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 .
Priority
This application claims benefit of priority to Provisional Application 63/071,630 filed 08/28/2020 and is also a 371 of PCT/US2021/047694 filed 08/26/2021. Support for the instant claims is found in Provisional Application 63/071,630, therefore, for the purposes of applying prior art, the effective filing date of the claimed invention is 08/28/2020.
Information Disclosure Statement
The Information Disclosure Statement filed 02/28/2023 has been acknowledged and considered.
Drawings
The drawings are objected to because multiple figures are blurry and illegible, specifically Figures 2 and 11. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Election/Restrictions
Applicant’s election without traverse of Group I in the reply filed on 08/27/2025 is acknowledged.
Regarding the species elections, Applicant’s election without traverse of V396A with respect to SEQ ID NO: 1 as the specific ADS substitution, V64L with respect to SEQ ID NO: 3 as the specific AO substitution, A82V with respect to SEQ ID NO: 6 as the specific ADH substitution, SEQ ID NO: 9 as the specific enzyme with DBR activity and SEQ ID NO: 369 as the specific enzymes for converting AA or DHAA to artemisinin in the reply filed on 08/27/2025 is acknowledged.
Claim Status
As stated immediately above, Applicant elected Group I, claims 1-3, 7, 9, 11, 16, 18, 22-25, 30, 32, 34-35, 39-40 and 47-49. Additionally, claim 47 is not encompassed by Applicant’s election of species of SEQ ID NO: 369 as the specific enzyme for converting AA or DHAA to artemisinin. Therefore, claims 47, 58, 63, 66-67, 77, 91 and 101 are withdrawn by the Examiner as they are not encompassed by the elected group/species.
Claims 1-3, 7, 9, 11, 16, 18, 22-25, 30, 32, 34-35, 39-40, 47-49, 58, 63, 66-67, 77, 91 and 101 are currently pending.
Claims 47, 58, 63, 66-67, 77, 91 and 101 are withdrawn.
Claims 1-3, 7, 9, 11, 16, 18, 22-25, 30, 32, 34-35, 39-40 and 48-49 are under examination.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 39-40 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 39 recites “the microbial cell of claim 1, further comprising a heterologous enzyme having a double bond reductase (DBR) activity” in lines 1-2. Claim 1, the claim from which claim 39 depends, states “a microbial host cell … comprising … a heterologous enzyme having a double bond reductase activity (DBR)” in lines 1-5 of the claim. Thus, claim 39 fails to further limit the subject matter of the claim upon which it depends because claim 1 already requires a heterologous enzyme having a double bond reductase activity.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 102
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, 11, 22-23 and 39-40 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Vainstein et al. (WO 2012156976 A1, 11/22/2012).
Regarding claims 1 and 39, Vainstein et al. disclose methods for generating and/or increasing content of artemisinin in a cell (See entire document, Abstract). Vainstein et al. further disclose:
a cell comprising a heterologous polynucleotide, wherein said heterologous polynucleotide comprises:
(i) a polynucleotide comprising a nucleic acid sequence encoding amorphadiene synthase (ADS) which catalyzes the formation of amorpha-4,11-diene from farnesyl diphosphate (FDP); and
(ii) a polynucleotide comprising a nucleic acid sequence encoding artemisinic aldehyde delta- 11(13) reductase (DBR2) which catalyzes reduction of artemisinic aldehyde to dihydroartemisinic aldehyde; and
(iii) a polynucleotide comprising a nucleic acid sequence encoding amorpha- 4,11-diene monooxygenase (CYP71AV1) which catalyzes oxidation of amorpha-4,11- diene and/or artemisinic alcohol (Claim 3 of Vainstein et al.).
Additionally, the cell is a yeast cell, a microbial cell or a fungal cell (Page 24, Lines 5-6).
Thus, Vainstein et al. anticipate instant claims 1 and 39 insofar as disclosing a cell comprising multiple heterologous polynucleotides, wherein the cell is a microbial cell, comprising a nucleic acid sequence encoding an amorphadiene synthase, reading on a heterologous enzyme having amorphadiene synthase activity (ADS), a nucleic acid sequence encoding artemisinic aldehyde delta-11(13) reductase, reading on a heterologous enzyme having double bond reductase activity (DBR), and a nucleic acid sequence encoding amorpha-4,11-diene monooxygenase, reading on a heterologous enzyme having amorphadiene oxidase activity (AO).
Regarding claims 2-3, Vainstein et al. disclose amorphadiene synthase (ADS) refers to a polypeptide which catalyzes formation of amorpha-4,11-diene from farnesyl diphosphate (Page 15, Lines 10-12). Vainstein et al. further disclose the ADS is encoded by a nucleic acid sequence encoding a polypeptide with at least 80%, up to 100%, homology to the polypeptide set forth in SEQ ID NO: 11 (Page 15, Lines 21-26). SEQ ID NO: 11 of Vainstein et al. shares 100% sequence identity to instant SEQ ID NO: 1. An alignment is provided below wherein Qy is instant SEQ ID NO: 1 and Db is SEQ ID NO: 11 of Vainstein et al.
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Regarding claim 11, Vainstein et al. disclose amorpha-4,11-diene monooxygenase refers to a polypeptide which catalyzes oxidation of amorpha-4,11-diene and/or artemisinic alcohol (Page 18, Lines 1-3). Vainstein et al. further disclose the amorpha-4,11-diene monooxygenase, or CYP71AV1, is encoded by a nucleic acid sequence encoding a polypeptide with at least 80%, up to 100%, homology to the polypeptide set forth in SEQ ID NO: 16 (Page 18, Lines 20-23). SEQ ID NO: 16 of Vainstein et al. shares 98.6% sequence identity to instant SEQ ID NO: 3, reading on an amino acid sequence of SEQ ID NO: 3 and a variant of SEQ ID NO: 3. An alignment is provided below wherein Qy is instant SEQ ID NO: 3 and Db is SEQ ID NO: 16 of Vainstein et al.
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Regarding claim 22, Vainstein et al. disclose the cell of claim 3 further comprises a heterologous polynucleotide comprising a nucleic acid sequence encoding cytochrome P450 reductase (CPR) which catalyzes the reduction of cytochrome P450 (Claim 13 of Vainstein et al.).
Regarding claim 23, Vainstein et al. disclose the cytochrome P450 reductase comprises a nucleic acid sequence encoding a polypeptide having at least 80%, and up to 100%, sequence identity to SEQ ID NO: 31 (Page 19, Lines 25-30). SEQ ID NO: 31 of Vainstein et al. shares 99.8% sequence identity to instant SEQ ID NO: 5, reading on a variant of instant SEQ ID NO: 5. An alignment is provided below wherein Qy is instant SEQ ID NO: 5 and Db is SEQ ID NO: 31 of Vainstein et al.
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Regarding claim 40, Vainstein et al. disclose the artemisinic aldehyde delta-11(13) reductase (DBR2) refers to a polypeptide which catalyzes the reduction of artemisinic aldehyde to dihydroartemisinic aldehyde (Page 17, Lines 7-9). The DBR2 of the invention comprises a nucleic acid sequence encoding a polypeptide having at least 80%, up to 100%, sequence identity to SEQ ID NO: 14 (Page 17, Lines 14-18). SEQ ID NO: 14 of Vainstein et al. shares 99.6% sequence identity and 100% local similarity to instant SEQ ID NO: 9, reading on an amino acid sequence of SEQ ID NO: 9 and a variant of SEQ ID NO: 9. An alignment is provided below wherein Qy is instant SEQ ID NO: 9 and Db is SEQ ID NO: 14 of Vainstein et al.
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Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
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 1-3, 11, 22-23, 34 and 39-40 are rejected under 35 U.S.C. 103 as being unpatentable over Vainstein et al. (WO 2012156976 A1, 11/22/2012).
The teachings of Vainstein et al. are discussed above.
Regarding claim 34, Vainstein et al. disclose aldehyde dehydrogenase (ALDH1) is involved in the oxidation of artemisinic and dihydroartemisinic aldehydes to their corresponding acids (Page 2, Lines 21-23). Vainstein et al. further discloses additional enzymes that can be incorporated into the invention include aldehyde dehydrogenase 1 (Page 22, Lines 25-27).
Vainstein et al. do not explicitly disclose their cell comprises ALD1.
However, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have incorporated ALD1 into the cell of Vainstein et al. motivated by the desire to convert artemisinic and/or dihydroartemisinic aldehyde to its corresponding acid because this is a step in the production of artemisinin as disclosed by Vainstein et al. and the cell of Vainstein et al. is directed to the production of artemisinin. Additionally, it would have obvious to incorporate ALD1 into the cell of Vainstein et al. because Vainstein et al. specifically state ALD1 can be incorporated into their cell.
Claims 1-3, 7, 9, 11, 22-23, 34 and 39-40 are rejected under 35 U.S.C. 103 as being unpatentable over Vainstein et al. (WO 2012156976 A1, 11/22/2012) in view of UniProt (M4GGS1_ARTAN, 05/01/2013).
The teachings of Vainstein et al. are discussed above.
Regarding claims 7 and 9, Vainstein et al. do not disclose the ADS comprises a V369A substitution.
However, UniProt discloses M4GGS1_ARTAN, an amorpha-4,11-diene synthase from Artemisia annua (Top of Page 1) which shares 83.1% sequence identity to SEQ ID NO: 11 of Vainstein et al. and instant SEQ ID NO: 1 and also has an alanine (A) at the position corresponding 396 of instant SEQ ID NO: 1. An alignment is provided below wherein Qy is instant SEQ ID NO: 1 and Db is M4GGS1_ARTAN of UniProt.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the ADS disclosed by UniProt, being M4GGS1_ARTAN, in the cell of Vainstein et al. because Vainstein et al. specifically disclose the ADS in their recombinant cell shares at least 80% sequence identity to their SEQ ID NO: 11 and the ADS disclosed by UniProt was a known and effective ADS with 83.1% sequence identity to SEQ ID NO: 11 of Vainstein et al. and instant SEQ ID NO: 1. It is reiterated, as stated above, that instant SEQ ID NO: 1 and SEQ ID NO: 11 of Vainstein et al. share 100% sequence identity.
It is noted, as stated above in the Election/Restriction section, Applicant elected V396A as the one or more specific substitutions in ADS. Therefore, regarding claims 7 and 9, only substitution V396A is addressed as that is the only elected substitution.
Claims 1-3, 11, 16, 18, 22-23, 34 and 39-40 are rejected under 35 U.S.C. 103 as being unpatentable over Vainstein et al. (WO 2012156976 A1, 11/22/2012) in view of UniProt (K7ZNY7_9ASTR, 02/16/2013).
The teachings of Vainstein et al. are discussed above.
Regarding claims 16 and 18, Vainstein et al. do not disclose the AO comprises a V64L substitution.
However, UniProt discloses K7ZNY7_9ASTR, a putative cytochrome P450 monooxygenase CYP71AV1 from Artemisia chamaemelifolia (Top of Page 1) which shares 90.4% sequence identity to instant SEQ ID NO: 3 and also has a leucine (L) at the position corresponding 64 of instant SEQ ID NO: 1. An alignment is provided below wherein Qy is instant SEQ ID NO: 1 and Db is K7ZNY7_9ASTR of UniProt.
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Additionally, K7ZNY7_9ASTR of UniProt shares 89.3% sequence identity to SEQ ID NO: 16 of Vainstein et al. An alignment is provided below wherein Qy is K7ZNY7_9ASTR of UniProt and Db is SEQ ID NO: 16 of Vainstein et al.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the AO disclosed by UniProt, being K7ZNY7_9ASTR, in the cell of Vainstein et al. because Vainstein et al. specifically disclose the AO in their recombinant cell shares at least 80% sequence identity to their SEQ ID NO: 16 and the AO disclosed by UniProt was a known and effective AO with 89.3% sequence identity to SEQ ID NO: 11 of Vainstein et al.
Claims 1-3, 11, 22-24, 34 and 39-40 are rejected under 35 U.S.C. 103 as being unpatentable over Vainstein et al. (WO 2012156976 A1, 11/22/2012) in view of Zhang et al. (US 20100299778 A1, 11/25/2010).
The teachings of Vainstein et al. are discussed above.
Regarding claim 24, Vainstein et al. do not disclose their host cell comprises a heterologous enzyme having alcohol dehydrogenase activity.
However, Zhang et al. disclose plant-derived compounds of health and commercial interest, more specifically, nucleotide sequences encoding enzymes that are used for producing dihydroartemisinic aldehyde, dihydroartemisinic acid and/or artemisinin (Paragraph [0002]). Zhang et al. further disclose an important step in the pathway to artemisinin is the reduction of artemisinic aldehyde to (11R)-dihydroartemisinic aldehyde (Paragraph [0029]). The genes involved in the reduction of artemisinic aldehyde to (11R)-dihydroartemisinic aldehyde include farnesyl diphosphate synthase, amorpha-4,11-diene synthase, amorpha-4,11-diene hydroxylase, alcohol dehydrogenase and aldehyde dehydrogenase (Paragraph [0029]).
Thus, 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 included a nucleotide sequence encoding an alcohol dehydrogenase in the cell of Vainstein et al. motivated by the desire to effectively reduce artemisinic aldehyde to (11R)-dihydroartemisinic aldehyde as it is a step in the production of artemisinin as taught by Zhang et al. with a reasonable expectation of success.
Claims 1-3, 11, 22-25, 30, 32, 34 and 39-40 are rejected under 35 U.S.C. 103 as being unpatentable over Vainstein et al. (WO 2012156976 A1, 11/22/2012) in view of Zhang et al. (US 20100299778 A1, 11/25/2010) and further in view of UniProt (A0A2U1KRU6_ARTAN, 07/18/2018).
The teachings of Vainstein et al. and Zhang et al. are discussed above.
Regarding claims 25, 30 and 32, neither Vainstein et al. nor Zhang et al. disclose the aldehyde dehydrogenase comprises an amino acid sequence of instant SEQ ID NO: 6 or a variant thereof, wherein the amino acid sequence has an A82V substitution.
However, UniProt discloses A0A2U1KRU6_ARTAN, an alcohol dehydrogenase from Artemisia annua (Top of Page 1). A0A2U1KRU6_ARTAN of UniProt shares 77.3% sequence identity, and 99.3% local similarity, to instant SEQ ID NO: 6, reading on a variant of instant SEQ ID NO: 6, and also has a valine (V) at position 82 corresponding to instant SEQ ID NO: 6.
As discussed above, 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 included a nucleotide sequence encoding an alcohol dehydrogenase in the cell of Vainstein et al. motivated by the desire to effectively reduce artemisinic aldehyde to (11R)-dihydroartemisinic aldehyde and produce artemisinin as taught by Zhang et al. with a reasonable expectation of success.
It would have been further obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the alcohol dehydrogenase A0A2U1KRU6_ARTAN in the cell of Vainstein et al. because a specific alcohol dehydrogenase is not required and A0A2U1KRU6_ARTAN was a known and effective alcohol dehydrogenase as taught by UniProt.
Claims 1-3, 11, 22-23, 34-35 and 39-40 are rejected under 35 U.S.C. 103 as being unpatentable over Vainstein et al. (WO 2012156976 A1, 11/22/2012) in view of Teoh et al. (US 20090265804 A1, 10/22/2009).
The teachings of Vainstein et al. are discussed above.
Regarding claim 35, Vainstein et al. do not disclose the aldehyde dehydrogenase comprises the amino acid sequence of SEQ ID NO: 8 or a variant thereof.
However, Teoh et al. disclose nucleic acid molecules, and the enzymes encoded thereby, useful for producing dihydroartemsinic aldehyde, dihydroartemisinic acid or artemisinic acid in a host cell (See entire document, Abstract). Teoh et al. further disclose an artemisinic/dihydroartemisinic aldehyde dehydrogenase with the sequence identifier of SEQ ID NO: 6 (Claim 5 of Teoh et al.). SEQ ID NO: 6 of Teoh et al. shares 99.7% sequence identity to instant SEQ ID NO: 8, reading on a variant of SEQ ID NO: 8. A sequence alignment is provided below wherein Qy is instant SEQ ID NO: 8 and Db is SEQ ID NO: 6 of Teoh et al.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the aldehyde dehydrogenase disclosed by Teoh et al. in the cell of Vainstein et al. because a specific aldehyde dehydrogenase is not required and the aldehyde dehyrogenase of Teoh et al. was a known and effective aldehyde dehydrogenase for producing dihydroartemsinic aldehyde, dihydroartemisinic acid or artemisinic acid in a host cell as taught by Teoh et al.
Claims 1-3, 11, 22-23, 34, 39-40 and 48-49 are rejected under 35 U.S.C. 103 as being unpatentable over Vainstein et al. (WO 2012156976 A1, 11/22/2012) in view of Seotaert et al. (BMC Plant Biology, 12/20/2013) and UniProt (A0A2U1M3G2_ARTAN, 07/18/2018).
The teachings of Vainstein et al. are discussed above.
Regarding claims 48-49, Vainstein et al. do not disclose the cell further expresses a heterologous enzyme having at least 70% sequence identity to instant SEQ ID NO: 369.
However, Seotart et al. disclose an important breakthrough in determining artemisinin biosynthesis was the localization of artemisinin production to the glandular trichomes of Artemisia annua (Page 1, Right Column, Paragraph 2). There are multiple genes known to be involved in the biosynthesis of artemisinin including CYP71AV1, ALDH1, DBR2 and ADH1 (Page 2, Left Column, Paragraph 1). Seotart et al. further state the enzymes involved in artemisinin biosynthesis are known up to the formation of dihydroartemisinic acid (DHAA) but it is not yet clear whether the last steps from DHAA involve a spontaneous auto-oxidation or if the last steps are catalyzed by enzymes (Page 2, Left Column, Paragraph 2). To find candidate genes that catalyze the last steps to artemisinin, Seotart et al. compared filamentous and glandular trichomes from A. annua (Page 3, Left Column, Paragraph 3). The comparison revealed several cytochromes, peroxidases and dioxygenases that are potentially involved in the biosynthesis of artemisinin that are upregulated in the glandular trichomes (Page 2, Left Column, Paragraph 2). Specifically, two dioxygenases both annotated as naringenin 2-oxoglutarate 3-dioxygenase (Page 8, Right Column, Paragraph 2).
Additionally, UniProt discloses A0A2U1M3G2_ARTAN, a non-heme dioxygenase N-terminal domain containing protein from Artemisia annua (Top of Page 1). UniProt further discloses A0A2U1M3G2_ARTAN reacts with 2-oxoglutarate (Page 1, Catalytic Activity) and contains specific 2-oxoglutarate dependent domains (Page 4, Family and domain databases). A0A2U1M3G2_ARTAN disclosed by UniProt shares 100% sequence identity to instant SEQ ID NO: 369. A sequence alignment is provided below wherein Qy is instant SEQ ID NO: 369 and Db is A0A2U1M3G2_ARTAN disclosed by UniProt.
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Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized A0A2U1M3G2_ARTAN disclosed by UniProt in the cell of Vainstein et al. motivated by the desire to effectively produce artemisinin. It would have been obvious to utilize A0A2U1M3G2_ARTAN disclosed by UniProt in the cell of Vainstein et al. because A0A2U1M3G2_ARTAN is a dioxygenase from A. annua containing specific 2-oxoglutarate dependent domains and Soetaert et al. specifically disclose two 2-oxoglutarate dioxygenases are significantly more expressed in the glandular trichomes of A. annua, the part of A. annua that synthesizes artemisinin, and therefore, are potential enzymes that can catalyze the final steps in artemisinin biosynthesis, converting DHAA to artemisinin. Thus, it would have been obvious to utilize A0A2U1M3G2_ARTAN because it is a dioxygenase from A. annua with specific 2-oxoglutarate dependent domains in the cell of Vainstein et al.
Conclusion
Claims 1-3, 7, 9, 11, 16, 18, 22-25, 30, 32, 34-35, 39-40 and 48-49 are rejected.
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ASHLEY T WHITE whose telephone number is (571)272-0683. The examiner can normally be reached Monday - Friday 8:30 - 5:00 EST.
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/A.T.W./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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