Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
The Office acknowledges the receipt of Applicant’s restriction election filed September 10, 2025. Applicant elects Group I and position 92 of SEQ ID NO:2, Because no traverse is presented, this election is treated as election without traverse. Claims 9, 11-13, 17-23, and 25 are pending. Claims 9, 11-13, 17-23, and 25 are withdraw from examination. Claims 1-6, 8, and 16, to the extent of position 92 of SEQ ID NO:2, are examined in the instant application.
The restriction is made FINAL
Information Disclosure Statement
The information disclosure statement filed March 25, 2024 fails to comply with 37 CFR 1.98(a)(2), which requires a legible copy of each cited foreign patent document; each non-patent literature publication or that portion which caused it to be listed; and all other information or that portion which caused it to be listed. It has been placed in the application file, but the information referred to therein has not been considered.
The information disclosure statement filed March 25, 2024 fails to comply with 37 CFR 1.98(a)(3)(i) because it does not include a concise explanation of the relevance, as it is presently understood by the individual designated in 37 CFR 1.56(c) most knowledgeable about the content of the information, of each reference listed that is not in the English language. It has been placed in the application file, but the information referred to therein has not been considered.
The information disclosure statement filed March 25, 2024 fails to comply with the provisions of 37 CFR 1.97, 1.98 and MPEP § 609 because the IDS does not include copies of the non-patent literature references as required. It has been placed in the application file, but the information referred to therein has not been considered as to the merits. Applicant is advised that the date of any re-submission of any item of information contained in this information disclosure statement or the submission of any missing element(s) will be the date of submission for purposes of determining compliance with the requirements based on the time of filing the statement, including all certification requirements for statements under 37 CFR 1.97(e). See MPEP § 609.05(a).
Claim Status
Claims 1-6, 8-9, 11-13, 16-23 and 25 are pending.
Claims 9, 11-13, 17-23 and 25 are withdrawn as a result of Restriction Requirement.
Claims 1-6, 8, and 16 are currently amended.
Claims 1-6, 8, and 16 are examined on the merits.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 3 and 5 is rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter, which the inventor regards as the invention by using “a homologue, variant or derivative thereof”
Claim 3 and 5 is deemed indefinite for the recitation of “a homologue, variant or derivative ”. Regarding the term “a homologue, variant or derivative ”, the Specification states “variant” with respect to a sequence is intended to mean substantially similar sequences, with from 30%-99% identity to SEQ ID NO:1 or SEQ ID NO:1; the specification states “Homologues” of a protein encompass peptides, oligopeptides, polypeptides, proteins and enzymes having amino acid substitutions, deletions and/or insertions relative to the unmodified protein in question and having similar biological and functional activity as the unmodified protein from which they are derived; the Specification states “derivative” of a protein encompass peptides, oligopeptides, polypeptides, proteins and enzymes having amino acid substitutions, deletions and/or insertions relative to the unmodified protein in question and having similar biological and functional activity as the unmodified protein from which they are derived. Obviously, these are not sufficiently clear definitions for “homologue”, “variant” or “derivative”; the state of the art regards the terms as broad, flexible, and lacking a universally accepted definition. Therefore, in the absence of clear definitions, identity thresholds, or functional limits in the specification, these terms leave the claim open to multiple interpretations and encompass an indeterminate number of sequences, making the claim scope unclear. The phase “a homologue, variant or derivative thereof” renders the metes and bounds of the claim unclear. These terms are relative and undefined in the context of the claim and the specification does not provide objective criteria for determining what degree of sequence similarity, functional equivalence, or structural modification would qualify a nucleic acid sequence or amino acid sequence as a “homologue,” “variant,” or “derivative” of the sequence.
Because these terms may encompass an indeterminate number of sequences with unknown or unpredictable structure-function relationships, a person of ordinary skill in the art cannot ascertain the exact scope of the claimed polynucleotide. As such, it is unclear whether sequences with low identity, altered regulatory regions, or only partial overlap with SEQ ID NO:1 or SEQ ID NO:2 fall within the scope of the claims. Accordingly, claims 3 and 5 are indefinite under 35 U.S.C. 112(b).
Claim 5 is rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor regards as the invention.
The claim recites “wherein the mutated TriA refers to a TriA polypeptide comprising the sequence of SEQ ID NO: 2, an orthologue, paralogue, or homologue thereof, wherein the amino acid sequence differs from the wildtype amino acid sequence at one or more positions corresponding to positions 92, 93, 155, 157 of SEQ ID NO: 2.”
The phrase “comprising the sequence of SEQ ID NO: 2” renders the scope of the claim unclear because it is internally inconsistent with the subsequent limitation that the polypeptide “differs from the wildtype amino acid sequence.” Accordingly, the claim fails to distinctly define the invention and is indefinite under 35 U.S.C. 112(b).
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.
Written Descriptions
Claims 3, 4, and 5 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 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.
The Federal Circuit has clarified the application of the written description requirement. The court stated that a written description of an invention "requires a precise definition, such as by structure, formula, [or] chemical name, of the claimed subject matter sufficient to distinguish it from other materials". University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568; 43 USPQ2d 1398, 1406 (Fed. Cir. 1997). The court also concluded that "naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not description of that material". Id. Further, the court held that to adequately describe a claimed genus, Patent Owner must describe a representative number of the species of the claimed genus, and that one of skill in the art should be able to "visualize or recognize the identity of the members of the genus". Id.
Claims 3 and 5 generically requiring the broad genus of mutated TriA polypeptide or nucleic acid, or “a homologue, variant or derivative”, specifically in claim 3 recites “he polynucleotide encoding the mutated TriA polypeptide comprises the nucleic acid sequence set forth in SEQ ID NO: 1, or a homologue, variant or derivative”; and in claim 5 recites “mutated TriA refers to a TriA polypeptide comprising the sequence of SEQ ID NO: 2, an orthologue, paralogue, or homologue”, to confers to the plant or plant part tolerance to herbicides.
Claims 4, requiring the broad genus of polypeptide having about 60% or more amino acid sequence identity to SEQ ID NO: 2 to confers to the plant or plant part tolerance to herbicides. The terms “orthologue, paralogue, or homologue” are interpreted as being directed to polypeptides having at least 60% identity to the amino acid sequence SEQ ID NO: 2. When a nucleotide mutation causes an amino acid change, a 60% identical protein might come from a much higher or much lower DNA identity, depending on which codons differ and how many substitutions occur. A protein claim with 60% identity does not cover any specific percentage identity at the nucleotide level unless explicitly recited. The two scopes do not automatically overlap. The specification describes “a nucleic acid molecule having 30% or more identity, preferably 40%, 50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, or more with the nucleic acid molecule sequence of a polynucleotide comprising the nucleic acid molecule of SEQ ID NO: 1, or a variant, paralogue, orthologue or homolog thereof, and confers increased herbicide tolerance or resistance, as compared to a corresponding, e.g. non-transformed, wild type plant cell, a plant or a part thereof”. A POSITA would interpret “orthologue, paralogue, or homologue” in the claim as at least about 30% identical to SEQ ID NO:1. For the sake of brevity, the narrower genus is used in the discussion below to exemplify the broadness of the scope of the lack of adequate description. Therefore, the lack of adequate description regarding the broad genus of polypeptides having at least 60% identity to SEQ ID NO: 2, is discussed below.
The specification describes orthologous and paralogues (paragraph 0101-0103) and lists sequences (SEQ ID Nos: 3-31) that are related to SEQ ID NO:2. It also discloses in silico alignment methods (paragraph 0106) and mutagenesis techniques (paragraph 0107-0108), and provides specific substitutions at certain amino acid positions (e.g., 92, 93, 155, 157; paragraph 0114-0260) that yield herbicide-tolerant TriA variants.
The specification fails to provide written description support for the full scope of the claimed “mutated TriA polypeptide” having at least 60% sequence identity to SEQ IDNO:2. The specification mentions about insertions “within the amino acid sequence will be smaller than N- or C-terminal fusions, of the order of about 1 to 10 residues with no evident to support such description.” The disclosure only describes four specific point-substitution variants (position 92, 93, 155 and 157) of SEQ ID NO:2 and does not describe any additional types of mutations-such as deletions, insertions, residue substitutions other than the residues of 92, 93, 155 and 157, or combinations thereof, that would reasonably convey possession of the vast sequence space encompassed by a 60% identity requirement. The specification does not disclose any data demonstrating that such substantially diverged variants retain TriA activity or confer herbicide tolerance in a plant. In the absence of guidance, representative examples , or functional data across this breadth, a person of ordinary skill would not recognize the inventors or co-inventor as being in possession of the full scope of variants falling within the claimed 60% identity range.
Specification mentions “the main regions responsible for coordination of the active-site metal ion; residues known to be essential for the amidohydrolase activity; residues that form the hydrophobic “base” of the active site or are essential for hydrolase activity interactions with the aromatic ring of the substrate, were not changed. The residues that form the active site and substrate binding pocket are modified in order to expand the enzyme pocket” (example 5, paragraph 0830). Inventors mentions about the structure of amidohydrolase superfamily referring that “nucleophilic water molecule is activated through complexation with a mononuclear or binuclear metal center. In the mononuclear metal centers, the substrate is activated by a proton transfer from the active site, and the water is activated by metal ligation and general base catalysis”. No further description of specific motifs or domains and how to improve enzyme other than to “expand the enzyme pocket towards a bulkier substrate acceptance”.
As mentioned above, although the inventor briefly discusses structure-function considerations, the disclosure does not provide sufficient guidance for a POSITA to reasonably predict whether sequences with only 60% identity to SEQ ID NO:2 would retain the same enzymatic activity for herbicide tolerance. Enzyme function depend not only on conserved residues, but also on subtle conformational effects mediated by loop regions, substrate accessibility, catalytic positioning, and evolutionary fitness, which cannot be reliably inferred from low-level sequence similarity alone.
In “Catalytic Improvement and Evolution of Atrazine Chlorohydrolase” Colin Scott (IAPPLIED AND ENVIRONMENTAL MICROBIOLOGY, Apr. 2009, p. 2184–2191) points out that AtzA and TriA share a common deaminase ancestor at the earlier stage during evolution. Scott also demonstrates that even for AtzA with known structure and function, small targeted mutations (only five residues) can result in up to a 20-fold change in catalytic efficiency, largely due to altered cooperativity and substrate affinity (Km). This indicates that minor sequence variation in critical regions can dramatically affect function, even when overall sequence identity is high, making predictions for 60% homologs speculative and unreliable. Furthermore, Miriam Kaltenbach (“Functional Trade-Offs in Promiscuous Enzymes Cannot Be Explained by Intrinsic Mutational Robustness of the Native Activity”, PLoS Genet 12(10):e1006305. doi:10.1371 /journal.pgen.1006305, 2016) emphasizes that, despite AtzA and TriA differing by only nine amino acid substitutions, they catalyze entirely different reactions-dechlorination vs. deamination, it further notes that it is not possible to generalize mutational tolerance or predictability across enzyme families due to evolutionary selection pressures and differential mutational robustness. Thus, it is scientifically unsupported to assume that proteins with only 60% identity-which would involve hundreds of substitutions-would still function as herbicide-tolerant TriA enzymes. The structure of amidohydrolase superfamily has a mononuclear or
binuclear metal center embedded within the confines of a (β/α)8-barrel structural fold, where each β-strand is followed by an α-helix, and the connecting segments form loops. Clara M. Seibert (Structural and Catalytic Diversity within the Amidohydrolase Superfamily, Biochemistry, volume 44, number 17, 2005) demonstrates that loop regions near catalytic sites exhibit high variability in length, conformation, and sequence, despite the rest of the enzyme being structurally conserved. These loops directly contribute to substrate specificity and active site geometry, and access to the active site may require conformational changes. Therefore, without explicit structural, biochemical, or functional characterization, the disclosure does not enable a POSITA to predict whether loop-altered or 60% identity variants would preserve herbicide tolerance.
Overall, the disclosure does not describe, either by representative species or by common structural features, the broader genus of all “functional variants” that share only ≥60% identity to SEQ ID NO:2. The examples are limited to close homologues or engineered derivatives of SEQ ID NO:2 differing by only a few substitutions of residues within the catalytic region. There is no description of variants having extensive sequence divergence throughout the polypeptide that would still maintain the claimed function (herbicide tolerance). Nor does the specification identify structural motifs or consensus domains that would allow a POSITA to recognize which of the innumerable sequences within the ≥60% identity range would retain the necessary enzymatic activity.
Accordingly, the disclosure therefor fails to reasonably convey possession of the claimed invention commensurate with the claim’s breath.
CLUSTAL O(1.2.4) multiple sequence alignment
U55933 MQTLSIQHGTLVTMDQYRRVLGDSWVHVQDGRIVALGVHAESVPPPADRVIDARGKVVLP 60
SEQIDNO2 MQTLSIQHGTLVTMDQYRRVLGDSWVHVQDGRIVALGVHAESVPPPADRVIDARGKVVLP 60
************************************************************
U55933 GFINAHTHVNQILLRGGPSHGRQFYDWLFNVVYPGQKAMRPEDVAVAVRLYCAEAVRSGI 120
SEQIDNO2 GFINAHTHVNQILLRGGPSHGRQLYDWLFNVLYPGQKAMRPEDVAVAVRLYCAEAVRSGI 120
***********************:*******:****************************
U55933 TTINENADSAIYPGNIEAAMAVYGEVGVRVVYARMFFDRMDGRIQGYVDALKARSPQVEL 180
SEQIDNO2 TTINDNADSAIYPGNIEAAMAVYGEVGVRVVYARMFFDRMDGRIQGYVDALKARSPQVEL 180
****:*******************************************************
U55933 CSIMEETAVAKDRITALSDQYHGTAGGRISVWPAPATTTAVTVEGMRWAQAFARDRAVMW 240
SEQIDNO2 CSIMEETAVAKDRITALSDQYHGTAGGRISVWPAPAITPAVTVEGMRWAQAFARDRAVMW 240
************************************ * *********************
U55933 TLHMAESDHDERIHGMSPAEYMECYGLLDERLQVAHCVYFDRKDVRLLHRHNVKVASQVV 300
SEQIDNO2 TLHMAESDHDERLHWMSPAEYMECYGLLDERLQVAHCVYFDRKDVRLLHRHNVKVASQVV 300
************:* *********************************************
U55933 SNAYLGSGVAPVPEMVERGMAVGIGTDNGNSNDSVNMIGDMKFMAHIHRAVHRDADVLTP 360
SEQIDNO2 SNAYLGSGVAPVPEMVERGMAVGIGTDDGNCNDSVNMIGDMKFMAHIHRAVHRDADVLTP 360
***************************:**.*****************************
U55933 EKILEMATIDGARSLGMDHEIGSIETGKRADLILLDLRHPQTTPHHHLAATIVFQAYGNE 420
SEQIDNO2 EKILEMATIDGARSLGMDHEIGSIETGKRADLILLDLRHPQTTPHHHLAATIVFQAYGNE 420
************************************************************
U55933 VDTVLIDGNVVMENRRLSFLPPERELAFLEEAQSRATAILQRANMVANPAWRSL 474
SEQIDNO2 VDTVLIDGNVVMENRRLSFLPPERELAFLEEAQSRATAILQRANMVANPAWRSL 474
******************************************************
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 1-6, 8 and 16 are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Schachtschabel (WO2016116870A1, publication of 07-28-2016, Doreen Schachtschabel et. al.,).
Claims 1 recites a plant or plant part comprising a polynucleotide encoding a mutated TriA polypeptide, wherein the expression of said polynucleotide confers to the plant or plant part tolerance to herbicides. Schachtschabel disclose a plant or plant part comprising a polynucleotide encoding a wildtype or mutant TriA polypeptide, the expression of said polynucleotide confers to the plant or plant part tolerance to herbicides (claim 1). The following figure presents the polynucleotide sequence alignment of wild type TriA polypeptide SEQ ID NO: 1 (paragraph 0832) from the instant application and wild type TriA polypeptide SEQ ID NO:1 (example 6) disclosed in the prior art of Schachtschabel. Both wild type TriAs are identical. Accordingly, all limitations of claim 1 are disclosed. Therefore, claim 1 is anticipated.
CLUSTAL O(1.2.4) multiple sequence alignment
SEQIDNO1-WO2016116870 atgcagaccctgagcattcagcatggcaccctggttacaatggatcagtatcgtcgtgtt 60
SEQIDNO1-18615786 atgcagaccctgagcattcagcatggcaccctggttacaatggatcagtatcgtcgtgtt 60
************************************************************
SEQIDNO1-WO2016116870 ctgggtgatagctgggttcatgttcaggatggtcgtattgttgcactgggtgttcatgca 120
SEQIDNO1-18615786 ctgggtgatagctgggttcatgttcaggatggtcgtattgttgcactgggtgttcatgca 120
************************************************************
SEQIDNO1-WO2016116870 gaaagcgttccgcctccggcagatcgtgttattgatgcacgtggtaaagttgttctgcct 180
SEQIDNO1-18615786 gaaagcgttccgcctccggcagatcgtgttattgatgcacgtggtaaagttgttctgcct 180
************************************************************
SEQIDNO1-WO2016116870 ggttttatcaatgcacatacccatgttaatcagattctgctgcgtggtggtccgagtcat 240
SEQIDNO1-18615786 ggttttatcaatgcacatacccatgttaatcagattctgctgcgtggtggtccgagtcat 240
************************************************************
SEQIDNO1-WO2016116870 ggtcgtcagctgtatgattggctgtttaatgttctgtatccgggtcagaaagcaatgcgt 300
SEQIDNO1-18615786 ggtcgtcagctgtatgattggctgtttaatgttctgtatccgggtcagaaagcaatgcgt 300
************************************************************
SEQIDNO1-WO2016116870 ccggaagatgttgcagttgcagttcgtctgtattgtgcagaagcagttcgtagcggtatt 360
SEQIDNO1-18615786 ccggaagatgttgcagttgcagttcgtctgtattgtgcagaagcagttcgtagcggtatt 360
************************************************************
SEQIDNO1-WO2016116870 accaccattaatgataatgcagatagcgccatttatccgggtaatattgaagcagcaatg 420
SEQIDNO1-18615786 accaccattaatgataatgcagatagcgccatttatccgggtaatattgaagcagcaatg 420
************************************************************
SEQIDNO1-WO2016116870 gccgtttatggtgaagttggtgttcgtgttgtttatgcccgtatgttttttgatcgtatg 480
SEQIDNO1-18615786 gccgtttatggtgaagttggtgttcgtgttgtttatgcccgtatgttttttgatcgtatg 480
************************************************************
SEQIDNO1-WO2016116870 gatggtcgcattcagggttatgttgatgcactgaaagcacgtagtccgcaggttgaactg 540
SEQIDNO1-18615786 gatggtcgcattcagggttatgttgatgcactgaaagcacgtagtccgcaggttgaactg 540
************************************************************
SEQIDNO1-WO2016116870 tgtagcattatggaagaaaccgcagttgcaaaagatcgtattaccgcactgagcgatcaa 600
SEQIDNO1-18615786 tgtagcattatggaagaaaccgcagttgcaaaagatcgtattaccgcactgagcgatcaa 600
************************************************************
SEQIDNO1-WO2016116870 tatcatggtacagcaggcggtcgtattagcgtttggcctgcaccggcaattacaccggca 660
SEQIDNO1-18615786 tatcatggtacagcaggcggtcgtattagcgtttggcctgcaccggcaattacaccggca 660
************************************************************
SEQIDNO1-WO2016116870 gttaccgttgaaggtatgcgttgggcacaggcatttgcacgtgatcgtgcagttatgtgg 720
SEQIDNO1-18615786 gttaccgttgaaggtatgcgttgggcacaggcatttgcacgtgatcgtgcagttatgtgg 720
************************************************************
SEQIDNO1-WO2016116870 accctgcatatggccgaaagcgatcatgatgaacgtctgcattggatgagtccggcagaa 780
SEQIDNO1-18615786 accctgcatatggccgaaagcgatcatgatgaacgtctgcattggatgagtccggcagaa 780
************************************************************
SEQIDNO1-WO2016116870 tatatggaatgttatggtctgctggatgagcgcctgcaggttgcacattgtgtttatttt 840
SEQIDNO1-18615786 tatatggaatgttatggtctgctggatgagcgcctgcaggttgcacattgtgtttatttt 840
************************************************************
SEQIDNO1-WO2016116870 gatcgcaaagatgttcgtctgctgcatcgtcataatgttaaagttgcaagccaggttgtt 900
SEQIDNO1-18615786 gatcgcaaagatgttcgtctgctgcatcgtcataatgttaaagttgcaagccaggttgtt 900
************************************************************
SEQIDNO1-WO2016116870 agcaatgcatatctgggtagcggtgttgcaccggttccggaaatggttgaacgtggtatg 960
SEQIDNO1-18615786 agcaatgcatatctgggtagcggtgttgcaccggttccggaaatggttgaacgtggtatg 960
************************************************************
SEQIDNO1-WO2016116870 gcagttggtattggcaccgatgatggtaattgtaatgatagcgtgaacatgatcggcgat 1020
SEQIDNO1-18615786 gcagttggtattggcaccgatgatggtaattgtaatgatagcgtgaacatgatcggcgat 1020
************************************************************
SEQIDNO1-WO2016116870 atgaaatttatggcccatattcatcgtgccgttcatcgtgatgcagatgttctgacaccg 1080
SEQIDNO1-18615786 atgaaatttatggcccatattcatcgtgccgttcatcgtgatgcagatgttctgacaccg 1080
************************************************************
SEQIDNO1-WO2016116870 gaaaaaattctggaaatggcaaccattgatggtgcacgtagcctgggtatggatcatgaa 1140
SEQIDNO1-18615786 gaaaaaattctggaaatggcaaccattgatggtgcacgtagcctgggtatggatcatgaa 1140
************************************************************
SEQIDNO1-WO2016116870 attggtagcattgaaaccggtaaacgtgcagatctgatcctgctggatctgcgtcatccg 1200
SEQIDNO1-18615786 attggtagcattgaaaccggtaaacgtgcagatctgatcctgctggatctgcgtcatccg 1200
************************************************************
SEQIDNO1-WO2016116870 cagacaacaccgcatcatcatctggcagccaccattgtttttcaggcatatggtaatgaa 1260
SEQIDNO1-18615786 cagacaacaccgcatcatcatctggcagccaccattgtttttcaggcatatggtaatgaa 1260
************************************************************
SEQIDNO1-WO2016116870 gttgacaccgttctgattgatggcaatgttgttatggaaaatcgtcgtctgagctttctg 1320
SEQIDNO1-18615786 gttgacaccgttctgattgatggcaatgttgttatggaaaatcgtcgtctgagctttctg 1320
************************************************************
SEQIDNO1-WO2016116870 cctccggaacgtgaactggcatttctggaagaagcacagagtcgcgcaaccgcaattctg 1380
SEQIDNO1-18615786 cctccggaacgtgaactggcatttctggaagaagcacagagtcgcgcaaccgcaattctg 1380
************************************************************
SEQIDNO1-WO2016116870 cagcgtgcaaatatggttgcaaatccggcatggcgtagcctgtga 1425
SEQIDNO1-18615786 cagcgtgcaaatatggttgcaaatccggcatggcgtagcctgtga 1425
*********************************************
19. Claim 2 recites that the herbicide comprises a compound which inhibits cellulose biosynthesis. Schachtschabel discloses the same features as in claim 1, including the plant or plant part, wherein the herbicide comprises a compound which inhibits cellulose biosynthesis (claim 2).
Claim 3 recites that the polynucleotide encoding the mutated TriA polypeptide comprises the nucleic acid sequence set forth in SEQ ID NO: 1, or a homologue, variant or derivative. Schachtschabel discloses the same features as in claim 1, Schachtschabel also discloses the polynucleotide encoding the wildtype or mutated TriA polypeptide comprises the nucleic acid sequence set forth in SEQ ID NO: 1 , or a homologue, variant or derivative thereof (claim 3).
Claims 4 recites wherein the mutated TriA polypeptide is a functional variant having, over the full-length of the variant, at least about 60%, illustratively, at least about 80%, 90%, 95%, 98%, 99% or more amino acid sequence identity to SEQ ID NO: 2. In instant application, SEQ ID NO: 1, encodings SEQ ID NO:2 (paragraph 0832). Schachtschabel discloses the same features as in claim 1, including the wildtype or mutated TriA polypeptide is a functional variant having, over the full-length of the variant, at least about 60%, illustratively, at least about 80%, 90%, 95%, 98%, 99% or more amino acid sequence identity to SEQ ID NO: 2(claim 4).
Claims 5 limits the mutated TriA as having the amino acid sequence differing from the wildtype amino acid sequence at one or more positions corresponding to position 92 of SEQ ID NO: 2. Schachtschabel discloses the mutated TriA polypeptide amino acid sequence that differs from the wildtype amino acid sequence at one or more positions corresponding to positions 70, 71 , 88, 91 , 92, 96, 126, 128, 155, 157, 167, 220 of SEQ ID NO: 2 (claim 5).
Claims 6 recites a transgenic seed carrying a TriA expression cassette including TriA gene and a plant promoter, which, upon germination, produces a TriA -expressing, herbicide tolerant plant. Schachtschabel discloses the seed capable of germination into a plant comprising in at least some of its cells a polynucleotide operably linked to a promoter operable in plant cells, the promoter capable of expressing a wildtype or mutated TriA polypeptide encoded by the polynucleotide, the expression of the wildtype or mutated TriA polypeptide conferring to the plant tolerance to herbicides (claim 6).
Claims 8 recites the plant, plant part, or plant cell of claim 1, wherein the polynucleotide is operably linked to a promoter operable in a plant cell. Schachtschabel discloses the same features as in claim 1, including “a plant cell” (claim 8) “plant product prepared from a plant or plant part comprising in at least some of its cells” (claim 9) a polynucleotide operably linked to a promoter operable in plant cells, the promoter capable of expressing a TriA polypeptide encoded by the polynucleotide
Claims 16 is recites the plant, plant part, further comprises a second or third herbicide-tolerant trait. Schachtschabel discloses the method of producing a progeny plant having tolerance double herbicides (claim 15 and page 4, line1-10).
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to YANXIN SHEN whose telephone number is (571)272-7538. The examiner can normally be reached Monday-Friday.
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/YANXIN SHEN/Examiner, Art Unit 1663
/WEIHUA FAN/Examiner, Art Unit 1663