or Dombrowski-2. Applicants submit the engineered polymerase of the pending claims exhibits increased uracil tolerance compared to the wild-type Candidatus Altiarchaeales Family B DNA polymerase of SEQ ID NO: 1, meaning there is a distinct difference between SEQ ID NO: 1 and the engineered polymerase via the functional phenotype defined by a distinct enzymatic activity.
Applicants submit in contrast, Sorge's polymerase is limited to exonuclease-deficient mutants (e.g., D141A/E143A) that permit incorporation of chain-terminating nucleotide analogs, and these mutations reside in the exonuclease motif, which does not determine uracil tolerance.
Applicants submit as established in In re Robertson, 169 F.3d 743, 745 (Fed. Cir. 1999), inherency may not be established by probabilities or possibilities, and the mere fact that a property might occur does not make it inherent. Likewise, In re Rijckaert, 9 F.3d 1531, 1533-34 (Fed. Cir. 1993), confirms that functional or biological properties cannot be presumed inherent absent factual proof demonstrating that the property is necessarily present (Emphasis added).
Applicants submit Sorge fails to provide any factual proof that modifying residues of the polymerase in the Exo I motif, that result in reduced 3'-5' exonuclease activity, would also lead to uracil tolerance, much less any measures of polymerase activity that the Exo I motif of the polymerase would lead to uracil tolerance of uracil-containing templates. Applicants submit that therefore, the element of Claims 1 and 2 reciting that engineered polymerase of the pending claims exhibits increased uracil tolerance compared to the wild-type Candidatus Altiarchaeales Family B DNA polymerase of SEQ ID NO: 1, is not an inherent feature of Sorge's polymerase.
Applicants submit that Dombrowski-1 and Dombrowski-2 fail to remedy the deficiencies of Sorge, although Dombrowski-1 provides the amino acid sequence of a Candidatus Altiarchaeales Family B polymerase that is 100% identical to SEQ ID NO: 1 of the pending claims, and Dombrowski-2, which provides the source from which the sequence originated, Dombrowski-1 and Dombrowski-2 fail to provide any factual proof of functional activity of the polymerase, much less any functional activity related to uracil tolerance. Applicants submit Database sequence records such as UnitProt as cited by the Examiner regarding Dombrowski-1 are evidence of sequence identity/homology, but do not provide experimental functional data. Applicants submit the sequence cited in Dombrowski-1 was simply a hypothetical sequence that was never characterized in terms of its functionality.
Applicants submit furthermore, one of ordinary skill in the art would not have any reasonable expectation of success to design an engineered polymerase with increased uracil tolerance based on the teachings of Sorge and Dombrowski-1 and Dombrowski-2, since both Sorge and Dombrowski-1 and Dombrowski-2 are completely silent as to any disclosure of an engineered polymerase that is uracil tolerant, much less any guidance in Sorge or Dombrowski-1 and Dombrowski-2 regarding uracil tolerant polymerases that have increase uracil tolerance compared to SEQ ID NO: 1, as claimed.
Applicants amendment of the claims and applicants complete argument is acknowledged and has been carefully considered, however is found non-persuasive for the reasons previously made of record and for those reasons repeated herein.
As stated previously and repeated above, the basis of the obviousness of the rejection is as such. One of skill in the art before the effective filing date would have been motivated to substitute the polymerase taught by Dombrowski et al. for those taught by Smith et al. and mutate them as taught by Smith et al. (D141A and E143A) for their use in methods of DNA synthesis as taught by Smith 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 Smith 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 compositions and methods of their use are those taught by Sorge et al., using the above 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 Smith et al. and Dombrowski et al.
In response to applicants submission that the Examiner has failed to provide evidence or reasoning to show inherency under 35 U.S.C. 103 that increased uracil tolerance in a Candidatus Altiarchaeales Family B DNA polymerase compared to the wild type polymerase of SEQ ID NO: 1 necessarily flows from the combination of the natural result of the combination of elements in Sorge in view of Dombrowski-1 or Dombrowski-2, the evidence of uracil tolerance of the obvious mutant polymerase is that in the normal course of DNA synthesis by a DNA polymerase, uracil is considered a nucleotide analog to the normal nucleotide bases of adenine, guanine, cytosine and thymine. As Sorge teaches that the taught mutant Family B DNA polymerases have increased nucleotide analog tolerance one would expect increased uracil tolerance also.
Regardless of the above evidence of inherency, it is noted that inherency and knowledge thereof is not required to arrive at the obvious DNA polymerase mutants. As previously stated and repeated above, 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 Smith 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.
Applicants submission that uracil tolerance of the engineered polymerase compared to the wild-type Candidatus Altiarchaeales Family B DNA polymerase of SEQ ID NO: 1, is a functional phenotype of the engineered polymerase that results in the ability of the engineered polymerase to replicate through uracil-containing templates without stalling or degradation, while appreciated and understood is not found relevant to the current rejection of obviousness over Sorge et al. and Dombrowski et al.
In response to applicants submission that one of ordinary skill in the art would not have any reasonable expectation of success to design an engineered polymerase with increased uracil tolerance based on the teachings of Sorge and Dombrowski-1 and Dombrowski-2, this is not found persuasive because as previously stated and repeated above, the expectation of success is high based upon the high level of skill in the art of recombinant DNA technology as exemplified by Smith et al. and Dombrowski et al. Further the motivation for obviousness is not related to uracil tolerance and thus any expectation of success related to uracil tolerance is not relevant to the current rejection. The motivation and expectation of success for substituting the polymerase taught by Dombrowski et al. is that they teach that the polymerase is a family B DNA polymerase and Smith 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.
Thus claim(s) 1-8, 24-29, 31 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 1-13, 15-17, 19, 21, 22, 24-40 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 1-13, 15-17, 19, 21, 22, 24-30 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:1 and having amino acid substitutions Asp141Ala and Glul43Ala, 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.
Applicants have asked that this rejection be held in abeyance.
Claims 1-13, 15-17, 19, 21, 22, 24-40 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-32 of US 12/270,056 (previously claims 1-4, 6-8, 10-26, 28-35 of copending Application No. 17/705,020 (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. 17/705,020, 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 Glul43Ala, 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 1-13, 15-17, 19, 21, 22, 24-30 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:1 and having amino acid substitutions Asp141Ala and Glul43Ala, 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.
Applicants have asked that this rejection be held in abeyance.
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
11/14/2025
/RICHARD G HUTSON/Primary Examiner, Art Unit 1652