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 .
DETAILED ACTION
Election/Restrictions
Applicant’s election without traverse of Group 1, claims 1-12, 14-15, and 18 in the reply filed on 08 December 2025 is acknowledged.
Claims 13 and 16 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 08 December 2025.
Claim Status
Claims 13 and 16 have been withdrawn, claim 17 has been cancelled, claims 1-12, 14-15, and 18 have been considered on their merits.
Claim Objections
Claim 10 is objected to because of the following informalities: The limitations regarding the order of the fusion protein are presented in the alternative, however, the alternatives are identical. It is recommended to either amend the limitations to be different or remove the alternative embodiment.
Appropriate correction is required.
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 15 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a target region of a sgRNA with a length of 10 to 30 nucleotides, does not reasonably provide enablement for a sgRNA with a length of 10 to 30 nucleotides. 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 the invention commensurate in scope with these claims.
The factors to be considered in determining whether undue experimentation is required are summarized In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988). The Court in Wands states: “Enablement is not precluded by the necessity for some 'experimentation.'” Clearly, enablement of a claimed invention cannot be predicated on the basis of quantity of experimentation required to make or use the invention. “Whether undue experimentation is needed is not a single simple factual determination, but rather is a conclusion reached by weighing many factual considerations.” (Wands, 8 USPQ2d 1404). The factors to be considered in determining whether undue experimentation is required include: (1) the quantity of experimentation necessary, (2) the amount or 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 claims. While all of these factors are considered, a sufficient amount for a prima facie case is discussed below.
SCOPE OF THE INVENTION
Claim 15 encompass a sgRNAs having a length of 10-30 nucleotides.
GUIDANCE & WORKING EXAMPLES
Regarding claim 15 encompassing a genus of sgRNAs between 10-30 nucleotides in length, the specification does not provide guidance for or a working example of a sgRNA limited to this length range.
By contrast Applicant specification discloses, the present inventors attempted to confirm the effect of the length of single guide RNA (sgRNA) on the indel efficiency of a base editor. Specifically, by extending 19 to 30 bases to each target site, sgRNAs with different lengths were constructed, indel efficiency was confirmed, and simultaneously, base editing efficiency, specificity, and editing windows of CBE and ABE variants at the target site were compared with each other (para. [0108]).
The specification discusses the length of the target site of the sgRNA with a length of 19-30 bases, this would suggest the 10-30 nucleotides disclosed in the claim is referring to the target site of the sgRNA, not the entire length of the sgRNA.
STATE OF THE ART & QUANTITY OF EXPERIMENTATION
Moreover, at the time of invention of the present application neither applicant’s specification nor the prior art provided guidance for making and using sgRNAs between 10-30 bases in length.
Specifically, the prior art of Zhang (US 2016/0175462) teaches making and using sgRNAs comprising about a 20 nucleotide targeting domain, followed by a scaffold of about 76 nucleotides (see Fig 31B of Zhang below).
PNG
media_image1.png
243
767
media_image1.png
Greyscale
[AltContent: textbox ([img-media_image2.png])]Furthermore, even when a sgRNA is not used, Zhang teaches that the length of a functional guide RNA would still be greater than 30 nucleotides in length. Specifically, Zhang teaches the target region alone is to be 20 nucleotides with a tracr sequence of at least 12 nucleotides, and then a corresponding crRNA sequence of at least another 12 nucleotides, and then additional tracr sequence to form a hairpin secondary structure necessary for Cas binding [0770, 0787-0793]. Zhang teaches the naturally occurring lengths of the crRNA is 39-42 nucleotides and the tracr RNA is 75-89 nucleotides [0957, 0959-0960], so as to create at least one stem loop structures for stable Cas9 binding (see Fig. 2A of Zhang).
Consequently, there is ample reason to conclude that there would be a high degree of unpredictability and undue experimentation in making and using a sgRNAs between 10-30 bases in length.
The physiological art is recognized as unpredictable (MPEP 2164.03). As set forth in In re Fisher, 166 USPQ 18 (CCPA 1970), compliance with 35 USC 112(a) requires: “That scope of claims must bear a reasonable correlation to scope of enablement provided by specification to persons of ordinary skill in the art; in cases involving predictable factors, such as mechanical or electrical elements, a single embodiment provides broad enablement in the sense that, once imagined, other embodiments can be made without difficulty and their performance characteristics predicted by resort to known scientific laws; in cases involving unpredictable factors, such as most chemical reactions and physiological activity, scope of enablement varies inversely with degree of unpredictability of factors involved.” Moreover, the courts have also stated that reasonable correlation must exist between scope of exclusive right to patent application and scope of enablement set forth in the patent application (27 USPQ2d 1662 Ex parte Maize!.). In view of the foregoing, due to the lack of sufficient guidance provided by the specification regarding the issues set forth above, the state of the relevant art, and the breadth of the claims, it would have required undue experimentation for one skilled in the art to make and use the instant broadly claimed invention.
CONCLUSION
In conclusion, given the breadth of the claims and the limited scope of the specification, an undue quantity of experimentation is required to make and use the invention.
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 6, 7, and 10 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.
Regarding claim 6, the claim recites the limitation “the CMP is located between the C-terminus of the fusion protein and/or the NLS peptide and the Cas9 protein.” This limitation is indefinite because it is unclear where the CMP is to be located because the CMP is to be located between two locations both locations would need to be recited. The limitations following “and/or” are presented in the alternative and therefore are not required. For the purposes of compact prosecution, the claim is interpreted as the CMP is located between the C-terminus of the fusion protein and the NLS peptide or the CMP is located between the NLS peptide and the C-terminus of the Cas9 protein.
Regarding claim 7, the claim recites the order of the gene editing fusion peptide from the N-terminus to the C-terminus of the fusion protein wherein the H1G and NLS peptides are required to be in different orientations simultaneously. Therefore, the scope of the claim is unclear because it is not clear how the fusion protein components are to be ordered.
For the purposes of compact prosecution, the claim is interpreted as wherein [NLS peptide]-[HN1]-[Cas9 protein]-[NLS peptide]-[HIG] or [NLS peptide]-[HN1]-[Cas9 protein]- [HIG]-[NLS peptide] are located in the order from the N-terminus to the C-terminus of the fusion protein.
Claim 10 recites the limitation " wherein [NLS peptide]-[HN1][dCas9 protein ]-[UGI peptide]-[UGI peptide ]-[NLS peptide ]-[H1G] are located in the order from the N-terminus to the C-terminus of the fusion protein" in the first through fifth line of the claim. There is insufficient antecedent basis for the NLS peptides, HN1 and H1G limitations in the claim. To obviate this rejection applicant is advised to modify the claim dependencies, as an example, change claim 8 dependency to depend from claim 7.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-3, 5, 11, and 14 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Fuqiang et al. (US 2019/0017042 A1, published 17 January 2019, IDS ref.)
Regarding claims 1 and 2, Fuqiang et al. teach CRISPR protein linked to at least one nucleosome interacting protein domain (para. [0006]). Fuqiang et al. teach the CRISPR protein has nuclease or nickase activity (para. [0008]). Fuqiang et al. teach at least one nucleosome interacting protein domain of the fusion protein can be a high mobility group (HMG) box (HMGB) DNA binding domain, a HMG nucleosome-binding (HMGN) protein, a central globular domain from a histone H1 variant, or a combination thereof (para. [0009]). Fuqiang et al. teach at least one nucleosome interacting protein domain of the fusion protein can be HMGN1 protein, histone H1 central globular domain (claim 2), or a combination thereof (para. [0009]). The HMGN1 protein and the histone H1 central globular domain read as chromatin-modulating peptides (CMPs) (claim 1).
Regarding claim 3, Fuqiang et al. teach the CRISPR protein of the fusion protein can be a CRISPR/Cas9 nuclease or nickase or can be CRISPR/Cas9 protein modified to lack all nuclease activity and linked to a non-nuclease domain, wherein the non-nuclease domain can have cytosine deaminase activity (para. [0017]). A CRISPR/Cas9 protein modified to lack all nuclease activity reads as dCas9.
Regarding claim 5, Fuqiang et al. teach Human HMGN1 was fused with SpCas9 (+NLS) at the nuclease carboxyl terminus with a linker between Cas9 and the HMGN peptide (para. [0198]).
Regarding claim 11, Fuqiang et al. teach introducing into a eukaryotic cell (a) at least one fusion protein or nucleic acid encoding at least one fusion protein, each fusion protein comprising a CRISPR protein linked to at least one nucleosome interacting protein domain, wherein the CRISPR protein (i) has nuclease or nickase activity or (ii) is modified to lack all nuclease activity and is linked to a non-nuclease domain and (b) at least one guide RNA or nucleic acid encoding at least one guide RNA (para. [0016]). Fuqiang et al. teach the guide RNA can be a single guide RNA (sgRNA), wherein the crRNA sequence is linked to the tracrRNA sequence (para. [0094]). Fuqiang et al. teach crRNA contains a guide sequence that hybridizes with the target sequence (para. [0089]). Fuqiang et al. teach nucleic acid encoding the fusion protein or the CRISPR protein and guide RNA of the complex can be present in a vector, to include plasmid vectors, viral vectors, and self-replicating RNA (para. [0101]). A plasmid vector comprising the nucleic acid encoding the CRISPR protein and guide RNA of the complex reads as a plasmid capable of expressing the sgRNA.
Regarding claim 14, Fuqiang et al. teach the nucleic acid encoding the fusion protein or the components of the complex or can be part of a viral vector, e.g., lentiviral vectors (para. [0101]).
Thus, the reference anticipates the subject matter of claims 1-3, 5, 11, and 14.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 4 and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Fuqiang et al. (US 2019/0017042 A1, published 17 January 2019, IDS ref.) as applied to claims 1-3, 5, 11, and 14 above, and further in view of Gaudelli et al. (Nature, vol 551, 2017).
Fuqiang et al. anticipate the subject matter of claims 1-3, 5, 11, and 14, and thus also, render them obvious.
Regarding claim 4, Fuqiang et al. teach the CRISPR protein has nuclease or nickase activity (para. [0008]).
However, Fuqiang et al. are silent to the fusion protein further comprising tRNA adenosine deaminase (TadA).
Gaudelli et al. teach a transfer RNA adenosine deaminase to operate on DNA when fused to a catalytically impaired CRISPR-Cas9 mutant (Abstract). Gaudelli et al. teach previously described base editors exploit the use of cytidine deaminase enzymes that operate on single-stranded DNA but reject double-stranded DNA (p. 465, 1st column). Gaudelli et al. teach utilization of ecTadA as the starting point to evolve a DNA adenine deaminase (p. 465, 1st column). Gaudelli et al. teach mammalian codon-optimized TadA–Cas9 nickase fusion construct that replaces dCas9 with the Cas9 D10A nickase to manipulate cellular DNA repair to favor the desired base editing outcomes, and adds a C-terminal nuclear localization signal (NLS) to create the TadA–XTEN–nCas9–NLS construct, wherein transfection of plasmids expressing said fusion protein and sgRNAs targeting six human genomic sites resulted in observable A-T to G-C editing efficiencies (p. 465, 2nd column).
Therefore, it would have been obvious to one of ordinary skill in the art to utilize TadA of Gaudelli et al. with the fusion protein of Fuqiang et al. with a reasonable expectation of success because Gaudelli et al. teach utilization of the TadA-nCas9 fusion protein resulted in observable editing efficiencies. One would be motivated to utilize TadA of Gaudelli et al. with the fusion protein of Fuqiang et al. because both references teach gene editing fusion proteins involving nCas9 and sgRNA.
Regarding claim 18, both Fuqiang et al. and Gaudelli et al. teach the gene editing fusion protein further comprises a NLS peptide.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Claims 6 and 7 are rejected under 35 U.S.C. 103 as being unpatentable over Fuqiang et al. (US 2019/0017042 A1, published 17 January 2019, IDS ref.) as applied to claims 1-3, 5, 11, and 14 above, and further in view of Hu et al. (G3, Volume 8, March 2018) and Luo et al. (Nucleic Acids Research, 2017, and supplemental information).
Fuqiang et al. anticipate the subject matter of claims 1-3, 5, 11, and 14, and thus also, render them obvious.
Regarding claim 6, Fuqiang et al. are silent to wherein [NLS peptide]-[Cas9protein]-[NLS peptide] are located in the order from an N-terminus to a C-terminus of the fusion protein.
However, Hu et al. teach the ability of Cas9 proteins with NLS fused to the N-, C-, or both the N- and C-termini and N-NLS-Cas9-NLS-C mRNA to target two different gene loci, concluding various NLS-fused Cas9 proteins and Cas9 mRNAs have similar genome editing efficiencies on targeting single or multiple genes (Abstract).
Luo et al. teach CRISPR/Cas9 system represents a gene targeting method with target flexibility made possible by computationally directed gRNA selection (p. 8419). Luo et al. teach dCas9 has been fused to transcriptional activators and repressors and nuclease domains and adding another NLS to create 2dCas9-PB improved nuclear localization (p. 8419, 2nd column). Luo et al. teach the pCMV-2dCas9-PB comprises NLS attached before and after the dCas9 as seen below (Fig. S1):
PNG
media_image3.png
38
417
media_image3.png
Greyscale
Therefore, it would have been obvious to one of ordinary skill in the art to include the second NLS at the N-terminus as taught by Hu et al. and Luo et al. with the Cas9 fusion protein of Fuqiang et al. with a reasonable expectation of success because using two NLS was known in the art and shown to improve nuclear localization of dCas9 as taught by Luo et al. One would have been motivated to include the second NLS at the N-terminus as taught by Hu et al. and Luo et al. with the Cas9 fusion protein of Fuqiang et al. because improved nuclear localization would improve Cas9 fusion proteins ability to be efficiently transported from the cytoplasm into the nucleus, which would increase editing efficiency and assist in overcoming cytoplasmic sequestering which would reduce the total amount of fusion protein required to achieve desirable results.
Regarding the limitation directed to the CMP being located between the C-terminus of the fusion protein and the NLS peptide or the Cas9 protein, Fuqiang et al. teach Human HMGN1 was fused with SpCas9 (+NLS) at the nuclease carboxyl terminus with a linker between Cas9 and the HMGN peptide wherein the NLS is located before the HMGN1 (para. [0198] and SEQ ID NO: 62). The HMGN1 reads as the CMP and therefore reads as the CMP is between the C-terminus end and the NLS.
Regarding claim 7, Fuqiang et al. teach fusion proteins comprising, from N to C terminus, HMGN1-SpCas9-NLS-Histone H1 globular fusion (H1G) (SEQ ID NO: 70 and para. [0201]). Therefore, Fuqiang et al. in view of Hu et al. and Luo et al. read on the limitations of the claim as adding an NLS at the N-terminus would be obvious in view of Hu et al. and Luo et al. as discussed in the rejection of claim 6. Thus, Fuqiang et al. in view of Hu et al. and Luo et al. teach a gene editing fusion protein where [NLS peptide]-[HN1]-[Cas9 protein]-[NLS peptide]-[H1G] are located in the order from the N-terminus to the C-terminus.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Claims 8, 9 and 12 are rejected under 35 U.S.C. 103 as being unpatentable over Fuqiang et al. (US 2019/0017042 A1, published 17 January 2019, IDS ref.) as applied to claims 1-3, 5, 11, and 14 above, and further in view of Wang et al. (Nature Biotechnology, Vol. 36, No. 10, October 2018).
Fuqiang et al. anticipate the subject matter of claims 1-3, 5, 11, and 14, and thus also, render them obvious.
Regarding claims 8 and 9, Fuqiang et al. do not teach wherein the fusion protein further comprises one or more uracil DNA-glycosylase inhibitor (UGI) peptides and wherein the UGI peptide is directly linked to the C-terminus of the dCas9 protein.
Wang et al. teach base editors (BEs), which combine a cytidine deaminase with Cas9, have been successfully applied to perform targeted base editing, including C-to-T edits (p. 946, 1st column). Wang et al. teach to further enhance the C-to-T base editing system, three copies of the 2A (self-cleaving peptide)-uracil DNA glycosylase inhibitor (UGI) sequence was fused to the C terminus (claims 8 and 9) of hA3A-BE3-Y130F and hA3A-BE3-Y132D to develop hA3A-eBE-Y130F and hA3A-eBE-Y132D (p. 949, 1st column). Wang et al. teach the Cas9 utilized with the fusion protein hA3A-BE3, was nCas9 (Fig. 1b). Wang et al. teach hA3A-eBE-Y130F and hA3A-eBE-Y132D mediated highly efficient base editing in narrowed editing windows compared to the original hA3A-BE3 in all contexts examined (p. 949, 2nd column).
Therefore, it would have been obvious to one of ordinary skill in the art to include the UGI peptide of Wang et al. linked to the C-terminus of the dCas9 protein of Fuqiang et al. with a reasonable expectation of success because Fuqiang et al. teach the CRISPR protein of the fusion protein can be a nCas9 or can be dCas9 and linked to a non-nuclease domain, wherein the non-nuclease domain can have cytosine deaminase activity (para. [0017]). Thus, one of ordinary skill would expect the UGI peptide to perform as Wang et al. described with dCas9 as Fuqiang et al. describes the utilization of either nCas9 or dCas9. One would be motivated to include the UGI peptide of Wang et al. linked to the C-terminus of the dCas9 protein of Fuqiang et al. because Wang et al. teach the addition of three copies of the UGI to the C-terminus further enhanced the C-to-T base editing system.
Regarding claim 12, Fuqiang et al. teach the fusion protein and sgRNA as set forth in the rejection of claim 11. Fuqiang et al. do not teach wherein the gene editing composition further comprises UGI. The teachings of Wang et al. have been set forth above.
Therefore, it would have been obvious to one of ordinary skill in the art to include the UGI peptide of Wang et al. linked to the C-terminus of the Cas9 fusion protein and sgRNA of Fuqiang et al. with a reasonable expectation of success because all of the reference teach gene editing fusion proteins and all the claimed elements were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in their respective functions, and the combination yielded nothing more than predictable results to one of ordinary skill in the art. See MPEP § 2143(I)(A). One would be motivated to include the UGI peptide of Wang et al. with the fusion protein of Fuqiang et al. because Wang et al. teach the addition of three copies of the UGI to the C-terminus further enhanced the C-to-T base editing system.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Claim 10 is rejected under 35 U.S.C. 103 as being unpatentable over Fuqiang et al. (US 2019/0017042 A1, published 17 January 2019, IDS ref.) in view of Wang et al. (Nature Biotechnology, Vol. 36, No. 10, October 2018) as applied to claims 8-9 and 12 above and further in view of Hu et al. (G3, Volume 8, March 2018) and Luo et al. (Nucleic Acids Research, 2017).
Fuqiang et al. anticipate the subject matter of claims 1-3, 5, 11, and 14, and thus also, render them obvious.
Regarding claim 10, Fuqiang et al. in view of Wang et al. teach a gene editing fusion protein comprising three copies of UGI peptide at the C-termini end of the dCas9 protein. The language of the claim does not limit the fusion protein to only two copies of the UGI peptide.
Fuqiang et al. in view of Hu et al. and Luo et al. teach a gene editing fusion protein where [NLS peptide]-[HN1]-[Cas9 protein]-[NLS peptide]-[H1G] are located in the order from the N-terminus to the C-terminus, as discussed in the rejection of claim 7 above.
Therefore, it would have been obvious to one of ordinary skill in the art to include the UGI peptide of Wang et al. with the fusion protein of Fuqiang et al. in view of Hu et al. and Luo et al. with a reasonable expectation of success because all of the reference teach gene editing fusion proteins and all the claimed elements were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in their respective functions, and the combination yielded nothing more than predictable results to one of ordinary skill in the art. See MPEP § 2143(I)(A). One would be motivated to include the UGI peptide of Wang et al. with the fusion protein of Fuqiang et al. in view of Hu et al. and Luo et al. because Wang et al. teach the addition of three copies of the UGI to the C-terminus further enhanced the C-to-T base editing system.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NICHOLAS A. HUMPHRIES whose telephone number is (703)756-5556. The examiner can normally be reached Monday - Friday, 7:30am - 4:30 pm.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, James Schultz can be reached at 571-272-0763. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/N.A.H./Examiner, Art Unit 1631
/LAURA SCHUBERG/Primary Examiner, Art Unit 1631