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 .
Election/Restrictions
In the response received on Mar. 6, 2026, Applicant canceled claim 21. Claims 1-7, 9, 11-20, and 23 are pending and are subject to a restriction requirement for lack of unity of invention (see Office Action mailed on Jan. 9, 2026). Applicant has elected Group I, claims 1-4 and 11 (Resp 11) and SEQ ID NOs: 41 and 3 (Resp 12) with traverse. Because claims 1-4 and 11 do not recite SEQ ID NO: 3, this election of species does not affect examination of the elected invention.
Claims 5-7, 9, 12-20, and 23 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected inventions/species, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on Mar. 6, 2026.
Applicant traverses on the grounds that the prior art relied upon by the Examiner to break unity of invention (Li et al.) discloses a mutation in the transmembrane domain of the protein in amino acid #297, and Applicant asserts that this is not in the N-terminal domain as claimed (Resp 10). Applicant points to the paragraph bridging pages 11-12 in the specification and states that this section defines the N-terminal domain (Resp 10). This is not persuasive, however, because this paragraph is describing a “particularly preferred embodiment”, and this is not a definition of “N-terminal domain” as argued by Applicant. The specification provides several examples of an N-terminal domain, but it does not provide a definition for “N-terminal domain”.
In the restriction requirement mailed on Jan. 9, 2026, the Examiner points out that Li teaches a mutation that causes a single amino acid substitution in a GORK voltage-gated potassium channel at position 297 of a protein that consists of a total of 824 amino acids. The N-terminal half of 824 amino acids is amino acids #1-412. Position 297 falls within the N-terminal half of the protein and the transmembrane domain comprising this amino acid position is an “N-terminal domain” as required by the current claims.
Applicant argues that Li focuses on the transmembrane domain compared with the cytosolic N termini as disclosed in their specification (Resp 10-11). This is not persuasive, however, because the claims do not require the mutation to be in a cytosolic domain.
It is noted that Applicant amended claim 1 to require 80% identity to one of the recited sequences, and Applicant elected SEQ ID NO: 43 for prosecution. Li does not teach a protein with at least 80% identity to the elected SEQ ID NO: 43, therefore, the Examiner has provided prior art by Collet et al (see below). The art rejections below demonstrate that the amended claims do not share unity of invention.
Applicant is reminded that unity of invention is evaluated at each step of prosecution, and at such a time that a claim is found to be allowable, then all claims that require every limitation of the allowable claim will be rejoined because unity of invention will have been restored for the claims that share the technical feature of all limitations in the allowable claim.
Claim Interpretation
Claim 1 is directed to a genetically altered plant, plant part or plant cell, wherein the plant has at least one mutation. This is a product-by-process claim because having a mutation and being “genetically altered” are mechanisms by which a polymorphism can be introduced into a plant’s genomic DNA. The process by which a product is made is only given weight for structural features that are conferred to the product by using that particular process to make the product. For the instant claims, if a plant, plant part or plant cell comprises a gene encoding a protein with an amino acid sequence having at least 80% identity to one of the recited sequences, and if the encoded protein has at least one amino acid change relative to the recited sequence, then the plant, plant part or plant cell meets the limitations of instant claim 1.
Claim 1 is interpreted to require a mutation in the N-terminal domain of one of the recited sequences in the recited plant, but it does not require said mutation in the recited plant part or plant cell. The “wherein” clause is only directed to the plant.
Similarly, in claim 11, the plant is required to be a monocot or a dicot, but the plant part or plant cell are not limited to a monocot or a dicot. The “wherein” clause is only directed to the plant.
Specification
The disclosure is objected to because of the following informalities: The acronym “GORK” is utilized throughout the specification, but the acronym was not defined until page 10 of the specification. “(Guard cell Outward Rectifying Potassium (K+))” should be inserted next to the first appearance of “GORK” in the specification.
Appropriate correction is requested.
Claim Objections
Claim 1 is objected to because of the following informalities: the claim recites “GORK” channel. This is reciting an acronym without first defining it which is improper. Appropriate correction is requested.
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 1-4 and 11 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. All dependent claims are included in these rejections unless they include a limitation that overcomes the deficiencies of the parent claim.
Claim 1 recites the limitation "the N-terminal domain amino acid sequence having at least 80% overall amino acid sequence identity with …" in lines 2-3. There is insufficient antecedent basis for this limitation in the claim. There is no previously recited N-terminal domain amino acid sequence.
In addition, the metes and bounds for what constitutes the “N-terminal domain” are not clear. In writing the restriction requirement, the Examiner interpreted any polypeptide in amino acids 1-412 to be an “N-terminal domain” because the full-length protein is 824 amino acids long, and therefore, amino acids 1-412 are in the N-terminal half of the protein. However, Applicant has argued that this is not the N-terminal domain. Applicant has argued that position #297 is not in the N-terminal domain (Resp 10). Applicant pointed to a “particularly preferred embodiment” and states that this is a “definition” (Id.). On pages 11-12 of the specification, there are multiple different embodiments set forth, each having a different scope. Because the Applicant is attempting to insert limitations from the specification into the claims, the intended scope of “N-terminal domain” is not clear.
Claim 4 recites “wherein the mutation is the substitution of all positively charged amino acids for negatively charged amino acids or neutral amino acids in the N-terminal domain…”. It is unclear what this recitation requires. Does this mean that the N-terminal domain is required to have only positively charged amino acid residues after the plant has been mutated? Or does this mean that any substitutions that have occurred must introduce a positively charged amino acid but negative or neutral amino acids can be retained so long as they are not substituted? As written, the Examiner is unable to determine what is required for a plant to be encompassed by the claim.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(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.
Anticipation by Collet
Claim(s) 1-4 and 11 is/are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Collet et al. (US Pre-Grant Publication US 2021/0171971 A1, published on June 10, 2021 for US Application No. 17/048,038 with priority to April 18, 2018).
The claims are directed to a plant, plant part or plant cell, wherein the plant has at least one mutation in the N-terminal domain amino acid sequence having at least 80% overall amino acid sequence identity with SEQ ID NO: 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, or 43 of a stomatal voltage-gated potassium channel, wherein the stomatal voltage-gated potassium channel is a GORK channel (claim 1), including wherein the mutation alters the pattern of charged amino acids in the N-terminal domain (claim 2), including wherein the mutation is a substitutions of at least one positively charged amino acid for a negatively charged or neutral amino acid and/or wherein the mutation is the substitution of at least one negatively charged amino acid for a positively charged or neutral amino acid (claim 3), including wherein the mutation is the substitutions of all positively charged amino acids for negatively charged amino acids or neutral amino acids in the N-terminal domain of the potassium channel (claim 4), and including wherein the plant is a monocot or dicot (claim 11).
Collet teaches an amino acid sequence they refer to as SEQ ID NO: 295 with 87.6% identity to the instant SEQ ID NO: 43, see sequence search result, below:
RESULT 3
US-17-048-038-295
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 295, US/17048038
Publication No. US20210171971A1
GENERAL INFORMATION
APPLICANT: Pioneer Hi-Bred International, Inc.
TITLE OF INVENTION: INTERACTORS AND TARGETS FOR IMPROVING PLANT AGRONOMIC
TITLE OF INVENTION: CHARACTERISTICS
FILE REFERENCE: 7841-US-PSP
CURRENT APPLICATION NUMBER: US/17/048,038
CURRENT FILING DATE: 2020-10-15
NUMBER OF SEQ ID NOS: 580
SEQ ID NO 295
LENGTH: 879
TYPE: PRT
ORGANISM: Zea mays
Query Match 87.6%; Score 304; Length 879;
Best Local Similarity 87.7%;
Matches 57; Conservative 3; Mismatches 5; Indels 0; Gaps 0;
Qy 1 EVVRDHIASSRGSRLALFGSELRLGRFRPRRRRRLPLAGEGAAEGFFHGLVIHPDNKWYR 60
| | ||||||||||||||||:||||||||||||| ||||||||||| | |||||||:||:
Db 29 EEVCDHIASSRGSRLALFGSDLRLGRFRPRRRRRRPLAGEGAAEGFLHDLVIHPDNRWYQ 88
Qy 61 LWTKF 65
|||||
Db 89 LWTKF 93
Collet identifies their SEQ ID NO: 295 as a cyclic nucleotide binding/inward rectifier potassium channel with ion gated channel activity (Collet 11, Table 1B). The neutral amino acid valine (V) at position #2 in the instant SEQ ID NO: 43 is substituted with a negatively charged glutamate (E) in Collet’s SEQ ID NO: 295 (see alignment, above). The neutral amino acid leucine (L) at position #35 in the instant SEQ ID NO: 43 is substituted with a positively charged arginine (R) in Collet’s SEQ ID NO: 295. The neutral amino acid glycine (G) at position #49 in the instant SEQ ID NO: 43 is substituted with a negatively charged aspartate (D) in Collet’s SEQ ID NO: 295.
These substitutions are in the N-terminal domain of a potassium channel, and alter the pattern of charged amino acids in this domain (claim 2). There are substitutions of neutral amino acids with both positive and negative amino acids (claim 3). The endogenous gene taught by Collet is identified as a Zea mays gene, and Zea mays is a monocot (claim 11).
Collet claims a method comprising introducing in a regenerable plant cell a targeted genetic modification at a genomic locus that encodes a polypeptide with at least 80% identity or 95% identity to multiple sequences, including SEQ ID NO: 295 and generating a plant (Collet claims 51 and 52), including wherein the plant is a monocot and is maize (Id. claims 55 and 56). This necessarily involves starting with a maize plant that comprises a gene encoding a protein with at least 95% identity to their SEQ ID NO: 295. As discussed in the claim interpretation section, any plant having the required substitutions/mismatches is encompassed by the instant claims not matter how the substitutions/mismatches were made. The process by which a product is made is only given weight for the structural features conferred by the process. In this case, the three mismatches discussed, above, which substitute either a positive or a negative charge for a neutral charge satisfy the limitations of the instant claims.
With regard to claim 4, it is unclear what claim 4 actually requires as far as positively charged amino acids, but the sequence taught by Collet has one positively charged amino acid substituted for a neutral amino acid. Furthermore, Collet teaches a plant cell, and the instantly claimed plant cells are not required to have the recited mutation (see claim interpretation, above).
Anticipation by Collet2
Claim(s) 1-4 and 11 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Collet et al. (WO 2019/204266 A1; published on Oct. 24, 2029). This document will be referred to hereafter as “Collet2”.
Collet2 teaches an amino acid sequence they refer to as SEQ ID NO: 295 with 87.6% identity to the instant SEQ ID NO: 43, see sequence search result, below:
RESULT 6
BGX16219
ID BGX16219 standard; protein; 879 AA.
XX
AC BGX16219;
XX
DT 12-DEC-2019 (first entry)
XX
DE Zea mays Zm00001d044717 protein, SEQ ID 295.
XX
KW CRISPR-Cas system;
KW Cyclic nucleotide binding inward rectifier potassium channel;
KW Genome editing; TALEN system; Zm00001d044717; biomass; crop improvement;
KW gene regulation; plant; seed.
XX
OS Zea mays.
XX
CC PN WO2019204266-A1.
XX
CC PD 24-OCT-2019.
XX
CC PF 16-APR-2019; 2019WO-US027617.
XX
PR 18-APR-2018; 2018US-0659579P.
PR 04-OCT-2018; 2018US-0741529P.
PR 11-DEC-2018; 2018US-0778086P.
XX
CC PA (DUPO ) PIONEER HI-BRED INT INC.
XX
CC PI Haug Collet K, Hou Z, Lawit S, Melo R, Mongar N, Van Hemert J;
CC PI Wu J, Zhou W;
XX
DR WPI; 2019-88270E/86.
DR N-PSDB; BGX16481.
XX
CC PT New polynucleotide useful for increasing grain or seed or biomass yield
CC PT in plant i.e. monocot plant, preferably maize, or modulating expression
CC PT level in plant, comprises amino acid sequence.
XX
CC PS Claim 1; SEQ ID NO 295; 85pp; English.
XX
CC The present invention relates to a novel polynucleotide useful for
CC increasing grain, seed or biomass yield in a plant. The polynucleotide
CC encodes a polypeptide selected from SEQ ID NO: 1-11 (see BGX15925-
CC BGX15935), SEQ ID NO: 23-31 (see BGX15947-BGX15955), SEQ ID NO: 40-299
CC (see BGX15964-BGX16223), SEQ ID NO: 563 (see BGX16487), SEQ ID NO: 565
CC (see BGX16489) and SEQ ID NO: 567-573 (see BGX16491-BGX16497). The
CC invention further provides: a recombinant DNA construct comprising the
CC polynucleotide operably linked to a regulatory element; a plant or a
CC plant cell comprising the polynucleotide or the recombinant DNA construct
CC ; a maize plant comprising a targeted genetic modification at a genomic
CC locus that encodes the polypeptide; a seed comprising the polynucleotide
CC or the recombinant DNA construct in its genome; a maize seed comprising
CC the targeted genetic modification at a genomic locus that encodes the
CC polypeptide; a method for increasing the grain, seed or biomass yield in
CC the plant; a method for increasing the yield of the plant; a method for
CC increasing the photosynthetic activity in the plant; and a method for
CC modulating the expression level in the plant by using polynucleotide-
CC guided endonuclease, CRISPR-Cas endonucleases, base editing deaminases,
CC zinc finger nuclease, transcription activator-like effector nuclease
CC (TALEN), engineered site-specific meganucleases or Argonaute.
XX
SQ Sequence 879 AA;
Query Match 87.6%; Score 304; Length 879;
Best Local Similarity 87.7%;
Matches 57; Conservative 3; Mismatches 5; Indels 0; Gaps 0;
Qy 1 EVVRDHIASSRGSRLALFGSELRLGRFRPRRRRRLPLAGEGAAEGFFHGLVIHPDNKWYR 60
| | ||||||||||||||||:||||||||||||| ||||||||||| | |||||||:||:
Db 29 EEVCDHIASSRGSRLALFGSDLRLGRFRPRRRRRRPLAGEGAAEGFLHDLVIHPDNRWYQ 88
Qy 61 LWTKF 65
|||||
Db 89 LWTKF 93
Collet2 identifies their SEQ ID NO: 295 as a cyclic nucleotide binding/inward rectifier potassium channel with ion gated channel activity (Collet2 18, Table 1B). The neutral amino acid valine (V) at position #2 in the instant SEQ ID NO: 43 is substituted with a negatively charged glutamate (E) in Collet2’s SEQ ID NO: 295 (see alignment, above). The neutral amino acid leucine (L) at position #35 in the instant SEQ ID NO: 43 is substituted with a positively charged arginine (R) in Collet2’s SEQ ID NO: 295. The neutral amino acid glycine (G) at position #49 in the instant SEQ ID NO: 43 is substituted with a negatively charged aspartate (D) in Collet2’s SEQ ID NO: 295.
These substitutions are in the N-terminal domain of a potassium channel, and alter the pattern of charged amino acids in this domain (claim 2). There are substitutions of neutral amino acids with both positive and negative amino acids (claim 3). The endogenous gene taught by Collet2 is identified as a Zea mays gene, and Zea mays is a monocot (claim 11).
Collet2 claims a maize/monocot plant cell comprising a polynucleotide encoding their instant SEQ ID NO: 295 (claims 5-7) and a maize/monocot plant comprising a polynucleotide encoding their instant SEQ ID NO: 295 (claims 14-16)
As discussed in the claim interpretation section, any plant having the required substitutions/mismatches is encompassed by the instant claims not matter how the substitutions/mismatches were made. The process by which a product is made is only given weight for the structural features conferred by the process. In this case, the three mismatches discussed, above, which substitute either a positive or a negative charge for a neutral charge satisfy the limitations of the instant claims.
With regard to claim 4, it is unclear what claim 4 actually requires as far as positively charged amino acids, but the sequence taught by Collet2 has one positively charged amino acid substituted for a neutral amino acid. Furthermore, Collet2 teaches a plant cell, and the instantly claimed plant cells are not required to have the recited mutation (see claim interpretation, above).
Anticipation by Mamidi
Claim(s) 1-4 and 11 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Mamidi et al. (Nature Biotechnology (2020) Vol. 38; pp. 1203-1210, taken with the evidence of UniProt Accession Number A0A4U6UZC2 (2019).
Mamidi teaches an amino acid sequence they deposit with the UniProt database where it gets assigned Accession Number A0A4U6UZC2. This sequence has 90.8% identity to the instant SEQ ID NO: 43, see sequence search result, below:
RESULT 12
A0A4U6UZC2_SETVI
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID A0A4U6UZC2_SETVI Unreviewed; 854 AA.
AC A0A4U6UZC2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 08-OCT-2025, entry version 25.
DE RecName: Full=Potassium channel {ECO:0000256|RuleBase:RU369015};
GN ORFNames=SEVIR_4G110300v2 {ECO:0000313|EMBL:TKW20764.1};
OS Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4556 {ECO:0000313|EMBL:TKW20764.1, ECO:0000313|Proteomes:UP000298652};
RN [1] {ECO:0000313|EMBL:TKW20764.1, ECO:0000313|Proteomes:UP000298652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. A10 {ECO:0000313|Proteomes:UP000298652};
RA Huang P., Jenkins J., Grimwood J., Barry K., Healey A., Mamidi S.,
RA Sreedasyam A., Shu S., Feldman M., Wu J., Yu Y., Chen C., Johnson J.,
RA Rokhsar D., Baxter I., Schmutz J., Brutnell T., Kellogg E.;
RT "WGS assembly of Setaria viridis.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Potassium channel. {ECO:0000256|RuleBase:RU369015}.
CC -!- SUBUNIT: The potassium channel is composed of a homo- or
CC heterotetrameric complex of pore-forming subunits.
CC {ECO:0000256|RuleBase:RU369015}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU369015}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU369015}.
CC -!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
CC present in the C-terminal part is likely to be important for
CC tetramerization. {ECO:0000256|RuleBase:RU369015}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids. The pore-
CC forming region H5 is enclosed by the transmembrane segments S5 and S6
CC in the Shaker-type (1P/6TM) and contains the GYGD signature motif which
CC seems to be involved in potassium selectivity.
CC {ECO:0000256|RuleBase:RU369015}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000256|ARBA:ARBA00007929,
CC ECO:0000256|RuleBase:RU369015}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU369015}.
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DR EMBL; CM016555; TKW20764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U6UZC2; -.
DR SMR; A0A4U6UZC2; -.
DR Gramene; TKW20764; TKW20764; SEVIR_4G110300v2.
DR OMA; VWIPHTI; -.
DR Proteomes; UP000298652; Chromosome 4.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd00038; CAP_ED; 1.
DR FunFam; 2.60.120.10:FF:000074; Potassium channel KAT2; 1.
DR FunFam; 1.10.287.70:FF:000139; Potassium channel SKOR; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR045319; KAT/AKT.
DR InterPro; IPR021789; KHA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45743; POTASSIUM CHANNEL AKT1; 1.
DR PANTHER; PTHR45743:SF3; POTASSIUM CHANNEL SKOR; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11834; KHA; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU369015};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU369015};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369015};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU369015};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826,
KW ECO:0000256|RuleBase:RU369015};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW ECO:0000256|RuleBase:RU369015};
KW Reference proteome {ECO:0000313|Proteomes:UP000298652};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU369015};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU369015};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU369015};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU369015}.
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 283..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT TRANSMEM 312..336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369015"
FT DOMAIN 411..531
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REPEAT 589..621
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 622..654
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 686..718
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 765..854
FT /note="KHA"
FT /evidence="ECO:0000259|PROSITE:PS51490"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 96770 MW; B5A6FCC2B059F1A4 CRC64;
Query Match 90.8%; Score 315; Length 854;
Best Local Similarity 89.2%;
Matches 58; Conservative 3; Mismatches 4; Indels 0; Gaps 0;
Qy 1 EVVRDHIASSRGSRLALFGSELRLGRFRPRRRRRLPLAGEGAAEGFFHGLVIHPDNKWYR 60
:|||||||||||||||||||:||||| ||||||| || |||||||||| |||||||:|||
Db 32 DVVRDHIASSRGSRLALFGSDLRLGRLRPRRRRRRPLGGEGAAEGFFHDLVIHPDNRWYR 91
Qy 61 LWTKF 65
|||||
Db 92 LWTKF 96
Mamidi identifies the protein comprising their sequence as a volage gated potassium channel (see annotation for UniProt record in sequence search result, above). The neutral amino acid leucine (L) at position #35 in the instant SEQ ID NO: 43 is substituted with a positively charged arginine (R) in Mamidi’s protein sequence. The neutral amino acid glycine (G) at position #49 in the instant SEQ ID NO: 43 is substituted with a negatively charged aspartate (D) in Mamidi’s protein sequence.
These substitutions are in the N-terminal domain of a potassium channel, and alter the pattern of charged amino acids in this domain (claim 2). There are substitutions of neutral amino acids with both positive and negative amino acids (claim 3). The endogenous gene taught by Mamidi is identified as a green millet (Setaria viridis) gene, and green millet is a monocot (claim 11).
As discussed in the claim interpretation section, any plant having the required substitutions/mismatches is encompassed by the instant claims not matter how the substitutions/mismatches were made. The process by which a product is made is only given weight for the structural features conferred by the process. In this case, the two mismatches discussed, above, which substitute either a positive or a negative charge for a neutral charge satisfy the limitations of the instant claims.
With regard to claim 4, it is unclear what claim 4 actually requires as far as positively charged amino acids, but the sequence taught by Mamidi has one positively charged amino acid substituted for a neutral amino acid. Furthermore, Mamidi teaches a seed of green millet (Mamidi 1203) which is a plant part, and the instantly claimed plant parts are not required to have the recited mutation (see claim interpretation, above).
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1-4 and 11 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a naturally occurring plant which is a judicial exception without significantly more. The claim(s) recite(s) a plant comprising specific amino acid substitutions in the N-terminal domain of a voltage-gated potassium channel. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because as discussed, above, in the anticipation rejection over Mamidi, the process by which the amino acid substitutions occurred is not given weight except for the structures that are conferred. In the instant case, the endogenous wild-type voltage-gated potassium channel in green millet has an amino acid sequence that falls within the scope of the instant claim. Mimidi teaches that green millet is a wild and weedy relative of domesticated crops (Mimidi abstract). Therefore the wild green millet plant, which is a product of nature, is encompassed by the instant plant claims.
Furthermore, the claimed plant parts and plant cells are not required to have the recited mutation, and therefore, the claims encompass wild-type plant parts and plant cells which are all products of nature.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-4 and 11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 2, 5-8, and 19 of copending Application No. 19/501,215 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims are directed to a plant, a plant cell, or a plant part each of which is a species that falls within the genus claimed in the ‘215 claims.
The Examiner is unable to provide a sequence alignment because the ‘215 application submitted a defective sequence listing which has not, yet, been corrected, therefore, it is not searchable. However, the ‘215 claim 1 is broad enough to encompass the instant claims because none of the instant claims have a substitution at position 313 which is the only substitution in a stomatal voltage-gated potassium channel that is excluded. The ‘215 claim 2 specifies a mutation in one of the N-terminal alpha helices, which are in the N-terminal domain of the potassium channel. The instant SEQ ID NO: 43 has “RLGR” at positions 23-26, and this appears to be what is recited in the ‘215 claim 5. The ‘215 claim 6 recites the limitations about substituting charged amino acids for neutral amino acids, and therefore instant claims 2-4 fall within the ‘215 claim 6. The ‘215 claim 19 requires the potassium channel to be a GORK channel which the instant claims require.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Summary
No claim is allowed.
Examiner’s Contact Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CATHY KINGDON whose telephone number is (571)272-8784. The examiner can normally be reached M-F 9:00 - 5:30 EST.
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CATHY KINGDON
Primary Examiner
Art Unit 1663
/CATHY KINGDON/Primary Examiner, Art Unit 1663
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