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 .
Claim Status
1. Claims 1-6 are pending and examined to the extent of the elected species of SEQ ID NO:203.
Claims 7-16 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on May 15, 2026.
Restrictions/Elections
2. The Office acknowledges receipt of Applicant’s restriction election filed May 15, 2026. Applicant elects Group I, claims 1-6, drawn to an HPPD mutant comprising an alanine, glycine, or valine substitution at the amino acid position corresponding to position F372 and a tryptophan substitution at position F383 of SEQ ID NO:1, with traverse. Applicant further elects the species of SEQ ID NO:203, with traverse.
Applicant traverses primarily that the cited art does not specifically disclose the claimed mutations (p. 02, fourth paragraph) and that the Examples of the instant specification as filed demonstrate synergistic effects from the combination of the specific recited mutations (p. 02, paragraphs 5-6).
Applicant’s argument has been fully considered but is not persuasive because the claims are rejected under 35 U.S.C. 103 and, therefore, lack novelty and unity of invention in view of the prior art (see below). Thus, the shared technical feature of a mutant HPPD comprising a mutation at the position corresponding to positions F372 and F383 of SEQ ID NO:1 is not a special technical feature as this feature does not make a contribution over the prior art.
The requirement is deemed proper and is made FINAL.
However, method claims may be rejoined in accordance with In re Ochiai when allowability is indicated.
Priority
3. The instant Application is a 371 of Internation Application No. PCT/CN2021/138425 filed December 15, 2021.
Information Disclosure Statement
4. The Information Disclosure Statements (IDS) submitted on January 02, 2025, May 13, 2025, and September 05, 2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDS have been considered to the extent of the English translations provided. Signed copies are attached.
Specification
5. The specification is objected to because of the following:
On p. 03, the sentence comprised within lns. 14-17 does not end with a period. Similarly, the sentence comprised within p. 03, lns. 34-38 does not end with a period. Applicant appears to make a similar error repeatedly throughout the specification wherein the following statement begins with the word “Preferably”. See p. 05, lns. 1-16 and p. 05, lns. 46-51 for a non-exhaustive list of such examples. A close and careful review is requested.
Correction and/or clarification is required.
Claim Objections
6. Claims 2-3 are objected to because claim 2, ln. 5 comprises a typographical and/or grammatical error. It is recommended “mutation” be amended to “mutations” because multiple options are listed.
Dependent claims are included. Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
7. 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.
8. Claims 1-6 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 claims 1 and 2, the word “preferably” renders the claims indefinite because it is unclear whether the limitations following “preferably” are claim limitations. Descriptions of examples and preferences is properly set forth in the specification rather than in a single claim. See MPEP 2173.05(c) and MPEP 2173.05(d).
The metes and bounds of claim 2 are indefinite because it is unclear how many mutations are comprised within the polypeptide of claim 2. Claim 2 recites the additional limitation of a second mutation to the polypeptide of claim 1, however, the polypeptide of claim 1 already comprises two mutations (i.e., the first mutation at position 372 and the second mutation at position 383). Therefore, claim 2 appears to simply restate a limitation of claim 1. It is also unclear if the mutations recited within claim 2 are intended to replace either of the mutations recited in claim 1. If claim 1 comprises two mutations, then the additional mutation recited in claim 2 would be a third or additional mutation. If claim 2 is not intended to recite a third mutation in addition to the two mutations recited in claim 1, then claims 2-3 may be subject to rejection under 35 U.S.C. 112(d).
The scope of claim 4 is indefinite because it is unclear what is encompassed by a polypeptide “derived” from an HPPD. It is unclear what features/structures are retained in the claimed polypeptide in comparison to the polypeptide from which the claimed peptide is derived. It is unclear if the mutated polypeptide sequence was discovered in/obtained from, and therefore natively present in, the recited plant or microorganism.
Dependent claims are included. Appropriate correction is required.
Claim Rejections - 35 USC § 103
9. 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.
10. Claims 1-6 are rejected under 35 U.S.C. 103 as being unpatentable over Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
Hawkes 2014 discloses a mutant HPPD, which retains the HPPD catalytic activity and is less sensitive to an HPPD-inhibitor herbicide than the native, unmutated HPPD[0006]. Hawkes 2014 discloses the mutations may comprise any substitution at position F372 of SEQ ID NO:27[0039], which is identical to the instant SEQ ID NO:1, and may further comprise a substitution at position 383[0042]. Hawkes 2014 also discloses a polynucleotide sequence and expression vector encoding the mutant HPPD and a method for co-expressing the HPPD with another protein to produce an HDDP inhibitor-resistant plant[0085], [0117], [0146].
Regarding claim 1, Hawkes 2014 teaches a mutant HPPD polypeptide, which retains the activity of catalyzing the reaction of transforming 4-hydroxyphenylpyruvic acid into homogentisic acid or homogentisate and is less sensitive to an HPPD-inhibitor herbicide than the native, unmutated HPPD of SEQ ID NO:27, wherein the mutant HPPD comprises one or more mutations[0006] including at position 372, wherein F372 is substituted with any other amino acid[0039] and a mutation at position F383, wherein F383 is substituted with any other amino acid[0042].
Hawkes 2019 teaches the development of transgenic crops with improved resistance to HPPD-inhibitor herbicides (p. 10, first full paragraph); conserved amino acid residues and regions involved in inhibitor binding in HPPD polypeptides from Arabidopsis thaliana, soybean, and Avena sativa (p. 11, Figure 2); the structure of mutated HPPD polypeptides comprising one or more substitutions and/or mutations affecting the sensitivity to HPPD-inhibitor herbicides (p. 18, Table 2); that amino acid residues F372, F383, and K351 are each in close proximity to the HPPD inhibitor binding site (p. 19, “3.2.1. Generation and detection of improved mutants”); and that multiple mutations could be combined together to create sufficiently functional HPPD polypeptides with high levels of herbicide tolerance (p. 19, “3.2.1. Generation and detection of improved mutants”, last paragraph; p. 20, left column, first partial paragraph).
Additionally, Fritze teaches amino acid residues conserved among Arabidopsis thaliana, Zea mays, Hordeum vulgare, Daucus carota, and Coleus blumei (presently known in the art as Coleus scutellarioides), including the positions corresponding to F372 and F383 of instant SEQ ID NO:1 (Abstract; p. 1393, Figure 3).
The combination of Hawkes 2014, Hawkes 2019, and Fritze teaches, suggests, and provides motivation to produce a mutant HPPD polypeptide, which retains the activity of catalyzing the conversion of 4-hydroxyphenylpyruvic acid into homogentisic acid or homogentisate and is less sensitive to an HPPD-inhibitor herbicide than the wild-type HPPD, characterized by comprising the following amino acid mutations at the positions corresponding to the positions of the amino acid sequence set forth in SEQ ID NO:1: substitutions of F with A, G, or V at position 372 and substitution of F with W at position 383.
The level of ordinary skill in the art is high as evidenced by Hawkes 2014, Hawkes 2019, and Fritze. The Examiner notes that the amino acid sequence of Hawkes 2014’s SEQ ID NO:63 is comprised within Hawkes 2014’s SEQ ID NO:27. The F residue of Hawkes 2014’s SEQ ID NO:63 corresponds to F372 of the instant SEQ ID NO:1[0039] and the second F residue of Hawkes 2014’s SEQ ID NO:66 corresponds to F383 of the instant SEQ ID NO:1[0042]. Therefore, Hawkes 2014 discloses positions 372 and 383 of Applicant’s SEQ ID NO:1 as target sites for substitution.
It would have been prima facie obvious to one of ordinary skill in the art to combine the F372 and F383 substitutions taught by Hawkes 2014 to generate a mutant HPPD protein comprising an F372 substitution and F383 substitution. One of ordinary skill would have been motivated to do so, because Hawkes 2014 teaches that substitution of F372 and F383 promote herbicide resistance and/or tolerance in a plant comprising a mutant HPPD comprising either mutation[0002], [0004], [0006], and that the mutations may be used in combination[0117] (Abstract). Furthermore, both Hawkes 2019 and Fritze teach that F372 and F383 are highly invariable. Hawkes 2019 further teaches that F372 and F383 are located within 5 or fewer angstroms of the inhibitor binding site (p. 10, Figure 2) and that combining different mutations within an HPPD polypeptide has combinatorial effects on inhibitor resistance and suggests that mutating amino acid residues that are located within 15 angstroms of the inhibitor binding site and are highly invariable among the assessed plant species may provide useful mutations wherein any potential catalytic impairment may be compensated for via improvements in herbicide resistance (p. 19, “3.2.1. Generation and detection of improved mutants”, second paragraph; pp. 19-20, “3.2.2. Kinetic characterization of improved mutant enzymes”, emphasis on first paragraph). Therefore, one of ordinary skill in the art would be motivated to produce a protein comprising multiple mutations to further increase herbicide tolerance in a plant comprising the double mutant HPPD. In particular, one of ordinary skill in the art would be motivated to modify positions 372 and 383 of SEQ ID NO:1, because Hawkes 2019 and Fritze both disclose these residues are highly invariable among distinct species, Hawkes 2019 suggests that mutation of such residues is useful for generating herbicide-resistance HPPDs, and Hawkes 2014 specifically teaches mutating F372 and F383 to produce inhibitor-resistance polypeptides. Accordingly, one of ordinary skill in the art would have been motivated to produce the claimed invention without any surprising or unexpected results.
Claim 2 is both indefinite and improperly expands the scope of claim 1 as described above in the rejections of the claims under 35 U.S.C. 112. For the purpose of compact prosecution, claim 2 is herein interpreted to encompass the mutant polypeptide of claim 1 wherein said polypeptide comprises a first and second mutation. However, as stated above, the polypeptide of claim 1 already comprises a first and second mutation. Therefore, claim 2 simply recites the mutant polypeptide of claim 1. Accordingly, for the same reasons claim 1 is rejected in view of the teachings of Hawkes 2014, claim 2 is also anticipated by Hawkes 2014.
Regarding claim 3, the teachings of Hawkes 2014, Hawkes 2019, and Fritze are as discussed above.
Hawkes 2014 is silent to the following mutations: A106G, A107 deletion, A111T, and K351N.
However, Hawkes 2019 teaches a mutant HPPD polypeptide lacking A111 from SEQ ID NO:1 (p. 12, “Protein sequences”) and that K351 of instant SEQ ID NO:1 is located within 15 angstroms of the inhibitor binding site and shows some variability in amino acid conservation among various plant species (p. 11, Figure 2).
Additionally, Fritze teaches amino acid residues conserved among Arabidopsis thaliana, Zea mays, Hordeum vulgare, Daucus carota, and Coleus blumei (presently known in the art as Coleus scutellarioides), including the position corresponding to K351 of instant SEQ ID NO:1.
The combination of Hawkes 2014, Hawkes 2019, and Fritze renders obvious a mutant HPPD polypeptide characterized in that the mutant HPPD polypeptide comprises SEQ ID NO:203.
It would have been prima facie obvious to one of ordinary skill in the art to combine the F372[0039] and F383[0042] substitutions taught by Hawkes 2014 with a further mutation comprising substitution or deletion of A111 and/or K351N to produce a polypeptide comprising any combination of mutations at F372, F373, K351, or A111. One of ordinary skill in the art would have been motivated by the teachings of Hawkes 2019 to delete or substitute A111 with any other amino acid because Hawkes 2019 discloses that HPPD polypeptides lacking A111 demonstrate increased inhibitor resistance when combined with substitutions of amino acids found in close proximity to the inhibitor binding site (p. 12, “Protein sequences”; p. 19, “3.2.1. Generation and detection of improved mutants”; p. 20, left column, first partial paragraph). One of ordinary skill in the art would have been motivated by the teachings of both Hawkes 2019 and Fritze to modify K351 because K351 is conserved among Arabidopsis thaliana, Avena sativa, Coleus blumei, Daucus carota, Hordeum vulgare, soybean, and Zea mays and Hawkes 2019 discloses and suggests that mutating amino acids within close proximity to the inhibitor binding site as the “most likely positions at which to identify mutations that could affect inhibitor binding without completely obviating or misdirecting catalytic function” (p. 19, “3.2.1. Generation and detection of improved mutants”). Furthermore, Hawkes 2019 discloses that K351 is located within close proximity to the polypeptide’s inhibitor binding site (p. 11, Figure 2). Therefore, one of ordinary skill in the art would have predicted, with a reasonable expectation of success, that mutating K351 would reduce inhibitor binding due to the residue’s proximity to the inhibitor binding site. Furthermore, one of ordinary skill in the art would have been motivated to substitute K351 with asparagine, specifically, because Hawkes 2019 teaches that the position corresponding to K351 of the Avena sativa SEQ ID NO:1 is asparagine in the corresponding rice HPPD polypeptide. Thus, one of ordinary skill in the art would have predicted, with a reasonable expectation of success, that substituting K351 with asparagine would not abolish HPPD activity, because the presence of an asparagine residue at the position corresponding to K351 of the rice HPPD polypeptide does not disrupt the functionality of the polypeptide. Accordingly, one of ordinary skill in the art would have been motivated to produce the claimed invention without any surprising or unexpected results.
Regarding claim 4, in addition to the teachings discussed above, the HPPD taught by Hawkes is obtained from the plant Avena sativa[0088], [0116].
Regarding claim 5, proteins are inherently encoded in polynucleotides. Therefore, in teaching a mutant HPPD polypeptides, Hawkes 2014 also teaches polynucleotide sequences encoding said polypeptides[0039]. Furthermore, in addition to the teachings discussed above, Hawkes 2014 teaches polynucleotides encoding mutant HPPDs[0085], [0146].
Regarding claim 6, in addition to the teachings discussed above, Hawkes 2014 teaches an expression cassette comprising the mutant HPPD under the regulation of effectively-linked regulatory sequences[0085], [0146].
Accordingly, one of ordinary skill in the art would have been motivated to produce the claimed invention without any surprising or unexpected results.
Double Patenting
11. The Office acknowledges the acceptance of the Terminal Disclaimer filed in co-pending Application No. 17/642,528 on January 05, 2026. Accordingly, any potential double patenting issues regarding the instant application and co-pending Application No. 17/642,528 are rendered moot.
12. Claims 1-6 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2 and 4-6 of copending Application No. 17/642,528 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)). Although the claims at issue are not identical, they are not patentably distinct from each other.
Instant claim 2 is indefinite as discussed above in the rejection of the claims under 35 U.S.C. 112(b) and is herein interpreted to recite and encompass the polypeptide of instant claim 1. Claims 1-2 of the instant Application are directed to a mutant HPPD polypeptide, which retains the activity of catalyzing the conversion of 4-hydroxyphenylpyruvic acid into homogentisic acid or homogentisate and is less sensitive to an HPPD-inhibitor herbicide than the wild-type HPPD, characterized by comprising the following amino acid mutations at the positions corresponding to the positions of the amino acid sequence set forth in SEQ ID NO:1: substitutions of F with A, G, or V at position 372 and substitution of F with W at position 383.
Claim 1 of copending Application No. 17/642,528 is directed to a mutant HPPD polypeptide comprising a F372A, F372G, F372V, F372P, F372S, F372T, F372C, F372M, F372Q, F372D, or F372 deletion mutation of a sequence identical to instant SEQ ID NO:1, wherein the mutant polypeptide can confer resistance to an HPPD-inhibitor herbicide to a plant comprising the polynucleotide; wherein the HPPD-inhibitor herbicide is at one-fold field concentration to four-fold field concentration, and wherein the plant has no plant damage or reduced plant damage cause by HPPD-inhibitor herbicide, and the reduced plant damage is a degree of damage of less than 50%. The recitation of “high-resistant tolerance” appears indefinite because this is not an art-recognized term or phrase, and Applicant provides no definition or parameters for the phrase. The recitations of “one-fold field concentration” and “four-fold field concentration” appear indefinite because these are not art-recognized terms of phrases and Applicant has provided no definition for these phrases in the specification or claims. The recitation of a “degree of damage of less than 50%” is indefinite because it is unclear what is encompassed by and how one would assess a “degree of damage of less than 50%”. The claims do not describe the parameters by which said plant damage is to be assessed. The specification provides no definition for the term “plant damage” and this term is not standard or recognized in the art. Though Applicant provides examples of “plant damage” in the specification, the claims are not limited to these embodiments (p. 21, lns. 4-19; p. 26, lns. 31-44). Accordingly, these indefinite recitations cannot be given patentable weight.
Co-pending claim 1 is silent to an F383W substitution.
The teachings of Hawkes 2014, Hawkes 2019, and Fritze are as discussed above in the rejection of the claims under 35 U.S.C. 103 and are incorporated herein.
As stated above, the combination of Hawkes 2014, Hawkes 2019, and Fritze teaches, suggests, and provides motivation to produce a mutant HPPD polypeptide, which retains the activity of catalyzing the conversion of 4-hydroxyphenylpyruvic acid into homogentisic acid or homogentisate and is less sensitive to an HPPD-inhibitor herbicide than the wild-type HPPD, characterized by comprising the following amino acid mutations at the positions corresponding to the positions of the amino acid sequence set forth in SEQ ID NO:1: substitutions of F with A, G, or V at position 372 and substitution of F with W at position 383. The level of ordinary skill in the art is high as evidenced by Hawkes 2014, Hawkes 2019, and Fritze. For the same reasons discussed above in the rejection of the claims under 35 U.S.C. 103, it would have been prima facie obvious to one of ordinary skill in the art to combine the F372 and F383 substitutions taught by Hawkes 2014 to generate a mutant HPPD protein comprising an F372 substitution and F383 substitution. Accordingly, one of ordinary skill in the art would have been motivated to produce the claimed invention without any surprising or unexpected results.
For the reasons stated above, instant claims 1-3 are provisionally unpatentable over claim 1 of copending Application No. 17/642,528 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
Claim 2 of co-pending Application No. 17/642,528 adds the further limitation that the claimed polypeptide must be obtained from plants or microorganisms including oats. The polypeptide of instant claim 1 is obtained from the oat Avena sativa. The scope of instant claim 1 is encompassed by co-pending claim 2; accordingly, instant claims 1-2 are provisionally unpatentable over co-pending claim 2 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
Claim 3 of co-pending Application No. 17/642,528 is directed to HPPD polypeptides comprising an F372L, F372I, F372W, F372N, F372E, or F372K. Hawkes 2014 teaches that F372 can be replaced with any amino acid to produce a polypeptide with increased resistance to HPPD inhibitors[0002], [0004], [0006], [0039]. Accordingly, instant claims 1-2 are provisionally unpatentable over co-pending claim 3 of Application No. 17/642,528 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
Claim 4 of co-pending Application No. 17/642,528 is directed to HPPD polypeptides comprising a mutation of G413W, G413H, G413M, G413F, or G413C, or wherein the second mutation is a deletion mutation at position 110 of the amino acid sequence set forth in SEQ ID NO:1. Instant claim 1 is silent to substitution of G413. However, Hawkes 2014 teaches that G413 can be substituted with any amino acid[0082] and Hawkes 2019 teaches G413W (p. 18, Table 2). Accordingly, instant claims 1-2 are provisionally unpatentable over co-pending claim 4 of Application No. 17/642,528 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
Instant claim 3 is directed to the HPPD polypeptide of SEQ ID NO:1 wherein the polypeptide comprises F372A, F383W, and K351N mutations. Such a mutation is obvious in view of the teachings of Hawkes 2014, Hawkes 2019, and Fritze, as discussed above in the rejection of the claims under 35 U.S.C. 103. Therefore, instant claim 3 is provisionally unpatentable over co-pending claim 1 of Application No. 17/642,528 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
Claim 2 of co-pending Application No. 17/642,528 adds the further limitation that the claimed polypeptide must be obtained from plants or microorganisms including oats. Instant claim 4 is directed to a mutant HPPD polypeptide wherein said polypeptide is obtained from plants or microorganisms. The scope of instant claim 4 is encompassed by co-pending claim 2; accordingly, instant claim 4 is provisionally unpatentable over co-pending claim 2 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
Claim 5 of co-pending Application No. 17/642,528 is directed to a polynucleotide encoding the mutant HPPD polypeptide of co-pending claim 1. Instant claim 5 is directed a polynucleotide encoding the mutant HPPD polypeptide of instant claim 1. Accordingly, instant claim 5 is provisionally unpatentable over co-pending claim 5 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
Claim 6 of co-pending Application No. 17/642,528 is directed to an expression cassette or recombinant vector, characterized by comprising the polynucleotide of co-pending claim 5 under the regulation of effectively-linked regulatory sequences. Instant claim 6 is directed to an expression cassette or recombinant vector, characterized by comprising the polynucleotide of instant claim 5 under the regulation of effectively-linked regulatory sequences. Accordingly, instant claim 6 is provisionally unpatentable over co-pending claim 6 in view of Hawkes et al. (US-20100197503-A1, published 09/24/2014 (N); hereinafter “Hawkes 2014”), further in view of Hawkes et al. (Pesticide Biochemistry and Physiology. 2019; 156:9-28 (Applicant’s IDS); hereinafter “Hawkes 2019”), and further in view of Fritze et al. (Plant Physiology. 2004; 134:1388–1400 (U)).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
13. No claim is allowed.
Examiner’s Contact Information
14. Any inquiry concerning this communication or earlier communications from the examiner should be directed to DEQUANTARIUS JAVON SPEED whose telephone number is (703)756-4779. The examiner can normally be reached M-F; 9AM-5PM ET.
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/DEQUANTARIUS JAVON SPEED/Junior Examiner, Art Unit 1663 /Amjad Abraham/SPE, Art Unit 1663
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