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 .
Application Status
This action is written in response to applicant’s correspondence received 20 January 2026. Claims 1-52 are currently pending. Claims 13-14, 16-48, and 52 are withdrawn from prosecution as being drawn to non-elected subject matter. Accordingly, claims 1-12, 15, and 49-51 are examined herein. The restriction requirement mailed 22 August 2024 is still deemed proper. Applicant's elected Groups I, claims 1-17 without traverse in the reply filed 22 November 2024. For the purposes of examination SEQ ID NOs 6-7 and 9 present in claim 6 have been rejoined into examination.
Applicant' s arguments have been thoroughly reviewed, but are not persuasive to place the claims in condition for allowance for the reasons that follow.
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 1-5 and 49-50 are rejected under 35 U.S.C. 103 as being unpatentable over Pernstitch (Protein expression and purification 101 (2014): 68-75) in view of PubChem (PubChem, SID 160645406 National Library of Medicine (2012)). This rejection is maintained.
Regarding claims 1, 5, and 49-50, Pernstitch is drawn to a study concerned with the expression, purification, and reconstitution of PcaK (i.e., a MFS aromatic acid antiporter) from Acinetobacter (Abstract). Pernstitch teaches that previous studies have demonstrated how a recombinant Escherichia coli cell line expressing PcaK from Pseudomonas putida was able to selectively transport 4-HB and protocatechuate (i.e., Pernstitch teaches that it is known in the art that modified E. coli cells can express heterologous PcaK and import substances into the modified cell) (pg. 68). Pernstitch teaches that PcaK’s dominant pathway in vivo is substrate import (pg. 74). Pernstitch teaches the use of a plasmid comprising a synthetic cDNA gene that encodes pcaK (i.e., Pernstitch teaches the use of an expression cassette comprising a promoter operably linked to a heterologous nucleic acid encoding a heterologous MFS aromatic acid antiporter transporter) (pg. 69). Pernstitch teaches that pcaK selectively imports certain substrates into a host cell in vivo in a culture (i.e., Pernstitch is interpreted as teaching that an E. coli cell comprising a pcaK transporter is able to import certain substrates at an increased rate compared to a cell not comprising pcaK) (pg. 74). Pernstitch teaches that pcaK is known to import 2,4-dihydroxybenzoate alongside other aromatic and non-aromatic acids (i.e., Pernstitch is interpreted as teaching that pcaK can import chemical substances that comprise 2,4-dihydroxybenzoate alongside other chemicals comprising different structures) (pg. 74; see Fig. 11).
Regarding claims 2-4, Pernstitch teaches that recombinant E. coli cells were able to express heterologously expressed PcaK and selectively transport compounds into the cells (pg. 68).
Pernstitch does not teach or suggest the use of an exogenous aromatic substrate olivetolate (Claim 1).
PubChem is drawn to the structure of 2,4-dihydroxy-6-pentylbenzoate (pg. 1). PubChem teaches that a synonym for 2,4-dihydroxy-6-pentylbenzoate is olivetolate (pg. 3). PubChem teaches that 2,4-dihydroxy-6-pentylbenzoate comprises a 2,4-dihydroxybenzoate motif (pg. 1).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the 2,4-dihydroxybenzoate of Pernstitch with the olivetolate of PubChem. A person of ordinary skill in the art would have had a reasonable expectation of success because Pernstitch teaches that pcaK can import 2,4- dihydroxybenzoate and PubChem teaches that olivetolate comprises a 2,4-dihydroxybenzoate motif. Further, Pernstitch teaches that pcaK has substrate specificity across different benzoate motifs, but not across different 2,4-dihydroxybenzoate motifs. Therefore, substituting the 2,4- dihydroxybenzoate of Pernstitch with the olivetolate of PubChem would have resulted in a predictable outcome of success.
Claim 6 is rejected under 35 U.S.C. 103 as being unpatentable over Pernstitch (Protein expression and purification 101 (2014): 68-75) in view of PubChem (PubChem, SID 160645406 National Library of Medicine (2012)) as applied to claims 1-5 and 49-50 above, and further in view of Adams (PG Pub No. US 2009/0100536 A1). This rejection is maintained.
Regarding claim 6, Pernstitch in view of PubChem renders obvious claims 1-5 and 49-50 as described above.
Pernstitch in view of PubChem dos not teach or suggest that the transporter is at least 90% identical to 100 contiguous amino acids of the sequence set forth in SEQ ID NO: 8 (Claim 6).
However, one of ordinary skill in the art would have considered the teachings of Adams as both references are analogous prior art pertaining to the use of polypeptide transporters.
Adams is drawn to an invention concerned with transgenic plant cells with recombinant DNA for expression of proteins (Abstract). Adams teaches the use of a polypeptide comprising 90.4% sequence identity to the claimed SEQ ID NO: 8 (Claim 2; see SEQ ID NO: 23744 in attached sequence alignment). In the sequence alignment previously provided, the sequence alignment identifies the SEQ ID NO: 23744 of Adams as being a pcaK polypeptide that has the function of a 4-hydroxybenzoate transporter and a benzoate transporter (see previously attached sequence alignment).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the pcaK polypeptide of Pernstitch in view of PubChem with the pcaK polypeptide of Adams. A person of ordinary skill in the art would have had a reasonable expectation of success because both references teach the use of a functional pcaK polypeptide. Therefore, substituting the pcaK polypeptide of Pernstitch in view of PubChem with the pcaK polypeptide of Adams would have resulted in the predictable outcome of success.
Claims 7-10 is/are rejected under 35 U.S.C. 103 as being unpatentable over Pernstitch (Protein expression and purification 101 (2014): 68-75) in view of PubChem (PubChem, SID 160645406 National Library of Medicine (2012)) as applied to claims 1-5 and 49-50 above, and further in view of Page (PG Pub No. US 2012/0144523 A1).
Regarding claims 7-10, Pernstitch in view of PubChem renders obvious claims 1-5 and 49-50 as described above.
Pernstitch in view of PubChem dos not teach or suggest that the host cell further comprises a heterologous aromatic prenyltransferase that is capable of prenylating the aromatic acid substrate and is a functional fragment of CBGAS that is at least 90% identical to SEQ ID NO: 3 (Claims 7-10).
However, one of ordinary skill in the art would have considered the teachings of Page as both references are analogous prior art pertaining to the use of olivetolate.
Page is drawn to an invention concerned with nucleic acid molecules from Cannabis sativa that have been isolated, characterized, and encode polypeptides having aromatic prenyltransferase activity (Abstract). Page teaches the use of an enzyme, CsPT1, that is a geranylpyrophosphate olivetolate geranyltransferase, active in the cannabinoid biosynthesis step of prenylation of olivetolic acid to form cannabigerolic acid (i.e., CsPT1 is an aromatic prenyltransferase that is capable of prenylating olivetolate) (Abstract). Page teaches the use of a CsPT1-395 enzyme that has 100% sequence identity to the claimed SEQ ID NO: 3 ([0063]; see SEQ ID NO: 2 in previously attached sequence alignment). Page teaches that a nucleic acid encoding the CsPT1 enzyme can be successfully transformed and expressed within E. coli ([0030]-[0031]).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the host cell of Pernstitch in view of PubChem such that the host cell further comprised a heterologous aromatic prenyltransferase that is capable of prenylating the aromatic acid substrate and is a functional fragment of CBGAS that is at least 50% identical to 100 contiguous amino acids of the sequence set forth in SEQ ID NO: 3, as described by Page. A person of ordinary skill in the art would have been motivated to do so in order to successfully prenylate the olivetolate substrate rendered obvious by Pernstitch in view of PubChem in order to generate cannabigerolic acid. A person of ordinary skill in the art would have had a reasonable expectation of success because Pernstitch in view of PubChem renders obvious an E. coli host cell comprising olivetolate and Page teaches the use of an a nucleic acid encoding a CsPT1 enzyme that can prenylate olivetolate.
Claims 11-12 are rejected under 35 U.S.C. 103 as being unpatentable over Pernstitch (Protein expression and purification 101 (2014): 68-75) in view of PubChem (PubChem, SID 160645406 National Library of Medicine (2012)) as applied to claims 1-5 and 49-50 above, and further in view of Gabrielsen (European journal of biochemistry 271.14 (2004): 3028-3035), Zhao (Annual review of biochemistry 82.1 (2013): 497-530), and Andre (Frontiers in plant science 7 (2016): 19). This rejection is maintained.
Regarding claims 11-12, Pernstitch in view of PubChem renders obvious claims 1-5 and 49-50 as described above.
Pernstitch in view of PubChem does not teach or suggest the use of an expression cassette comprising a promoter operably linked to a nucleic acid encoding ispDF (Claims 11-12).
However, one of ordinary skill in the art would have considered the teachings of Gabrielsen as both references are analogous prior art pertaining to the use of various enzymes and chemical compounds present in the MEP pathway.
Gabrielsen is drawn to a study concerned with the biosynthesis of isoprenoids (Abstract). Gabrielsen teaches the use of a plasmid comprising an expression cassette comprising a heterologous promoter operably linked to a nucleic acid encoding a bifunctional ispDF enzyme (i.e., a heterologous nucleic acid) that was successfully transformed into an E. coli strain (pg. 3029).
Zhao is drawn to a study concerned with the methylerythritol phosphate pathway (i.e., the MEP pathway) of isoprenoid biosynthesis (Abstract). Zhao teaches that ispD and ispF both play a role in the MEP pathway that ultimately produces IPP and DMAPP and that bifunctional ispDF proteins have been found in many proteins and possess the activity of both ispD and ispF (i.e., the activity of ispDF can be used in the production of IPP and DMAPP) (pg. 2-3; see Figure 1c).
Andre is drawn to a study concerned with biochemical pathways present in Cannabis sativa (Abstract). Andre teaches that IPP, DMAPP, and olivetolate are important chemicals present in pathways that ultimately produce cannabinoids and secondary metabolites (pg. 3; see Figure 2).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the host cell of Pernstitch in view of PubChem such that an expression cassette comprising a promoter operably linked to a nucleic acid encoding ispDF was utilized in the cell, as described by Gabrielsen, Zhao, and Andre. A person of ordinary skill in the art would have been motived to do so in order to successfully produce IPP, DMAPP, and olivetolate in a host cell in order to produce cannabinoids and secondary metabolites. A person of ordinary skill in the art would have had a reasonable expectation of success because Pernstitch in view of PubChem teaches the use of an E. coli host cell while Gabrielsen teaches the use of a plasmid comprising an expression cassette comprising a heterologous promoter operably linked to a nucleic acid encoding a bifunctional ispDF enzyme that was successfully transformed into an E. coli strain.
Claims 15 and 51 are rejected under 35 U.S.C. 103 as being unpatentable over Pernstitch (Protein expression and purification 101 (2014): 68-75) in view of PubChem (PubChem, SID 160645406 National Library of Medicine (2012)) as applied to claims 1-5 above, and further in view of Hermsen (Molecular systems biology 11.4 (2015): 801). This rejection is maintained.
Regarding claims 15 and 51, Pernstitch in view of PubChem renders obvious claims 1-5 as described above.
Pernstitch in view of PubChem does not teach or suggest that the host cell is in a culture medium comprising a substrate selected from olivetolate, DVA, olivetol, or divarinol (Claims 15 and 51).
However, one of ordinary skill in the art would have considered the teachings of Hermsen as both references are analogous prior art pertaining to the study of E. coli.
Hermsen is drawn to a study concerned with how culture medium comprising a carbon substrate affects the growth of E. coli (Abstract). Hermsen teaches that E. coli can successfully be cultured in a medium comprising a substate of interest such that the substrate is uptaken by the host cells (pg. 2). Hermsen teaches that in biotechnical applications, growing E. coli in a mixed culture medium comprising at least two different substrates is preferred (pg. 5).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the culture medium of Pernstitch in view of PubChem such that the culture mcdium comprised a substrate of interest (i.e., the exogenous aromatic substrate), as described by Hermsen. A person of ordinary skill in the art would have been motived to do so in order to utilize a preferred growth culture medium for E. coli and to grow the host cells directly alongside the substrate of interest. A person of ordinary skill in the art would have had a reasonable expectation of success because both Pernstitch in view of PubChem and Hermsen teach the successful growth of E. coli via the use of different culture mediums. Therefore, modifying the culture medium of Pernstitch in view of PubChem such that the culture medium comprised a substrate of interest (i.e., the exogenous aromatic substrate), as described by Hermsen, would have resulted in the predicable outcome of success.
Response to Arguments
Applicant's arguments filed 20 January 2026 have been fully considered but they are not found persuasive.
Applicant alleges that the PubChem reference relied upon by the Office shows an improper chemical structure lacking the hydroxyl groups present in olivetolate and instead shows oxygen atoms as substituents of the benzyl ring, but without charge notation or the necessary hydrogens (Remarks; pg. 9-10). Applicant alleges that the reference to olivetolate is as a synonym, as noted by the reference itself, “is presented as provided to PubChem by the source (depositor)” (Remarks; pg. 9-10). Therefore, Applicant alleges that the information in the PubChem reference relied up on by the Office Action is not subject to verification or confirmation and is contrary to the well-known structure of olivetolate (Remarks; pg. 9-10).
These arguments are not found persuasive because the relied upon PubChem reference correctly shows the charge notion of an oxygen atom without a corresponding hydrogen. The lack of “OH” notation present in the PubChem reference’s benzyl ring being evidence of the reference not teaching the structure of olivetolate is not a persuasive argument because there exists a correctly notated lone oxygen atom that comprises a negative charge. Therefore, one of ordinary skill in the art would interpret the two neutrally charged oxygen atoms that are substituents of the benzyl ring in the PubChem reference as hydroxyl groups and that the PubChem reference teaches the well-known structure of olivetolate. Further, the reference to the structure as olivetolate in the reference by the depositor is merely a recitation of the well-known name of a well-known structure.
Applicant alleges that Pernstitch does not disclose or suggest that its modified E. coli cells can import certain substrates at an increased rate, let alone at any rate (Remarks; pg. 10-11). Applicant alleges that there is no disclosure or suggestion in Pernstitch that the E. coli cells were competent to transport substrates via the pcaK transporter (Remarks; pg. 10-11). Applicant alleges that Pernstitch does not teach substrate import in the E. coli cell, rather, Pernstitch comments on substrate import being the dominant pathway in vivo referring to the activity of pcaK in its native form, not heterologously expressed in a host cell (Remarks; pg. 10-11). Applicant notes that the only reference in Pernstitch for transport in E. coli cells is for the transport of protocatechuate and 4-HB in other studies (Remarks; pg. 10-11).
These arguments are not found persuasive because Pernstitch explicitly teaches that a previous study has demonstrated that a recombinant Escherichia coli cell line expressing PcaK from Pseudomonas putida was able to selectively transport 4-HB and protocatechuate (pg. 68). Because the teaching was from another study does not detract from the fact that Pernstitch teaches that a heterologous PcaK can be expressed within an E. coli cell and is able to import substances into the cell. Although Pernstitch as a study is drawn towards an in vitro assay, the reference also teaches that PcaK’s dominant pathway in vivo is substrate import and the purpose of Pernstitch’s study is to closely examine how PcaK imports substances and how its activity would work when present within a host cell (pg. 74).
Applicant alleges that the Office further misinterprets Pernstitch as teaching that pcaK can import chemical substances that comprise 2-4,dihydroxybenzoate (Remarks; pg. 11-12). Applicant alleges that Pernstitch does not suggest that pcaK can transport substituted hydroxylbenzoates and that the reference suggests that additional substituents may be deleterious to transport efficiency (Remarks; pg. 11-12). Applicant alleges that none of the compounds tested in Pernstitch have an alkyl substitution nor is there any discussion or suggestion that compounds outside of those tested would or could be efficiently transported by pcaK (Remarks; pg. 11-12). Applicant alleges that nowhere is there any suggestion in Pernstitch to specifically select a pentyl-substituted hydroxybenzoate such as olivetolate (Remarks; pg. 11-12).
These arguments are not found persuasive because Pernstitch teaches that one of the study’s findings was that “PcaK can transport a variety of aromatic acids with hydroxyl substitutions at the 2-, 3- and 4-positions, with the 2- and 4-positions being favored” (pg. 74). Pernstitch further teaches that PcaK is capable of transporting 8 different substances, with a preference for a 2,4-DHB (pg. 74; see Fig. 11). Although Pernstitch does teach that certain substituents may be deleterious to transport efficiency, Pernstitch does not teach that PcaK is incapable of transporting the substituents nor that the E. coli cell could not import olivetolate. Further, MPEP 716.01(c) makes clear that arguments of counsel cannot take the place of evidence in the record.
One of ordinary skill in the art would have interpreted the teachings of Pernstitch as teaching that PcaK is capable of importing aromatic acids with hydroxyl substitutions at the 2- and 4-positions. One of ordinary skill in the art would not interpret the teachings of Pernstitch as narrowly as alleged by Applicant because Pernstitch teaches that PcaK is capable of transporting a variety of compounds, including aromatic acids and non-aromatic acids (pg. 74; see Fig. 11). However, if further evidence to the contrary (i.e., factually supported evidence objective evidence that PcaK is incapable of transporting aromatic acids with alkyl substitutions) is provided, further consideration will be given to this argument.
With regard to the lack of motivation present in Pernstitch and in the pending 35 USC 103 rejection of record of claims 1-5 and 49-50, MPEP 2143(I)(B) teaches that a motivation statement is not explicitly required in order to make a rejection based on the simple substitution rationale. MPEP 2144 teaches that the references do not have to explicitly suggest to combine the teachings. Rather, establishing a prima facie case of obviousness requires a clear articulation of a rationale for combining the teachings of the references, and such rationale has been provided in the rejection above.
Applicant alleges that the Office uses improper hindsight to arrive at the claimed invention (Remarks; pg. 12).
This argument is not found persuasive because it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
Applicant alleges that the instant application demonstrates the unexpected results of E. coli cells expressing the heterologously expressed pcaK increased the uptake of olivetolate inside the cells compared to control cells (Remarks; pg. 13). Applicant alleges that the instant application demonstrates the unexpected results of increasing CGBA in vivo in the presence of olivetolate (Remarks; pg.13).
Regarding the increased uptake of olivetolate, the results demonstrated by applicant are expected in view of the prior art. Since Pernstitch teaches that pcaK can be heterologously expressed within E. coli cells in order to import compounds of interest into the cells, and pcaK’s main function is to import a variety of aromatic acids with hydroxyl substitutions at the 2-, 3-, and 4- positions, with the 2- and 4- position being favored, one of ordinary skill in the art would have expected a recombinant E. coli that expresses the transporter to be able to import an aromatic acid comprising a 2,4-dihydroxybenzoate motif at a higher rate compared to a control host cell that does not express the transporter.
In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., the increased production of CBGA in vivo) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Applicant alleges that the Office Action fails to articulate any reason why one of ordinary skill in the art would specifically select the claimed SEQ ID NO: 23744 that has at least 90% identity to the claimed SEQ ID NO: 8 from the tens of thousands of sequences in Adams and there is no motivation to select the claimed SEQ ID NO: 8.
This argument is not found pervasive because, as discussed above, the previously provided sequence alignment of Adams identifies the polypeptide as a pcaK polypeptide that ahs the function of a 4-hydroxybenzoate transporter and a benzoate transporter (see previously attached sequence alignment).
Further, MPEP 2143(I)(B) teaches that a motivation statement is not explicitly required in order to make a rejection based on the simple substitution rationale. Further, MPEP 2144 teaches that the references do not have to explicitly suggest to combine the teachings. Rather, establishing a prima facie case of obviousness requires a clear articulation of a rationale for combining the teachings of the references, and such rationale has been provided in the rejection above.
Applicant alleges that one of ordinary skill in the art would not have been motivated to have included olivetolate in the culture medium because Hermsen is drawn towards a study concerned with optimizing the growth conditions of E. coli cells.
This argument is not found persuasive because Hermsen’s teachings were relied upon for the disclosure that growing E. coli cells in mediums that comprise substrates that are intended to be uptaken by the E. coli cells is a known method and advantageous method of introducing substrates of interest to the host cells.
Additionally, applicant has provided only arguments of counsel, and arguments of counsel cannot take the place of factually supported objective evidence. See, e.g., In re Huang, 100 F.3d 135,139-40, 40 USPQ2d 1685, 1689 (Fed. Cir. 1996); In re De Blauwe, 736 F.2d 699, 705, 222 USPQ 191, 196 (Fed. Cir. 1984).
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to KYLE T REGA whose telephone number is (571)272-2073. The examiner can normally be reached M-R 8:30-4:30, every other F 8:30-4:30 (EDT/EST).
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Neil Hammell can be reached at 571-270-5919. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/KYLE T REGA/Examiner, Art Unit 1636
/NEIL P HAMMELL/Supervisory Patent Examiner, Art Unit 1636
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