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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 01/15/2026 has been entered.
Status of the Claims
Claims 1, 6-9, and 19-21 are pending.
Claims 1, 6-9, and 19-21 are examined herein.
Claims 1, 6-9, and 19-21 are rejected.
Priority
Application No. 18/272,978 filed on 07/18/2023 is a PCT of Application No. PCT/JP2022/002162 filed on 01/21/2022 which claims priority to provisional Application No. 63/285/223 filed on 12/02/2021. Application No. 18/272,978 also claims foreign priority to Japanese Application No. JP2021-009001 filed on 01/22/2021.
A certified English translation of the foreign priority document has been provided, dated 01/15/2026.
Upon review, the pending claims dated 01/15/2026 are benefited the following priority dates:
Japanese Application No. JP2021-009001 filed on 01/22/2021 only provides support for claim 20 because the priority document describes the invention comprising a plastid localization signal, and does not describe the method comprising adding a nuclear or mitochondrial localization signal. Therefore, claim 20 is benefitted the priority date of 01/22/2021.
Provisional Application No. 63/285/223 filed on 12/02/2021 only provides support for claim 21 because the priority document only describes the invention comprising a mitochondrial localization signal, and does not describe the method comprising adding a nuclear or plastid localization signal. Therefore, claim 21 is benefitted the priority date of 12/02/2021.
PCT of Application No. PCT/JP2022/002162 filed on 01/21/2022 provides support for all pending claims. Therefore, remaining claims 1, 6-9, and 19 are benefitted the priority date of 01/21/2022.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claim(s) 1, 6-9,19, and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Mok (Mok, B. Y., de Moraes, M. H., Zeng, J., Bosch, D. E., Kotrys, A. V., Raguram, A., ... & Liu, D. R. (2020). A bacterial cytidine deaminase toxin enables CRISPR-free mitochondrial base editing. Nature, 583(7817), 631-637) and Kang (Kang, B. C., Bae, S. J., Lee, S., Lee, J. S., Kim, A., Lee, H., ... & Kim, J. S. (2021). Chloroplast and mitochondrial DNA editing in plants. Nature Plants, 7(7), 899-905).
Claim 1 is drawn to a method for editing a plant genomic DNA, comprising converting a target nucleotide on the genomic DNA to another nucleotide, wherein the conversion is carried out with cytidine deaminase which is a protein described in the following (a) or (b):(a) a protein comprising the amino acid sequence as set forth in SEQ ID NO: 35; or (b) a protein comprising an amino acid sequence having a sequence identity of 90% or more to the amino acid sequence as set forth in SEQ ID NO: 35, and having cytidine deaminase activity, wherein an N-terminal portion of the cytidine deaminase and another portion are each fused with a different transcription activator-like effector (TALE), and wherein the conversion comprises introducing a DNA encoding a fusion protein comprising a part of or the entire cytidine deaminase and TALE, to which a nuclear localization signal peptide, a plastid localization signal peptide or a mitochondrial localization signal peptide is added, into a nuclear genome in a plant cell, and then allowing the signal peptide-added fusion protein to express in the plant cell.
Claim 6 is drawn to a plant genome, comprising a plant genomic DNA edited by the method according to claim 1.
Claim 7 is drawn to a plant cell, comprising the plant genome according to claim 6.
Claim 8 is drawn to a seed or a plant, comprising the plant cell according to claim 7.
Claim 9 is drawn to a method for producing a plant having an edited plant genome, the method comprising editing a plant genome by the method for editing a plant genomic DNA according to claim 1.
Claim 19 is drawn to the method according to claim 1, wherein the conversion comprises introducing the DNA encoding the fusion protein comprising the part of or the entire cytidine deaminase and TALE, to which the nuclear localization signal peptide is added, into the nuclear genome in the plant cell.
Claim 21 is drawn to the method according to claim 1, wherein the conversion comprises introducing the DNA encoding the fusion protein comprising the part of or the entire cytidine deaminase and TALE, to which the mitochondrial localization signal peptide is added, into the nuclear genome in the plant cell.
Regarding claim 1, Regarding claim 1, Mok teaches a cytidine deaminase polypeptide sequence (UniProt Accession No. AOA1V2VU04, published online 12/02/2020) that comprises an amino acid sequence with 100% identity to instant SEQ ID NO: 35 (see alignment in Office Action dated 04/29/2025). Mok also teaches the cytidine deaminase (named DddA) is split in half, wherein one half contains the C-terminus and the other half contains the N-terminus (p. 633, section titled Splitting DddAtox into non-toxic halves), and each portion is fused with a different TALE (Fig. 3a). Further, Mok also teaches the cytidine deaminase is used to edit genomes to convert C*G to T*A by expressing two halves of a cytidine deaminase (named DddA) that are fused to two different TALEs and also operably linked to a mitochondrial targeting signal (Fig. 3a and p. 634, section titled Mitochondrial base editing by TALE- DddAtox) in cells.
Regarding claim 19, Mok teaches the TALE-DddAtox can be used for nuclear base editing when a nuclear localization signal is added (p. 634, ¶2).
However, Mok does not explicitly teach:
The method is used for editing plant genomic DNA, and the conversion comprises introducing a DNA encoding a fusion protein comprising the cytidine deaminase and TALE into a nuclear genome in a plant cell, and then allowing the signal peptide-added fusion protein to express in the plant cell (remaining limitations of claim 1).
A plant genome, comprising a plant genomic DNA edited by the method according to claim 1 (claim 6).
A plant cell, comprising the plant genome according to claim 6 (claim 7).
A seed or a plant, comprising the plant cell according to claim 7 (claim 8).
The method according to claim 1, wherein the conversion comprises introducing the DNA encoding the fusion protein comprising the part of or the entire cytidine deaminase and TALE, to which the nuclear localization signal peptide is added, into the nuclear genome in the plant cell (claim 19).
The method according to claim 1, wherein the conversion comprises introducing the DNA encoding the fusion protein comprising the part of or the entire cytidine deaminase and TALE, to which the mitochondrial localization signal peptide is added, into the nuclear genome in the plant cell (claim 21).
Regarding the remaining limitations of claim 1 and claim 19, in analogous art Kang teaches applying the method described by Mok to lettuce and rapeseed plant cells (abstract, p. 899, ¶2) to edit mitochondrial and chloroplast DNA by adding a chloroplast transit peptide (CTP) or a mitochondrial targeting sequence (MTS) respectively to generate fusion peptides (abstract, p. 899, ¶3). The fusion peptides are expressed via transient expression of plasmids and via DNA-free in vitro transcribed ddCBE mRNA using polyethylene glycol (PEG)-mediated transfection methods. In other analogous art, Kavipriya teaches a review of various transformation methods (title). In this review, Kavipriya teaches alternative methods of plant cell transformation including, e.g., agrobacterium-mediated transformation which generates high transformation frequencies and stable transformants (i.e. the plasmids are introduced into the nuclear genomes) (Table 2).
Regarding claim 6, Kang teaches mitochondria and chloroplasts contain their own genomes, and the DddA-derived cytosine deaminase base editor induced base editing in lettuce or rapeseed calli at frequencies of up to 25% in mitochondria (abstract) and 38% in chloroplasts (i.e. therefore Kang teaches a plant genome comprising edited plant genomic DNA).
Regarding claim 7, Kang teaches rapeseed and lettuce protoplasts with base editing in in chloroplasts at frequencies of 15% and 30% respectively (p. 899, ¶4), and base editing in mitochondria at frequencies of 11% and 23% respectively (p. 900, ¶2) (i.e. therefore Kang teaches a plant cell comprising the edited plant genome).
Regarding claims 8-9, Kang teaches regenerating DNA-edited callus from the protoplasts, and further regenerating DNA-edited plants from the callus (abstract, Fig. 3f) (i.e. a plant comprising the plant cell, and also a method of producing a plant having the edited plant genome).
Regarding claim 21, Kang teaches the localization signal fused to the base-editing peptide used for base editing in the plant cells is a mitochondrial targeting sequence (p. 899, ¶3) (i.e. a mitochondrial localization signal peptide).
It would therefore have been obvious to a person of ordinary skill in the art to modify the invention taught by Mok to include the limitations of Kang and Kavipriya to arrive at the instantly claimed method with a reasonable expectation of success because Kang explicitly teaches the DddAtox cytidine deaminase-TALE complex taught by Mok can also be used to edit mitochondrial genomes of plant cells (title, abstract), and Kavipriya teaches various transient and stable transformation methods are available as functional alternatives. One having ordinary skill in the art would have been motivated to combine the teachings because Kang teaches successfully editing mitochondrial DNA in plants using the DddAtox-TALE base editor of Mok, and Kavipriya teaches PEG-induced DNA uptake (i.e. whether transient transfection or stable transformation) uses protoplasts which are often difficult to regenerate plants from (p. 286, ¶1, Table 2), a demerit not associated with other methods including the known, functionally equivalent methods for expressing plasmid DNA including stable transformation via agrobacterium-mediated transformation. Furthermore, it would have been obvious to apply the method of adding a nuclear localization signal for nuclear genome base editing as taught by Mok to plants and plant cells as taught by Kang for the same purpose that is targeted base editing of the nuclear genome in plants rather than mammalian cells.
Claims 1 and 20 are separately rejected under 35 U.S.C. 103 as being unpatentable over Mok (Mok, B. Y., de Moraes, M. H., Zeng, J., Bosch, D. E., Kotrys, A. V., Raguram, A., ... & Liu, D. R. (2020). A bacterial cytidine deaminase toxin enables CRISPR-free mitochondrial base editing. Nature, 583(7817), 631-637) and Zhang (US-20200181623-A1).
Claim 1 is drawn to a method for editing a plant genomic DNA, comprising converting a target nucleotide on the genomic DNA to another nucleotide, wherein the conversion is carried out with cytidine deaminase which is a protein described in the following (a) or (b):(a) a protein comprising the amino acid sequence as set forth in SEQ ID NO: 35; or (b) a protein comprising an amino acid sequence having a sequence identity of 90% or more to the amino acid sequence as set forth in SEQ ID NO: 35, and having cytidine deaminase activity, wherein an N-terminal portion of the cytidine deaminase and another portion are each fused with a different transcription activator-like effector (TALE), and wherein the conversion comprises introducing a DNA encoding a fusion protein comprising a part of or the entire cytidine deaminase and TALE, to which a nuclear localization signal peptide, a plastid localization signal peptide or a mitochondrial localization signal peptide is added, into a nuclear genome in a plant cell, and then allowing the signal peptide-added fusion protein to express in the plant cell.
Claim 20 is drawn to the method according to claim 1, wherein the conversion comprises introducing the DNA encoding the fusion protein comprising the part of or the entire cytidine deaminase and TALE, to which the plastid localization signal peptide is added, into the nuclear genome in the plant cell.
Regarding claim 1, Regarding claim 1, Mok teaches a cytidine deaminase polypeptide sequence (UniProt Accession No. AOA1V2VU04, published online 12/02/2020) that comprises an amino acid sequence with 100% identity to instant SEQ ID NO: 35 (see alignment in Office Action dated 04/29/2025). Mok also teaches the cytidine deaminase (named DddA) is split in half, wherein one half contains the C-terminus and the other half contains the N-terminus (p. 633, section titled Splitting DddAtox into non-toxic halves), and each portion is fused with a different TALE (Fig. 3a). Further, Mok also teaches the cytidine deaminase is used to edit genomes to convert C*G to T*A by expressing two halves of a cytidine deaminase (named DddA) that are fused to two different TALEs and also operably linked to a mitochondrial targeting signal (Fig. 3a and p. 634, section titled Mitochondrial base editing by TALE- DddAtox) in cells.
However, Mok does not explicitly teach:
The method is used for editing plant genomic DNA, and the conversion comprises introducing a DNA encoding a fusion protein comprising the cytidine deaminase and TALE into a nuclear genome in a plant cell, and then allowing the signal peptide-added fusion protein to express in the plant cell (remaining limitations of claim 1).
wherein the conversion comprises introducing the DNA encoding the fusion protein comprising the part of or the entire cytidine deaminase and TALE, to which the plastid localization signal peptide is added, into the nuclear genome in the plant cell (claim 20).
Regarding the remaining limitations of claim 1, in analogous art Zhang teaches a similar method of modifying a target locus of interest within a plant cell using cytidine deaminase, wherein the method modifies the cell by manipulation of one or more target sequences at genomic loci of interest (claims 1, 24, and 26 of Zhang), and the modified cell comprises a uracil or thymine in replacement of a cytosine in the target locus (claim 41 of Zhang). Zhang teaches in particular embodiments, the cytosine deaminase functionalized crispr system is introduced for stable integration into the genome of a plant cell, and the design of the transformation vector or the expression system can be adjusted depending on for when, where and under what conditions the guide RNA and/or fusion protein of cytidine deaminase and Cpf1 are expressed (¶0524). Zhang further teaches the fusion protein comprises a nuclear localization signal (claim 18 of Zhang).
Regarding claim 20, Zhang teaches alternatively, it is envisaged to target one or more of the CD-functionalized CRISPR components to the plant chloroplast by incorporating in the expression construct a sequence encoding a chloroplast transit peptide (CTP) or plastid transit peptide, operably linked to the 5′ region of the sequence encoding the fusion protein of cytidine deaminase and Cpf1 (¶0542).
It would therefore have been obvious to a person of ordinary skill in the art to modify the invention taught by Mok to include the limitations of Zhang to arrive at the instantly claimed method with a reasonable expectation of success because both inventions are directed to targeted base editing in cells using cytidine deaminases, and one of ordinary skill could apply the DddAtox-TALE cytidine deaminase of Mok to the method of editing chloroplast DNA of plant cells by incorporating a plastid localization signal as taught by Zhang without encountering any special technical difficulties. One having ordinary skill in the art would have been motivated to do so because it would be obvious to use one known cytidine deaminase base editor rather than another for the same purpose that is targeted nucleic acid editing (title) including targeting to the chloroplast as taught by Zhang (¶0542).
Response to Arguments
Applicant argues beginning on p. 7 of remarks dated 01/15/2026 the
following arguments:
Previously, Applicant noted that the method of Mok transiently expresses CD-TALE in animal cells using a plasmid, whereas the claimed method stably expresses CD-TALE in the nuclear genome of plant cells using the floral dip method, thereby introducing nucleotide substitutions in plastid and mitochondrial genomic DNA. The claimed method has high efficiency and avoids the risks associated with splitting DddAtox into two non-toxic halves. In reply, in the Office Action dated October 20, 2025, the Examiner stated that these were "mere conclusory statements" and also stated that transient transformation is usually a first experimental step, which is routinely followed by stable transformation using an appropriate localization signal. See pages 14 and 16.
In response, Applicant discusses this point with respect to Kang et al. (filed in IDS of September 15, 2023, and attached herewith), which is prior art with respect to embodiments relating the nuclear and mitochondrial genomes.
Kang discloses that the editing of the plant mitochondrial genome and the chloroplast genome was carried out by transient expression of DbCBE (corresponding to "TALECD" in the present application). Kang allows TALECD to transiently express by PEG transfection of plasmid DNA or mRNA, thus attempting to edit the mitochondrial genome and chloroplast genome of plants (see "Methods" of Kang). Kang discloses as follows:
Base edits induced by the DdCBE specific to the chloroplast or mitochondrial genes were detected in 22 out of 26 lettuce calli and 7 out of 14 rapeseed calli
with frequencies of up to 38% and 25%, respectively (Fig. 3c). See p. 900, right
column, lines 17-21.
The editing frequencies were at maximum 38% in chloroplasts and at maximum 25% in mitochondria, demonstrating significantly lower editing efficiency than the stable expression method of the present disclosure, which enables homoplasmic editing.
Kang also discloses as follows:
These results suggest that overexpression or prolonged, plasmid-based expression
of DdCBEs can give rise to off-target mutations and that transient, mRNA-based
expression using mRNA is desirable for avoiding off-target base editing.
See p. 903, right column, lines 6-10, emphasis added.
Thus, Kang states that in order to avoid off-target base editing, overexpression or long- term expression is undesirable, and that an mRNA-based transient expression method is desirable. This suggests that a long-term expression using a stable expression method is unacceptable.
Kang's last author, Dr. Jin-Soo Kim, is a researcher with an extremely large number of achievements in the field. Since Dr. Kim, as a skilled person, suggests that stable expression of TALECD is undesirable, it would have been commonly thought that even in a case where transient expression has been successfully carried out, desirable results cannot be necessarily obtained by stable expression.
In the telephone interview, the Examiners noted that Kang is not prior art, and could only be considered to teach away from stable expression if it is prior art to the application. However, Applicant notes that the July 2021 publication date of Kang is after the January 22, 2021 filing date of the Japanese priority document, but before the January 21, 2022 filing date of the PCT application. The subject matter relating to the plastid nuclearization signal was first disclosed in the Japanese priority document, and the subject matter of the nuclear localization signal and the mitochondrial localization signal were first disclosed in the PCT application. As per the request of the Examiners, Applicant herewith submits a verified translation of the Japanese priority document.
Additionally, Applicant notes that even if Kang is not prior art (i.e., with respect to the plastid subject matter), its disclosure may be characterized as a 'failure by others.' See MPEP 716.04.
Furthermore, Applicant now provides additional references which show that undesirable off-target effects were obtained when attempting stable expression. Specifically, Applicant cites to Modrzejewski et al. and Han et al. (enclosed), both of which discuss factors that affect the occurrence of off-target effects during genome editing. Modrzejewski focuses on plant genomes, while Han focuses on mammalian genomes. CRISPR-Cas is used as the genome editing tool. Both Modrezjewski and Han predate the filing date of the priority application.
In particular, Modrezjewski states as follows:
Stable transformation leads to a permanent expression of the CRISPR/Cas system compared to the transient approach in which the CRISPR/Cas system is available
only for a limited time. Therefore, it is supposed that a stable transformation
leads to an increased on-target as well as an increased off-target activity
(Zischewski et al., 2017; Metje-Sprink et al., 2018; Jansing et al., 2019).
See page 3, right column, lines 3-9, emphasis added.
This demonstrates that there have been concerns that stable expression in plant genome editing may increase off-target activity.
Meanwhile, Han states as follows:
Prolonged expression of the sgRNA and Cas9 nuclease due to the persistence of
plasmid DNA can also increase the potential of OTEs [88]. In addition,
introduction of foreign DNA can trigger cellular immune responses [89]. One
study proposed an engineered plasmid expression cassette to contain 2 sgRNAs,
one targeting the gene of interest and the other targeting the Cas9 itself [90].
Designed in this manner, the Cas9 transgene would be cleaved simultaneously
with the gene of interest, hence reducing the duration of Cas9 expression. As
expected, the Cas9 nuclease expression level was found to be diminished by post- treatment day 2 while measured off-target effects (OTEs) were significantly reduced correspondingly
[90]. See page 622, right column, lines 4-16, emphasis added.
The integration of an inducible promoter upstream of the tissue-specific promoter
can impose spatial and temporal control over Cas9 expression, culminating in lower OTE frequencies given that one of the determinants of OTE rates is the length of time the genome is exposed to the nuclease. See page 624, left column, lines 10-15, emphasis added.
As such, Han discloses that prolonging the expression of gRNA and Cas9 nuclease by plasmid DNA may increase the frequency of off-target activity, and that shortening the expression time of Cas9, i.e., shortening the expression time of the genome editing enzyme (equivalent to TALECD in this application), reduced the frequency of off-target activity. Furthermore, Han states that shortening the time the genome is exposed to the genome editing enzyme (nuclease in Han) by using an inducible promoter reduces the frequency of off-target activity. These findings in Han suggest that stable expression of genome editing enzymes may increase off-target activity and lead to undesirable results, even in genome editing of mammalian cells.
Together, Modrzejewski and Han, which are both published before the earliest priority date of this application, suggest that long-term expression (stable expression) of genome editing enzymes increases the frequency of off-target activity when editing the genomes of plants and animals. Therefore, these publications can be considered a teaching away from stable expression.
The structure of the claimed embodiments, in which the plant genome is edited by allowing TALECD to stably express, involves the possibility of off-target base editing. As shown by Kang, Modrzejewski and Han, those skilled in the art would avoid stable expression methods. However, despite the suggestion of Kang, Modrzejewski and Han, the inventors have introduced TALECD into the nuclear genome, and have shown excellent results also regarding off-target base editing, while using a stable expression method.
In other words, the specification discloses that the off-target base editing of the plastid genome, the mitochondrial genome and the nuclear genome is extremely low. See paragraphs [0073], [0089], and [0099]. The claimed method has realized very high base editing efficiency (homoplasmic editing).
According to the disclosed stable expression method, the introduced base editing is stably inherited by offspring such as T2 individuals, and it is possible to obtain individuals free from the gene introduced into the nuclear genome. See paragraphs [0074] and [0086]. Therefore, it is possible to eliminate the gene introduced into the nuclear genome, i.e., the TALECD expression construct, and to obtain offspring plants that inherit with high efficiency the edited base editing as is. This makes it possible to create plants with new functions, without being subject to international restrictions imposed by the Cartagena Act. This would not have been obvious in view of the cited art and the knowledge of one skilled in the art.
Accordingly, Applicant respectfully submits that the claimed embodiments are patentable over the cited art for at least the above reasons. Favorable reconsideration is respectfully requested.
This argument has been fully considered and is found not persuasive for
the following reason(s):
In view of the recently submitted certified English translation of the foreign priority document, the benefitted priority dates of the pending claims have been adjusted as described in the priority section above. As a result, the 35 USC 103 rejections have been modified since the previous Office Action dated 10/20/2025 based on the benefitted priority dates.
Applicant first points out in Kang that the editing frequencies were at maximum 38% in chloroplasts and at maximum 25% in mitochondria, demonstrating significantly lower editing efficiency than the stable expression method of the present disclosure, which enables homoplasmic editing. Applicant argues these frequencies are significantly lower than the instant application. Although Applicant may shower higher mutation frequencies in certain instances, these frequencies do not appear significantly greater than the prior art, especially given that the frequencies taught by Kang were not considered low frequencies in the field. Applicant also argues the stable expression enables homoplasmic editing, however there is no evidence from the Applicant or prior art that describes transient expression as unable to result in the homoplasmic editing. Even if such a showing existed, it would still be obvious to stably express the plasmids (see 103 rejection above) and the resulting homoplasmic editing would then be observed.
Applicant then essentially argues that Kang teaches away from stable expression, noting “Kang states that in order to avoid off-target base editing, overexpression or long- term expression is undesirable, and that an mRNA-based transient expression method is desirable. This suggests that a long-term expression using a stable expression method is unacceptable”. However, a known or obvious composition does not become patentable simply because it has been described as somewhat inferior to some other product for the same use." In re Gurley, 27 F.3d 551, 553, 31 USPQ2d 1130, 1132 (Fed. Cir. 1994) (See MPEP 2145.D.1). This same concept may be applied to the presented method. In the instant case, Kang states “These results suggest that overexpression or prolonged, plasmid-based expression of DdCBEs can give rise to off-target mutations and that transient, mRNA-based expression using mRNA is desirable for avoiding off-target base editing” (p. 903). Although Kang states prolonged expression can give rise to off target mutations and teaches transient expression is desirable for avoiding off-target mutations, Kang does not teach that stable or prolonged expression should not be used. It is further added that the off-target mutations Kang refers to are at low frequencies of 1.2% to 4.1% (p. 903). So although prolonged expression may result in very low frequencies of off-target mutations, this somewhat inferior method (i.e. stable expression of the plasmid) would be expected to produce the same result of targeted edited DNA. Therefore this obvious method does not constitute patentability because it has been described as somewhat inferior to another method for the same use. Applicant adds, similarly, Modrzejewski and Han teach stable expression of gene editing machinery may be an inferior method and increase the potential of off-target effects, However, they do not teach away from stable expression for the same reasons described above.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JESSICA N STOCKDALE whose telephone number is (703)756-5395. The examiner can normally be reached M-F 8:30-5:00 CT.
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JESSICA N. STOCKDALE
Examiner
Art Unit 1663
/JESSICA NICOLE STOCKDALE/Examiner, Art Unit 1663
/CHARLES LOGSDON/Primary Examiner, Art Unit 1662