DETAILED ACTION
Applicant’s Preliminary Amendment, filed 11/14/2023, is acknowledged. Claims 1-63 are canceled. Claims 64-83 are newly added and pending in the instant application.
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 .
Priority
The instant application is a U.S. National Phase of PCT/US2022/029326, filed 5/13/2022, and claims Domestic Benefit to U.S. Provisional Application No. 63/188,648, filed 5/14/2021.
Election/Restrictions
Applicant’s election of Group I, claims 64-82, and SEQ ID NO: 38 from Genus A, SEQ ID NO: 4 from Genus B, SEQ ID NO: 65 from Genus C, SEQ ID NO: 107 from Genus D, and SEQ ID NO: 92 from Genus E, in the reply filed on 4/3/2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). Claims 65-68 and 83 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention and species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 4/3/2026.
Claims 64 and 69-82 are the subject of this office action.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 11/14/2023, 10/29/2024, 3/18/2025, 7/25/2025, 9/4/2025, and 1/8/2026 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Specification
The disclosure is objected to because of the following informalities:
Tables 2, 4, 9-12, and 14 are cutoff at the last column.
Appropriate correction is required.
Claim Objections
Claims 64, 76, 78, 80, and 82 are objected to because of the following informalities:
Claims 64, 76, 78, 80, and 82 inconsistently recite an enzyme name or sequence ID number followed by the sequence ID number or enzyme name, respectively, in parentheses. Since it is clear that the enzyme names and sequence ID numbers refer to the same thing, the claims are not rejected under 35 U.S.C. 112(b). However, it is not necessary to recite the enzyme names in the claims and only the sequence ID numbers should be recited in the claims.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 64 and 69-82 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention.
Scope of the claimed genus. Claim 64 is drawn to a recombinant aromatic prenyltransferase (APT) comprising an amino acid sequence having at least one amino acid modification as compared to a naturally occurring membrane-bound or aromatic prenyltransferase, wherein the APT comprises an amino acid sequence with at least 90% identity to SEQ ID NOs: 37, 38, or 39, or a functional fragment or variant thereof. A functional fragment or variant thereof as recited in the claims fails to receive written description support.
Claim 76 is drawn to polypeptides having geranyl diphosphate synthase activity comprising a polypeptide of SEQ ID NOs: 4-6, or a functional fragment or variant thereof.
State of the prior art. Functional fragments or variants of aromatic prenyltransferases having at least 90% identity to SEQ ID NOs: 37-39 are not described in the art at the time of the invention.
Mori (J. Nat. Med., 2020, Vol. 74, pp.501-512) discloses that aromatic prenyltransferases have been isolated in plants and microorganisms such as bacteria and fungi (see Abstract, p.501, left column, 1st passage and right column, 2nd passage). Two main types of aromatic prenyltransferases exist in bacteria and fungi, characterized by distinct structural signatures (see p.501, last passage,-p.502, left column, 1st passage, and Fig. 1). A certain level of promiscuity exists for aromatic prenyltransferases in regards to the substrates and conversion products (see p.502, passage bridging left and right columns, p.505, right column, 2nd passage, Fig. 2, and Table 1). More than 15 crystal structures of aromatic prenyltransferases have been reported, and the majority of mutations have been single and double point mutations that retain function (see p.506, right column, last passage,-p.509, left column, last paragraph). However, no sequence conservations associated with structure and function of the aromatic prenyltransferases have been set forth.
Functional fragments or variants of SEQ ID NOs: 4-6 are not described in the prior art at the time of the invention.
Zhao et al. (Appl. Microbiol. Biotechnol., 2016, Vol. 100, pp.4561-4571) demonstrates mutants of the GPP synthase ERG20, all having single or double point mutations (see Abstract). Functional fragments of GPP synthases have not been adequately described in the art.
Summary of species disclosed in the original specification. MPEP § 2163 states that a “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
SEQ ID NOs: 37-39 are the only aromatic prenyltransferases set forth in the description. SEQ ID NO: 37 and 38 are 99.5% identical. SEQ ID NO: 37 and 39 are 94.2% identical. SEQ ID NO: 38 and 39 are 94.4% identical. No functional fragments or variants of SEQ ID Nos: 37-39 are set forth in the specification.
SEQ ID NOs: 4-6 are the only geranyl diphosphate synthases set forth in the description. SEQ ID NOs: 4 and 5 are 10.2% identical. SEQ ID NOs: 4 and 6 are 5.4% identical. SEQ ID NOs: 5 and 6 are 12.5% identical. A person of ordinary skill in the art would not be able to discern any similarity among the disclosed GPP synthases.
Given the potential variability encompassed by the genus, this disclosure cannot be considered representative of the genus.
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied by disclosure of relevant, identifying characteristics; i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. As noted above, the art teaches that aromatic prenyltransferases are divided in two major types characterized by a broad spectrum of substrates and structures. The only variant GPP synthases described in the art have single or double point mutations. The specification does not set forth any sequence conservation that must be retained in any functional fragment or variant of SEQ ID NOs: 37-39. The specification does not set forth any conservation that must be retained in a functional fragment or variant of SEQ ID NOs: 4-6.
For all the reasons presented above, one of skill in the art would not know which of the possible fragments or variants of SEQ ID NOs: 37-39 would remain functional as aromatic prenyltransferases, which of the possible fragments or variants of SEQ ID NOs: 4-6 would remain functional as geranyl diphosphate synthases, or which of the possible functional fragments or variants of fused aromatic prenyltransferases and geranyl diphosphate synthases would remain functional. Therefore, the skilled artisan would not reasonably conclude that the inventors, at the time the application was filed, had full possession of the genus of functional fragment or variants as broadly claimed.
Given the lack of disclosure of a structure/function relationship, the description of zero functional fragment or variant species, applicant was not in possession of the invention as claimed.
Applicant may overcome this rejection by removing every recitation of “functional fragment or variant thereof” in claims 64, 76, and 78.
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)(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 64, 69, 72, and 74 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Bourgeois et al. (US2022/0259603; effectively filed 5/21/2020) as evidenced by Krivoruchko et al. (Metabol. Engin., 2015, Vol. 28, pp.28-42).
Regarding claim 64, Bourgeois teaches the protein PT42 comprising the sequence SEQ ID NO: 65 which has 96.2% sequence identity to SEQ ID NO: 38 of the claimed invention (see paragraphs [0261]-[0278] and Tables 14 and 16; see Appendix B, p.1-2, for sequence alignment).
Regarding claim 69, Bourgeois teaches the expression of PT42 comprising SEQ ID NO: 65 in E. coli BL21 (DE3) and the production of CBGA in the presence of GPP and OA (see paragraphs [0261]-[0278], specifically paragraphs [0265] and [0275]).
Regarding claim 72, Bourgeois teaches an E. coli BL21 (DE3) host cell (see paragraphs [0261]-[0278]). Krivoruchko provides evidence that acetyl-CoA is produced in E. coli from acetic acid, a carboxylic acid (see p/28, right column, 1st paragraph, and Fig. 2).
Regarding claim 74, Bourgeois teaches the host cell may be a yeast cell that expresses PT42 comprising SEQ ID NO: 65 (see paragraphs [0232]-[0233]).
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.
Claim 70 is rejected under 35 U.S.C. 103 as being unpatentable over Bourgeois et al. (US2022/0259603; effectively filed 5/21/2020) as evidenced by Krivoruchko et al. (Metabol. Engin., 2015, Vol. 28, pp.28-42), as applied to claims 64, 69, 72, and 74 above, and further in view of Yadav et al. (WO2020/176998).
Bourgeois teaches the invention of claims 64 and 69 as outlined in the rejection above.
Regarding claim 70, Bourgeois does not teach wherein the cell expresses an exogenous membrane transporter that improves OA or DVA uptake.
Yadav teaches membrane transporters that increase the transport of extracellular aromatic prenyltransferase substrates such as divarinolic acid and olivetolic acid to improve cannabinoid production in a host cell (see Abstract and paragraphs [0006] and [0010]).
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have further expressed an membrane transporter that increases transport of extracellular olivetolic acid to improve cannabinoid production in a host cell, as taught by Yadav, in the E. coli host cell expressing PT42, as taught by Bourgeois, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to improve the internalization of extracellular prenyltransferase substrate olivetolic acid to improve cannabinoid production by the prenyltransferase PT42 expressed in the E. coli of Bourgeois, yielding predictable results. Thus, claim 70 is prima facie obvious.
Claim 71 is rejected under 35 U.S.C. 103 as being unpatentable over Bourgeois et al. (US2022/0259603; effectively filed 5/21/2020) in view of Yadav et al. (WO2020/176998) as evidenced by Krivoruchko et al. (Metabol. Engin., 2015, Vol. 28, pp.28-42) as applied to claims 64, 69-70, 72, and 74 above, and further in view of Noble et al. (WO2020160289).
Bourgeois in view of Yadav teach the invention of claim 70 as outlined in the rejection above.
Regarding claim 71, Bourgeois and Yadav do not teach wherein one or more genes in the cell encoding a protein that exports OA or DVA is down-regulated or deactivated.
Noble teaches cells engineered to produce a cannabinoid in which genes encoding lactone transporters that may transport PDAL, HTAL, or other OA derivative byproduct molecules out of the cell (see p.11, lines 16-18). This is interpreted as preventing the transport of OA molecules and derivatives out of the host cell.
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to further disrupt genes encoding lactone transporters that may transport OA molecules out of the cell, as taught by Noble, in the E. coli cell expressing PT42 and an exogenous membrane transporter of OA, as taught by Bourgeois in view of Yadav, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to prevent OA transported into the cell by the exogenous membrane transporter to be exported back out of the cell, yielding predictable results. One of ordinary skill in the art would have been motivated to retain the imported OA for cannabinoid synthesis. Thus, claim 71 is prima facie obvious over Bourgeois in view of Yadav and Noble.
Claim 73 is rejected under 35 U.S.C. 103 as being unpatentable over Bourgeois et al. (US2022/0259603; effectively filed 5/21/2020) as evidenced by Krivoruchko et al. (Metabol. Engin., 2015, Vol. 28, pp.28-42), as applied to claims 64, 69, 72, and 74 above, and further in view of Carvalho et al. (FEMS Yeast Res., 2017, Vol. 17, fox037, pp.1-11).
Bourgeois teaches the invention of claims 64 and 69 as outlined in the rejection above.
Regarding claim 73, Bourgeois does not teach wherein the cell encodes an exogenous hexanoyl-CoA synthetase and/or butyryl-CoA synthase.
Carvalho teaches hexanoyl-CoA synthetase 1 isolated from the transcriptome of glandular trichomes is most likely the enzyme responsible for the formation of hexanoyl-CoA for the cannabinoid pathway (see p.3, right column, 1st paragraph). Carvalho teaches it may be beneficial to introduce a Cannabis hexanoyl-CoA synthetase or a homolog from another organism to achieve an efficient conversion of hexanoic acid to hexanoyl-CoA in yeast engineered for cannabinoid production (see Abstract, paragraph bridging pp.2-3, and p.5, right column, 3rd paragraph). Table 2 discloses E. coli is established for hexanoic acid engineering.
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to further express an exogenous hexanoyl-CoA synthetase, as taught by Carvalho, in the E. coli expressing PT42 that produces CBGA, as taught by Bourgeois, to arrive at the claimed invention. One of ordinary skill in the art would have been applying known engineering techniques for heterologous cannabinoid biosynthesis in a host organism, yielding predictable results. There would have been a reasonable expectation of success since hexanoic acid engineering was established in E. coli at the time of the invention. Thus, claim 73 is prima facie obvious over Bourgeois in view of Carvalho.
Claims 75 and 79 is rejected under 35 U.S.C. 103 as being unpatentable over Bourgeois et al. (US2022/0259603; effectively filed 5/21/2020) as evidenced by Krivoruchko et al. (Metabol. Engin., 2015, Vol. 28, pp.28-42), as applied to claims 64, 69, 72, and 74 above, and further in view of Blatt-Janmaat et al. (Int. J. Mol. Sci., 2021, Vol. 22, 2454, pp.1-19) and Aalbers et al. (CemBioChem, 2019, Vol. 20, pp.20-28).
Bourgeois teaches the invention of claim 64 as outlined in the rejection above.
Bourgeois teaches olivetolic acid and GPP are precursors for the production of CBGA (see Figs. 2 and 5).
Regarding claim 75, Bourgeois does not teach wherein the APT is fused with a polypeptide having geranyl diphosphate synthase activity.
Blatt-Janmaat teaches E. coli for cannabinoid production such as CBGA effectively express enzymes for the cannabinoid synthesis and that GPPS can be overexpressed in E. coli for cannabinoid production (see p.12, 3rd paragraph).
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have further overexpressed GPPS in cannabinoid producing E. coli, as taught by Blatt-Janmaat, in the E. coli that produces CBGA, as taught by Bourgeois, to arrive at the claimed invention. One of ordinary skill in the art would have been applying known engineering techniques for heterologous cannabinoid biosynthesis in E. coli, yielding predictable results. There would have been a reasonable expectation of success since effective cannabinoid production and expression of enzymes was established in E. coli at the time of the invention.
Blatt-Janmaat does not teach wherein the APT is fused with a polypeptide having geranyl diphosphate synthase activity.
Aalbers teaches enzyme fusions enables efficient cascade reactions for biosynthesis of specific compounds requiring multiple enzymes (see Abstract and p.20, left column, 1st passage,-right column, last paragraph).
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have fused the GPPS polypeptide to the PT42 polypeptide expressed in E. coli for CBGA production, as taught by Bourgeois in view of Blatt-Janmaat, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to efficiently produce CBGA by coupling the cascade reactions of the precursor molecules olivetolic acid and GPP to a fused enzyme, yielding predictable results. Thus, claim 75 is prima facie obvious over Bourgeois in view of Blatt-Janmaat and Aalbers.
Regarding claim 79, Bourgeois teaches E. coli can produce olivetol, a cannabinoid precursor, when fed hexanoic acid and expresses acyl-CoA synthase and polyketide cyclase (see paragraphs [0387]-[0390]). Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have further fused acyl-CoA synthase and polyketide cyclase to PT42 and GPPS to enable the E. coli cell to produce olivetol which is a precursor in cannabinoid synthesis, yielding predictable results.
Claims 76-78 are rejected under 35 U.S.C. 103 as being unpatentable over Bourgeois et al. (US2022/0259603; effectively filed 5/21/2020) in view of Blatt-Janmaat et al. (Int. J. Mol. Sci., 2021, Vol. 22, 2454, pp.1-19) and Aalbers et al. (CemBioChem, 2019, Vol. 20, pp.20-28) as evidenced by Krivoruchko et al. (Metabol. Engin., 2015, Vol. 28, pp.28-42), as applied to claims 64, 69, 72, 74-75, and 79 above, and further in view of Mikheev et al. (WO2022/051433; effectively filed 9/1/2020).
Bourgeois in view of Blatt-Janmaat and Aalbers teach the invention of claim 75 as outline in the rejection above.
Regarding claim 76, Bourgeois, Blatt-Janmaat, and Aalbers do not teach wherein the polypeptide having geranyl diphosphate synthase activity comprises a polypeptide of SEQ ID NO: 4 or a functional fragment thereof.
Mikheev teaches ERG20 converts GPP to FPP (see paragraph [00140]). Mikheev teaches the mutated Y. lipolytica ERG20 comprising SEQ ID NO: 36, which has 100% sequence identity to SEQ ID NO: 4 of the claimed invention, for the heterologous production of cannabinoids (see paragraph [00221] and Appendix B – pp.3-5). Thus, Mikheev apparently teaches a GPP synthase.
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have substituted Y. lipolytica ERG20 comprising SEQ ID NO: 36, as taught by Mikheev, for the GPPS fused to PT42, as taught by Bourgeois in view of Blatt-Janmaat and Aalbers, to arrive at the claimed invention. One of ordinary skill in the art would have been substituting known GPPS useful for cannabinoid production, yielding predictable results. Thus, claim 76 is prima facie obvious over Bourgeois in view of Blatt-Janmaat, Aalbers, and Mikheev.
Regarding claim 77, Aalbers teaches it is common to introduce a sequence coding for a peptide linker between enzyme fusions to affect the orientation of the two enzymes (see p.20, right column, 1st paragraph). Therefore, it would have been obvious to fuse the PT42 enzyme and the Y. lipolytica ERG20 comprising SEQ ID NO: 36 enzyme with a linker between the enzymes, as this is common practice in the relevant technical field. The resulting fusion protein thus reads on a functional variant of SEQ ID NO: 65 as recited in claim 78.
Claims 80-81 are rejected under 35 U.S.C. 103 as being unpatentable over Bourgeois et al. (US2022/0259603; effectively filed 5/21/2020) in view of Blatt-Janmaat et al. (Int. J. Mol. Sci., 2021, Vol. 22, 2454, pp.1-19) and Aalbers et al. (CemBioChem, 2019, Vol. 20, pp.20-28) as evidenced by Krivoruchko et al. (Metabol. Engin., 2015, Vol. 28, pp.28-42), as applied to claims 64, 69, 72, 74-75, and 79 above, and further in view of Horwitz et al. (WO2020069214).
Bourgeois in view of Blatt-Janmaat and Aalbers teach the invention of claim 79 as outline in the rejection above.
Regarding claim 80, Bourgeois, Blatt-Janmaat, and Aalbers do not teach wherein the polypeptide having polyketide cyclase activity comprises a polypeptide sequence having at least 90% identity to the polypeptide sequence of SEQ ID NO: 107.
Horwitz teaches modified host cells that produce a cannabinoid and teaches expressing the olivetolic acid cyclase (OAC) polypeptide comprising SEQ ID NO: 215 in the cell (see Abstract and paragraphs [0006] and [0060]). SEQ ID NO: 215 has 100% sequence identity to SEQ ID NO: 107 of the claimed invention (see Appendix B – pp.6-8).
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have substituted OAC comprising SEQ ID NO: 215, as taught by Horwitz, for the polyketide cyclase in the fusion protein of PT42 and Y. lipolytica ERG20 comprising SEQ ID NO: 36, as taught by Bourgeois in view of Blatt-Janmaat and Aalbers, to arrive at the claimed invention. One of ordinary skill in the art would have been substituting known cyclases useful in the technical field for heterologous cannabinoid production, yielding predictable results.
Regarding claim 81, Bourgeois in view of Blatt-Janmaat, Aalbers, and Horwitz teach each and every structural requirement of the claim is expected to improve production of CBGA as compared to a control membrane bound prenyltransferase, absent evidence to the contrary.
Thus, claims 80 and 81 are prima facie obvious over Bourgeois in view of Blatt-Janmaat, Aalbers, and Horwitz.
Allowable Subject Matter
The following is a statement of reasons for the indication of allowable subject matter: the sequences of claim 82 are free of the prior art.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JOHN PAUL SELWANES whose telephone number is (571)272-9346. The examiner can normally be reached Mon-Fri 7:30-5:00.
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/J.P.S./ Examiner, Art Unit 1651
/MELENIE L GORDON/Supervisory Patent Examiner, Art Unit 1651
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