Prosecution Insights
Last updated: October 24, 2026
Application No. 19/059,554

ENGINEERED PESTICIDAL PROTEINS AND METHODS OF CONTROLLING PLANT PESTS

Non-Final OA §101§102§112
Filed
Feb 21, 2025
Priority
Feb 20, 2019 — provisional 62/807,941 +3 more
Examiner
RADOSAVLJEVIC, ALEKSANDAR
Art Unit
1662
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Syngenta AG
OA Round
1 (Non-Final)
81%
Grant Probability
Favorable
1-2
OA Rounds
1y 2m
Est. Remaining
87%
With Interview

Examiner Intelligence

Grants 81% — above average
81%
Career Allowance Rate
101 granted / 125 resolved
+20.8% vs TC avg
Moderate +6% lift
Without
With
+6.3%
Interview Lift
resolved cases with interview
Typical timeline
2y 10m
Avg Prosecution
16 currently pending
Career history
146
Total Applications
across all art units

Statute-Specific Performance

§101
9.1%
-30.9% vs TC avg
§103
20.0%
-20.0% vs TC avg
§102
15.0%
-25.0% vs TC avg
§112
44.5%
+4.5% vs TC avg
Black line = Tech Center average estimate • Based on career data from 125 resolved cases

Office Action

§101 §102 §112
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 Applicant’s election without traverse of the species “Cry1Fa” in the reply filed on 15 July 2026 is acknowledged. SEQ ID NOs: 12-17 and 28-33 are encompassed by this species. Claims 1, 8-14, 17-22 and 25 are pending and examined herein. Claim Interpretation Claim 9 recites “a nucleotide sequence of any one of SEQ ID NOs: 19-33 or a toxin-encoding fragment thereof”. Because the claim recites the indefinite article “a”, for the purpose of examination claim the is interpreted to encompass any sequence of at least two consecutive nucleotides from any one of SEQ ID NOs: 28-33. 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. Claim 1, 8-14, 17-22 and 25 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. A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 1 recites the broad recitation of part (e) drawn to an amino acid sequence that has at least 80% identity to the amino acid sequences and toxin fragments of parts (a)-(d), and the claim also recites the amino acid sequences of parts (a)-(d), which is the narrower statement of the range/limitation. The claim is considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims. Dependent claims 8-14, 17-22 and 25 fail to recite any limitations which clarify the metes and bounds of claim 1, and are therefore rejected on the same ground. Claim 9 is indefinite in its recitation of “substantially identical”. Here, “substantially” is used an approximate term rather than a term of degree. The specification does not provide a clear definition of what is considered “substantially identical” nor is there a standard definition in the art. The specification states that such nucleotides sequences can have at least about 50% nucleotide identity when compared and aligned, or, in some embodiments “60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more nucleotide identity…” (instant specification, paragraph 00134). The scope of a claim drawn to a nucleotide with 99% identity to SEQ ID NO: 28, for example, is vastly smaller than the scope of a claim drawn to a nucleotide with 50% identity to SEQ ID NO: 28. Given the number of mutations present in a nucleotide with 50% identity to a second nucleotide, the two nucleotides could encode proteins with completely different amino acid sequences and functions. Thus, the metes and bound of claim 9 are unclear. Claim 9 is further indefinite in its recitation of “stringent hybridization conditions”. The term is a relative term of degree and is not defined in the claims or the specification. One of ordinary skill in the art would recognize that hybridization conditions may or may not be considered “stringent” based on a particular experimental scenario and that there is no single art-established standard for which hybridization conditions would be considered stringent. Thus, the metes and bounds of claim 9 are unclear. Claims 13 and 14 are indefinite in their recitation of “ (a) a monocot cell, optionally a barley cell, a maize cell, an oat cell, a rice cell, a sorghum cell, a sugarcane cell or a wheat cell; or (b) a dicot cell, optionally a soybean cell, a sunflower cell, a tomato cell, a cole crop cell, a cotton cell, a sugar beet cell or a tobacco cell” and “(a) a monocot plant, optionally a barley plant, a maize plant, an oat plant, a rice plant, a sorghum plant, a sugarcane plant or a wheat plant; or (b) a dicot plant, optionally a soybean plant, a sunflower plant, a tomato plant, a cole crop plant, a cotton plant, a sugar beet plant or a tobacco plant”, respectively. While alternative limitations are not inherently indefinite, in the instant case the claim language results in ambiguity regarding the claim scope (See MPEP 2173.05(h)). In the instant case it is unclear if the monocot or dicot cells and plants are limited to one of the recited species or if all monocot and dicot plants and cells are encompassed by the claims. Thus the metes and bounds of claims 13 and 14 are unclear. Dependent claims 17-19 fail to recite any limitations that clarify the metes and bounds of claim 14 and are rejected on the same grounds. 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 Description Claims 1, 8-14, 17-22 and 25 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 claims contain 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. Applicant claims a chimeric insecticidal protein that is toxic to lepidopteran insect pests comprising a an amino acid sequence with as little as 80% identity to the amino acid sequence of SEQ ID NOs: 12-17 or a toxin fragment of any size thereof, or an amino acid sequence with as little as 80% identity to a sequence comprising positions 1 to 597 of SEQ ID NOs: 4-5, and 7-11 or a toxin fragment of any size thereof; polynucleotides encoding said protein; vectors, transgenic plants, and compositions comprising said chimeric insecticidal protein or a polynucleotide which encodes it; and methods of making said transgenic plants and methods of using said compositions to control lepidopteran pests. Applicant claims polynucleotides encoding said chimeric insecticidal protein, wherein the polynucleotide comprises a nucleotide sequence of any one of SEQ ID NOs: 28-33, a toxin encoding fragment of any size thereof, a nucleotide sequence that is substantially identical to any one of SEQ ID NOs: 28-33, or a nucleotide sequence that anneals under stringent hybridization conditions to any one of SEQ ID NOs: 28-33. Applicant describes the full length SEQ ID NOs: 2 and 3 as Cry1 proteins BT-0002 and Cry1Fa, respectively (“Description of Sequences”, pages 8-9). Applicant describes SEQ ID NOs: 12-17 as chimeric insecticidal proteins, comprising domain I and II and a protoxin tail from BT-0002 (SEQ ID NO: 2) and domain III from Cry1Fa (SEQ ID NO: 3) (“Description of Sequences”, page 9; Table 2). These sequences share over 99% identity with each other (See Search Results of 24 Sept 2026 for SEQ ID NOs: 12-17 queried against Published Applications database). Applicant discloses that SEQ ID NOs: 12-17 have insecticidal activity against lepidopteran pests, but that this activity varies among the proteins (Tables 4 and 5). For example, the protein of SEQ ID NOs: 12 has no activity against sugarcane borer, while the proteins of SEQ ID NOs: 13-17do have activity against this pest. The protein of SEQ ID NO: 16 is the only protein of the claimed group to have activity against black cutworm. Additionally, the strength of the insecticidal activity against each of the assayed insect pests varies between the claimed proteins. Applicant describes SEQ ID NOs: 28-33 as polynucleotides which encode the amino acids of SEQ ID NOs: 12-17, respectively (“Description of Sequences”, pages 9-10). Applicant does not describe the genus of insecticidal proteins and nucleic acids encompassed by the claims. Applicant has not described sequences with as little as 80% identity to a) the amino acid sequence of SEQ ID NOs: 12-17, b) a sequence comprising positions 1 to 597 of SEQ ID NOs:12-17, or c) a toxin fragment of any size thereof and which have the required function of insecticidal activity against lepidopterans. Applicant has not described any toxin fragments, beyond those which encompass positions 1 to 597 of SEQ ID NOs:12-17 (approximately corresponding to the first three domains of the proteins; see page 86; Example 6). Examiner notes, however, Applicant does not disclose which chimeras were truncated or which pests they have activity against, but merely that two chimeras were generated and that they “were active against insect pests”. Amino acids with as little as 80% identity to the amino acid sequence of the 1168 amino acid long SEQ ID NO: 12-17, would encompass sequences with 233 substitutions, or over 20233 (1.38 x 10303) sequences—a genus of sequences that is nearly infinite in practical terms. Amino acids comprising a sequence with as little as 80% identity to positions 1 to 597 of SEQ ID NO: 12-17, or comprising a sequence with 80% identity to a toxin fragment of any size of SEQ ID NO: 12-17 would encompass a slightly smaller, but nonetheless vast, genus of sequences. In addition, Applicant has not described polynucleotides which anneal under stringent hybridization conditions to SEQ ID NOs: 28-33 or with polynucleotides which are “substantially identical” to SEQ ID NOs: 28-33. One of ordinary skill in the art would recognize that even under stringent hybridization conditions, the degree of identity between the two polynucleotides could and does vary. As evidenced by Fourgoux-Nicol et al, a probe having less than 50% sequence identity to a polynucleotide fragment could hybridize with that polynucleotide under stringent conditions that include three consecutive 30 min washes in 2X, 1X, and 0.1X SSC with 0.1% SDS at 650C. (Plant Mol. Biol. (1999) 40: 857-872; see page 859, left col., 2nd paragraph; page 862, Fig. 2). As explained in the 112(b) rejection of claim 9 above, “substantially identical” encompasses as little as 50% sequence identity. These teachings indicate that the claims would encompass polynucleotide sequences with as little as 50% identity to SEQ ID NOs: 28-33, which are 3507 nucleotides long. And because a mutation in one nucleotide could result in a difference at one encoded amino acid, a polynucleotide which has as little as 50% identity to SEQ ID NOs: 28-33 (and thus differs from said sequences at 1753 positions) could encode a polypeptide with no identity to SEQ ID NO: 12-17, which are 1168 amino acids long, and which may or may not have the claimed insecticidal function. It is noted that a definition by function alone “does not suffice” to sufficiently describe a coding sequence “because it is only an indication of what the gene does, rather than what it is.” Eli Lilly, 119 F.3 at 1568, 43 USPQ2d at 1406. See also Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen Inc. v. Chugai Pharm. Co., 927 F.2d 1200, 18 USPQ2d 1016 (Fed. Cir. 1991)). The specification does not describe the structures that are necessary and sufficient for the required insecticidal function of the claimed chimeric proteins. Furthermore, the chimeric Cry proteins that are disclosed in the specification do not provide the missing structure-function relationship because, as indicated in Tables 4 and 5, said chimeric proteins have substantially different function (insecticidal activity) even though SEQ ID NOs: 12-17 have only minor differences in their primary structure (amino acid sequence). And while the prior art does teach chimeric Cry toxins (see, for example, Cardineau et al (US Patent 6,218,188), it appears to be silent with regard to the specific combination of domains that make up the full-length SEQ ID NOs: 12-17. Given the size of the genera encompassed by the claims, the described species are not sufficiently representative. In addition, Applicant has failed to set forth any structural features that would allow one having ordinary skill in the art to visualize which members of the claimed genus of proteins will have the recited insecticidal activity and which do not. For these reasons, it is unclear whether at the time of filing Applicant was in possession of the invention as broadly claimed. Scope of Enablement Claims 1, 8-14, 17-22 and 25 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a chimeric insecticidal protein comprising the amino acid sequence of SEQ ID NOs: 12-17, the amino acid sequence from positions 1 to 597 of SEQ ID NO: 12-17, o, and the full-length nucleic acid sequence SEQ ID NOs: 28-33; for transgenic plants and plant cells, vectors, compositions, seeds, and products comprising said sequences; and for methods of making said transgenic plants and cells and methods of using said compositions, does not reasonably provide enablement across the full scope of the claims. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make or use the invention commensurate in scope with these claims. In re Wands, 858 F.2d 731 (Fed. Cir. 1988) lists the following eight factors for determining whether undue experimentation would be required to practice an invention: (1) quantity of experimentation necessary; (2) amount of direction or guidance supplied; (3) presence or absence of working examples; (4) nature of the invention; (5) state of the prior art; (6) relative skill of those in the art; (7) predictability or unpredictability or the prior art; (8) breadth of the claims. Applicant claims a chimeric insecticidal protein that is toxic to lepidopteran insect pests comprising a an amino acid sequence with as little as 80% identity to the amino acid sequence of SEQ ID NOs: 12-17 or a toxin fragment of any size thereof, or an amino acid sequence with as little as 80% identity to a sequence comprising positions 1 to 597 of SEQ ID NOs: 4-5, and 7-11 or a toxin fragment of any size thereof; polynucleotides encoding said protein; vectors, transgenic plants, and compositions comprising said chimeric insecticidal protein or a polynucleotide which encodes it; and methods of making said transgenic plants and methods of using said compositions to control lepidopteran pests. Applicant claims polynucleotides encoding said chimeric insecticidal protein, wherein the polynucleotide comprises a nucleotide sequence of any one of SEQ ID NOs: 28-33, a toxin encoding fragment of any size thereof, a nucleotide sequence that is substantially identical to any one of SEQ ID NOs: 28-33, or a nucleotide sequence that anneals under stringent hybridization conditions to any one of SEQ ID NOs: 28-33. Applicant claims methods of making transgenic plants comprising polynucleotides encoding said chimeric insecticidal proteins and methods of using said insecticidal compositions to control lepidopteran pests. Applicant teaches the full length SEQ ID NOs: 2 and 3 as Cry1 proteins BT-0002 and Cry1Fa, respectively (“Description of Sequences”, pages 8-9). Applicant teaches SEQ ID NOs: 12-17 as chimeric insecticidal proteins, comprising domain I and II and a protoxin tail from BT-0002 (SEQ ID NO: 2) and domain III from Cry1Fa (SEQ ID NO: 3) (“Description of Sequences”, page 9; Table 2). These sequences share over 99% identity with each other (See Search Results of 24 Sept 2026 for SEQ ID NOs: 12-17 queried against Published Applications database). Applicant teaches that SEQ ID NOs: 12-17 have insecticidal activity against lepidopteran pests, but that this activity varies among the proteins (Tables 4 and 5). For example, the protein of SEQ ID NOs: 12 has no activity against sugarcane borer, while the proteins of SEQ ID NOs: 13-17do have activity against this pest. The protein of SEQ ID NO: 16 is the only protein of the claimed group to have activity against black cutworm. Additionally, the strength of the insecticidal activity against each of the assayed insect pests varies between the claimed proteins. Applicant teaches SEQ ID NOs: 28-33 as polynucleotides which encode the amino acids of SEQ ID NOs: 12-17, respectively (“Description of Sequences”, pages 9-10). Applicant does not teach how to predictably make or use the genus of insecticidal proteins and nucleic acids encompassed by the claims. Applicant has not taught sequences with as little as 80% identity to a) the amino acid sequence of SEQ ID NOs: 12-17, b) a sequence comprising positions 1 to 597 of SEQ ID NOs:12-17, or c) a toxin fragment of any size thereof and which have the required function of insecticidal activity against lepidopterans. Applicant has not taught any toxin fragments, beyond those which encompass positions 1 to 597 of SEQ ID NOs:12-17 (approximately corresponding to the first three domains of the proteins; see page 86; Example 6). Examiner notes, however, Applicant does not teach which chimeras were truncated or which pests they have activity against, but merely that two chimeras were generated and that they “were active against insect pests”. Amino acids with as little as 80% identity to the amino acid sequence of the 1168 amino acid long SEQ ID NO: 12-17, would encompass sequences with 233 substitutions, or over 20233 (1.38 x 10303) sequences—a genus of sequences that is nearly infinite in practical terms. Amino acids comprising a sequence with as little as 80% identity to positions 1 to 597 of SEQ ID NO: 12-17, or comprising a sequence with 80% identity to a toxin fragment of any size of SEQ ID NO: 12-17 would encompass a slightly smaller, but nonetheless vast, genus of sequences. Similarly, Applicant has not taught polynucleotides which anneal under stringent hybridization conditions to SEQ ID NOs: 28-33 or polynucleotides which are “substantially identical” to SEQ ID NOs: 28-33, which would encompass polynucleotide sequences with as little as 50% identity to SEQ ID NOs: 28-33, which are 3507 nucleotides long. Given that a polynucleotide which has as little as 50% identity to SEQ ID NOs: 28-33 (and thus differs from said sequences at 1753 positions) could encode a polypeptide with no identity to SEQ ID NOs: 12-17, (which are 1168 amino acids long), and which may or may not have the claimed insecticidal function. This would amount to a very large genus of sequences. Applicant has failed to teach the genus of nucleic acids encoding the claimed genus of insecticidal proteins. Both the specification and the state of the art indicate that it would be highly unpredictable to attempt to practice the invention through the full scope of the claims. For example, besides the full-length chimeric Cry1 proteins identified in Table 2, the specification teaches no variants or fragments having the recited activity. The specification does not teach which structures within the chimeric proteins would be necessary and sufficient for the recited function. And while the prior art does teach chimeric Cry toxins, it appears to be silent with regard to the specific combination of domains that make up the full-length SEQ ID NOs: 12-17. At the same time, it is well-known in the art that making random mutations in delta endotoxins is highly unpredictable. For example, Pardo-Lopez et al teach that although site-targeted mutagenesis has been extensively used to study Cry protein domains, most of the tested mutations adversely affect the proteins’ toxicity (Pardo Lopez et al, Peptides (2009) 30:589-595, pp. 591-92). Aronson et al teach that the interactions between the three structural domains of the Cry proteins are critical for the proteins' toxicity (Aronson et al, FEMS Microbiol. Lett. (2001) 195:1-8, p. 7). Herrero et al teach that even a two-amino acid mutation may be sufficient to dramatically disrupt those interactions (Herrero et al., Biochem. J. (2004) 384:507–513, p. 510). Moreover, even a single amino acid substitution has been shown to reduce the toxicity towards one species of an insect without affecting it towards another (Abdul-Rauf et al, Curr. Microbiol. (1999) 39, 94-98, p. 95). In the context of a hybrid delta endotoxin, specifically, Malvar et al teach that while altering the “exchange site” between the two parental endotoxins can produce improvements in toxicity against some target species, “It is important to note that improvements in hybrid delta-endotoxin bioactivity by altering exchange sites is unpredictable” (US Patent Publication 2003/0119158; paragraph 00313). Given limited guidance supplied by Applicant, the breadth of the claims and the nature of the invention, as well as the unpredictability in the art, it would have required one skilled in the art undue trial and error experimentation to practice the claimed invention through the full scope of its claims. 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, 8-9, 20 and 25 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (product of nature) without significantly more. Claim 1 is drawn to a chimeric insecticidal protein that is toxic to lepidopteran insect pests comprising wherein the protein comprises an amino acid sequence with at least 80% identity to a) the amino acid sequence of positions 1 to 597 of any one of SEQ ID NOs: 12-17, b) the amino acid sequence of any one of SEQ ID NOs: 12-17, or c) a toxin fragment of a or b. Dependent claims 8 and 9 are drawn to a polynucleotide comprising a nucleotide sequence encoding the chimeric insecticidal protein of claim 1. Dependent claims 20 and 25 are drawn to an insecticidal composition comprising the chimeric insecticidal protein of claim 1 and a method of controlling lepidopteran pests by administering said composition, respectively. The claims do not include any additional elements that are sufficient to amount to significantly more than the judicial exception because they read on naturally occurring proteins and compositions comprising said proteins and do not recite any additional structural limitations that would distinguish the claimed invention form a product of nature. The claims are broadly drawn to a chimeric insecticidal protein comprising portions of two different Cry1 proteins with a crossover position in conserved block 3. However, chimeric refers to how a protein was made and does not impart any requisite structural features on said protein. If the resulting structure, i.e. the amino acid sequence in the instant case, is identical to a naturally occurring structure and the method does not impart any additional structural features, the instantly recited protein reads on the naturally occurring protein. There would be no way to distinguish two proteins, one chimeric and one not chimeric, from each other if their respective amino acid sequences were identical. Thus, the claims encompass naturally occurring proteins to the extent that that structures meet the recited claim limitations, such as UniProt Accession Q45738 (uniprot.org/uniprotkb/Q45738/entry; integrated 30 May 2000). UniProt Accession Q45738, an amino acid sequence of a Cry1Ja protein isolated from Bacillus thuringiensis strain NRRL B-21110 / EG5847 with activity against lepidopterans, has at least 92% identity to SEQ ID NOs: 12-17. Thus, claims 1 encompass the naturally occurring Cry1Ja protein of UniProt Accession Q45738 and is drawn to a judicial exception, i.e. a natural product. Alignment of SEQ ID NO: 12 and UniProt Accession Q45738: Query Match 92.7%; Score 5731.5; Length 1167; Best Local Similarity 92.7%; Matches 1083; Conservative 24; Mismatches 60; Indels 1; Gaps 1; Qy 1 MEINNQKQCIPYNCLSNPEEVLLDGERILPDIDPLEVSLSLLQFLLNNFVPGGGFISGLV 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 MEINNQKQCIPYNCLSNPEEVLLDGERILPDIDPLEVSLSLLQFLLNNFVPGGGFISGLV 60 Qy 61 DKIWGALRPSEWDLFLAQIERLIDQRIEATVRAKAIA ELEGLGRSYQLYGEAFKEWEKTP 120 |||||||||||||||||||||||||||||||||||| |||||||:||:| ||||||| | Db 61 DKIWGALRPSEWDLFLAQIERLIDQRIEATVRAKAITELEGLGRNYQIYAEAFKEWESDP 120 Qy 121 DNTAARSRVTERFRIIDAQIEANIPSFRVSGFEVPLLLVYTQAANLHLALLRDSVVFGER 180 || ||:||| :||||:| |||||||||: ||||||| || ||||||||||||||:|||| Db 121 DNEAAKSRVIDRFRILDGLIEANIPSFRIIGFEVPLLSVYVQAANLHLALLRDSVIFGER 180 Qy 181 WGLTTTNVNDIYNRQVNRIGEYSNHCVDTYNTELERLGFRSIAQWRIYNQFRRELTLTVL 240 ||||| |||||||||: | |||||||||||||||||||||||||||||||||||||||| Db 181 WGLTTKNVNDIYNRQIREIHEYSNHCVDTYNTELERLGFRSIAQWRIYNQFRRELTLTVL 240 Qy 241 DIVALFPNYDSRLYPIQTFSQLTREIVTSPVSEFYYGVINSGNINGTLTEQQIRRPHLMD 300 |||||||||||||||||||||||||||||||||||||||||||| ||||||||||||||| Db 241 DIVALFPNYDSRLYPIQTFSQLTREIVTSPVSEFYYGVINSGNIIGTLTEQQIRRPHLMD 300 Qy 301 FFNSMIMYTSDNRREHYWSGLEMTAYFTGFAGAQVSFPLVGTRGESAPPLTVRSVNDGIY 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 FFNSMIMYTSDNRREHYWSGLEMTAYFTGFAGAQVSFPLVGTRGESAPPLTVRSVNDGIY 360 Qy 361 RILSAPFYSAPFLGTIVLGSRGEKFDFALNNISPPPSTIYRHPGTVDSLVSIPPQDNSVP 420 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 361 RILSAPFYSAPFLGTIVLGSRGEKFDFALNNISPPPSTIYRHPGTVDSLVSIPPQDNSVP 420 Qy 421 PHRGSSHRLSHVTMRASSPIFHWTHRSATTTNTINPNAIIQIPLVKAHTLQSGTTVVRGP 480 ||||||||||||||||||||||||||||||||||||||||||||||| | || |||||| Db 421 PHRGSSHRLSHVTMRASSPIFHWTHRSATTTNTINPNAIIQIPLVKAFNLHSGATVVRGP 480 Qy 481 GFTGGDILRRTSGGPFAYTIVNINGQLPQRYRARIRYASTTNLRIYVTVAGERIFAGQFN 540 |||||||||||: | || ||| | | |||| ||||||||:|: : : | : | | Db 481 GFTGGDILRRTNTGTFADMRVNITGPLSQRYRVRIRYASTTDLQFFTRINGTSVNQGNFQ 540 Qy 541 KTMDTGDPLTFQSFSYATINTAFTFPMSQSSFTVGADTFSSGNEVYIDRFELIPVTATFE 600 :||: || | :| | :| |:| :||:||:| ||: |||||| | :| ||| Db 541 RTMNRGDNLESGNFRTAGFSTPFSFSNAQSTFTLGTQAFSN-QEVYIDRIEFVPAEVTFE 599 Qy 601 AESDLERAQKAVNALFTSTNQLGLKTDVTDYQIDQVSNLVECLSDEFCLDEKRELSEKVK 660 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 600 AESDLERAQKAVNALFTSTNQLGLKTDVTDYQIDQVSNLVECLSDEFCLDEKRELSEKVK 659 Qy 661 HAKRLSDKRNLLQDPNFTSINRQLDRGWRGSTDITIQGGNDVFKENYVTLPGTFDECYPT 720 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 660 HAKRLSDKRNLLQDPNFTSINRQLDRGWRGSTDITIQGGNDVFKENYVTLPGTFDECYPT 719 Qy 721 YLYQKIDESKLKAYTRYELRGYIEDSQDLEVYLIRYNAKHETVNVPGTGSLWPLSVESPI 780 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 720 YLYQKIDESKLKAYTRYELRGYIEDSQDLEVYLIRYNAKHETVNVPGTGSLWPLSVESPI 779 Qy 781 GRCGEPNRCVPHIEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIK 840 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 780 GRCGEPNRCVPHIEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIK 839 Qy 841 TQDGHARLGNLEFLEEKPLLGEALARVKRAEKKWRDKREQLQFETNIVYKEAKESVDALF 900 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 840 TQDGHARLGNLEFLEEKPLLGEALARVKRAEKKWRDKREQLQFETNIVYKEAKESVDALF 899 Qy 901 VDSHYNRLQADTNITMIHAADKRVHRIREAYLPELSVIPGVNADIFEELEGLIFTAFSLY 960 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 900 VDSHYNRLQADTNITMIHAADKRVHRIREAYLPELSVIPGVNADIFEELEGLIFTAFSLY 959 Qy 961 DARNIIKNGDFNNGLSCWNVKGHVDIQQNDHRSVLVVPEWESEVSQEVRVCPGRGYILRV 1020 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 960 DARNIIKNGDFNNGLSCWNVKGHVDIQQNDHRSVLVVPEWESEVSQEVRVCPGRGYILRV 1019 Qy 1021 TAYKEGYGEGCVTIHEIEDNTDELKFSNCIEEEVYPTDTGNDYTAHQGTTGCADACNSRN 1080 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1020 TAYKEGYGEGCVTIHEIEDNTDELKFSNCIEEEVYPTDTGNDYTAHQGTTGCADACNSRN 1079 Qy 1081 VGYEDGYEINTTASVNYKPTYEEEMYTDVRRDNHCEYDRGYGNHTPLPAGYVTKELEYFP 1140 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1080 VGYEDGYEINTTASVNYKPTYEEEMYTDVRRDNHCEYDRGYGNHTPLPAGYVTKELEYFP 1139 Qy 1141 ETDTVWIEIGETEGTFIVDSVELLLMEE 1168 |||||||||||||||||||||||||||| Db 1140 ETDTVWIEIGETEGTFIVDSVELLLMEE 1167 Dependent claims 8-9 are drawn to a polynucleotide encoding the protein of claim 1. The protein of UniProt Accession Q45738 would be natively encoded by a nucleic acid comprising a polynucleotide in the genetic material of the source bacterium. Claim 9 only requires two consecutive nucleotides of any one of SEQ ID NOs: 28-33, which said nucleic acid encoding UniProt Accession Q45738 would inherently comprise. Thus, claims 8-9 are not directed to significantly more than a product of nature. Claims 20 and 25 are Dependent claims 20 and 25 are drawn to an insecticidal composition comprising the chimeric insecticidal protein of claim 1 and a method of controlling lepidopteran pests by administering said composition Dependent claim 20 recites the additional elements of “an insecticidal composition” which comprises chimeric insecticidal protein of claim 1 and “an agriculturally acceptable carrier”. As explained above, chimeric insecticidal protein of claim 1 encompasses a naturally occurring Cry1 protein isolated from a naturally occurring B. thuringiensis strain. In nature, B. thuringiensis is dispersed onto plants by means including animal defecation and rain splash (Argolo-Filho et al, 2014, Insects 5:62-91, See Figure 1). An agriculturally acceptable carrier encompasses water. Thus, the claims encompass rain splash comprising naturally occurring B. thuringiensis. Thus, the claims are not directed to significantly more than products of nature. Dependent claim 25 is drawn to a method of controlling a lepidopteran pest, comprising delivering to the pest or an environment thereof an insecticidal composition comprising the chimeric insecticidal protein of claim 1. As discussed above, the chimeric insecticidal protein of claim 1 encompasses a naturally occurring Cry1 protein isolated from a naturally occurring B. thuringiensis strain and an insecticidal composition comprising said Cry1 protein and water (via rain splash) is also a natural product. The judicial exception is not integrated into a practical application because the active step of the claimed method, in its entirety, would encompass the naturally occurring process by which an insect pest, which would inherently live on a plant at some point during its life cycle, would come into contact with said composition distributed by rain splash. The judicial exception is not integrated into a practical application because the claimed method, in its entirety, reads on the natural phenomenon described above. 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)(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 and 8-9 are rejected under are rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Accession Q45738 (uniprot.org/uniprotkb/Q45738/entry; integrated 30 May 2000). Claim 1 is drawn to a chimeric insecticidal protein that is toxic to lepidopteran insect pests comprising an amino acid sequence with at least 80% identity to a) the amino acid sequence of positions 1 to 597 of any one of SEQ ID NOs: 12-17, b) the amino acid sequence of any one of SEQ ID NOs: 12-17, or c) a toxin fragment of a or b. Dependent claims 8 and 9 are drawn to a polynucleotide comprising a nucleotide sequence encoding the chimeric insecticidal protein of claim 1. The claims are broadly drawn to a chimeric insecticidal protein comprising portions of two different Cry1 proteins with a crossover position in conserved block 3. However, chimeric refers to how a protein was made and does not impart any requisite structural features on said protein. If the resulting structure, i.e. the amino acid sequence in the instant case, is identical to a naturally occurring structure and the method does not impart any additional structural features, the instantly recited protein reads on the naturally occurring protein. There would be no way to distinguish two proteins, one chimeric and one not chimeric, from each other if their respective amino acid sequences were identical. UniProt Accession Q45738 discloses an amino acid sequence of a Cry1Ja protein isolated from Bacillus thuringiensis strain NRRL B-21110 / EG5847 with activity against lepidopterans, has at least 92% identity to SEQ ID NOs: 12-17. Alignment of SEQ ID NO: 12 and UniProt Accession Q45738: Query Match 92.7%; Score 5731.5; Length 1167; Best Local Similarity 92.7%; Matches 1083; Conservative 24; Mismatches 60; Indels 1; Gaps 1; Qy 1 MEINNQKQCIPYNCLSNPEEVLLDGERILPDIDPLEVSLSLLQFLLNNFVPGGGFISGLV 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 MEINNQKQCIPYNCLSNPEEVLLDGERILPDIDPLEVSLSLLQFLLNNFVPGGGFISGLV 60 Qy 61 DKIWGALRPSEWDLFLAQIERLIDQRIEATVRAKAIA ELEGLGRSYQLYGEAFKEWEKTP 120 |||||||||||||||||||||||||||||||||||| |||||||:||:| ||||||| | Db 61 DKIWGALRPSEWDLFLAQIERLIDQRIEATVRAKAITELEGLGRNYQIYAEAFKEWESDP 120 Qy 121 DNTAARSRVTERFRIIDAQIEANIPSFRVSGFEVPLLLVYTQAANLHLALLRDSVVFGER 180 || ||:||| :||||:| |||||||||: ||||||| || ||||||||||||||:|||| Db 121 DNEAAKSRVIDRFRILDGLIEANIPSFRIIGFEVPLLSVYVQAANLHLALLRDSVIFGER 180 Qy 181 WGLTTTNVNDIYNRQVNRIGEYSNHCVDTYNTELERLGFRSIAQWRIYNQFRRELTLTVL 240 ||||| |||||||||: | |||||||||||||||||||||||||||||||||||||||| Db 181 WGLTTKNVNDIYNRQIREIHEYSNHCVDTYNTELERLGFRSIAQWRIYNQFRRELTLTVL 240 Qy 241 DIVALFPNYDSRLYPIQTFSQLTREIVTSPVSEFYYGVINSGNINGTLTEQQIRRPHLMD 300 |||||||||||||||||||||||||||||||||||||||||||| ||||||||||||||| Db 241 DIVALFPNYDSRLYPIQTFSQLTREIVTSPVSEFYYGVINSGNIIGTLTEQQIRRPHLMD 300 Qy 301 FFNSMIMYTSDNRREHYWSGLEMTAYFTGFAGAQVSFPLVGTRGESAPPLTVRSVNDGIY 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 FFNSMIMYTSDNRREHYWSGLEMTAYFTGFAGAQVSFPLVGTRGESAPPLTVRSVNDGIY 360 Qy 361 RILSAPFYSAPFLGTIVLGSRGEKFDFALNNISPPPSTIYRHPGTVDSLVSIPPQDNSVP 420 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 361 RILSAPFYSAPFLGTIVLGSRGEKFDFALNNISPPPSTIYRHPGTVDSLVSIPPQDNSVP 420 Qy 421 PHRGSSHRLSHVTMRASSPIFHWTHRSATTTNTINPNAIIQIPLVKAHTLQSGTTVVRGP 480 ||||||||||||||||||||||||||||||||||||||||||||||| | || |||||| Db 421 PHRGSSHRLSHVTMRASSPIFHWTHRSATTTNTINPNAIIQIPLVKAFNLHSGATVVRGP 480 Qy 481 GFTGGDILRRTSGGPFAYTIVNINGQLPQRYRARIRYASTTNLRIYVTVAGERIFAGQFN 540 |||||||||||: | || ||| | | |||| ||||||||:|: : : | : | | Db 481 GFTGGDILRRTNTGTFADMRVNITGPLSQRYRVRIRYASTTDLQFFTRINGTSVNQGNFQ 540 Qy 541 KTMDTGDPLTFQSFSYATINTAFTFPMSQSSFTVGADTFSSGNEVYIDRFELIPVTATFE 600 :||: || | :| | :| |:| :||:||:| ||: |||||| | :| ||| Db 541 RTMNRGDNLESGNFRTAGFSTPFSFSNAQSTFTLGTQAFSN-QEVYIDRIEFVPAEVTFE 599 Qy 601 AESDLERAQKAVNALFTSTNQLGLKTDVTDYQIDQVSNLVECLSDEFCLDEKRELSEKVK 660 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 600 AESDLERAQKAVNALFTSTNQLGLKTDVTDYQIDQVSNLVECLSDEFCLDEKRELSEKVK 659 Qy 661 HAKRLSDKRNLLQDPNFTSINRQLDRGWRGSTDITIQGGNDVFKENYVTLPGTFDECYPT 720 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 660 HAKRLSDKRNLLQDPNFTSINRQLDRGWRGSTDITIQGGNDVFKENYVTLPGTFDECYPT 719 Qy 721 YLYQKIDESKLKAYTRYELRGYIEDSQDLEVYLIRYNAKHETVNVPGTGSLWPLSVESPI 780 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 720 YLYQKIDESKLKAYTRYELRGYIEDSQDLEVYLIRYNAKHETVNVPGTGSLWPLSVESPI 779 Qy 781 GRCGEPNRCVPHIEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIK 840 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 780 GRCGEPNRCVPHIEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIK 839 Qy 841 TQDGHARLGNLEFLEEKPLLGEALARVKRAEKKWRDKREQLQFETNIVYKEAKESVDALF 900 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 840 TQDGHARLGNLEFLEEKPLLGEALARVKRAEKKWRDKREQLQFETNIVYKEAKESVDALF 899 Qy 901 VDSHYNRLQADTNITMIHAADKRVHRIREAYLPELSVIPGVNADIFEELEGLIFTAFSLY 960 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 900 VDSHYNRLQADTNITMIHAADKRVHRIREAYLPELSVIPGVNADIFEELEGLIFTAFSLY 959 Qy 961 DARNIIKNGDFNNGLSCWNVKGHVDIQQNDHRSVLVVPEWESEVSQEVRVCPGRGYILRV 1020 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 960 DARNIIKNGDFNNGLSCWNVKGHVDIQQNDHRSVLVVPEWESEVSQEVRVCPGRGYILRV 1019 Qy 1021 TAYKEGYGEGCVTIHEIEDNTDELKFSNCIEEEVYPTDTGNDYTAHQGTTGCADACNSRN 1080 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1020 TAYKEGYGEGCVTIHEIEDNTDELKFSNCIEEEVYPTDTGNDYTAHQGTTGCADACNSRN 1079 Qy 1081 VGYEDGYEINTTASVNYKPTYEEEMYTDVRRDNHCEYDRGYGNHTPLPAGYVTKELEYFP 1140 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1080 VGYEDGYEINTTASVNYKPTYEEEMYTDVRRDNHCEYDRGYGNHTPLPAGYVTKELEYFP 1139 Qy 1141 ETDTVWIEIGETEGTFIVDSVELLLMEE 1168 |||||||||||||||||||||||||||| Db 1140 ETDTVWIEIGETEGTFIVDSVELLLMEE 1167 Dependent claims 8-9 are drawn to a polynucleotide encoding the protein of claim 1. The protein of UniProt Accession Q45738 would be inherently encoded by a nucleic acid comprising a polynucleotide in the genetic material of the source bacterium. Claim 9 only requires two consecutive nucleotides of any one of SEQ ID NOs: 28-33, which said nucleic acid encoding UniProt Accession Q45738 would inherently comprise. Thus UniProt Accession Q45738 anticipates all the limitations of claims 1 and 8-9. Claims 1, 8-9, 10-14, 17-22 and 25 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Baum et al (US 20220281927 A1, Priority Date of 16 October 2014). The claims are broadly drawn to a chimeric insecticidal protein that is toxic to lepidopteran insect pests comprising an amino acid sequence with at least 80% identity to a) the amino acid sequence of positions 1 to 597 of any one of SEQ ID NOs: 12-17, b) the amino acid sequence of any one of SEQ ID NOs: 12-17, or c) a toxin fragment of a or b. The claims are further drawn to polynucleotides encoding the chimeric insecticidal protein; cells, plants, plant products and compositions comprising said chimeric insecticidal protein or the polynucleotide encoding it; methods of making transgenic plants by transformation, and methods of controlling lepidopteran pests by delivering said composition to said pests. Regarding instant claims 1 Baum et al discloses a chimeric insecticidal protein comprising the amino acid sequence of SEQ ID NO: 50, wherein the insecticidal protein is toxic to lepidopteran pests (claims 1-2; Table 4). Baum et al discloses that SEQ ID NO: 50 comprises domains I and II of a Cry1Ja1 protein, domain III of a Cry1Jx protein (a different Cry1 protein), and a protoxin tail (page 13, Table 1). Regarding instant claims 1 Baum et al’s SEQ ID NO: 50 has 83.1% sequence identity to the amino acid sequence of instant SEQ ID NO: 12: Query Match 83.1%; Score 5137.5; Length 1143; Best Local Similarity 84.1%; Matches 989; Conservative 54; Mismatches 92; Indels 41; Gaps 7; Qy 1 MEINNQKQCIPYNCLSNPEEVLLDGERILPDIDPLEVSLSLLQFLLNNFVPGGGFISGLV 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 MEINNQKQCIPYNCLSNPEEVLLDGERILPDIDPLEVSLSLLQFLLNNFVPGGGFISGLV 60 Qy 61 DKIWGALRPSEWDLFLAQIERLIDQRIEATVRAKAIA ELEGLGRSYQLYGEAFKEWEKTP 120 |||||||||||||||||||||||||||||||||||| |||||||:||:| ||||||| | Db 61 DKIWGALRPSEWDLFLAQIERLIDQRIEATVRAKAITELEGLGRNYQIYAEAFKEWESDP 120 Qy 121 DNTAARSRVTERFRIIDAQIEANIPSFRVSGFEVPLLLVYTQAANLHLALLRDSVVFGER 180 || ||:||| :||||:| |||||||||: ||||||| || ||||||||||||||:|||| Db 121 DNEAAKSRVIDRFRILDGLIEANIPSFRIIGFEVPLLSVYVQAANLHLALLRDSVIFGER 180 Qy 181 WGLTTTNVNDIYNRQVNRIGEYSNHCVDTYNTELERLGFRSIAQWRIYNQFRRELTLTVL 240 ||||| |||||||||: | |||||||||||||||||||||||||||||||||||||||| Db 181 WGLTTKNVNDIYNRQIREIHEYSNHCVDTYNTELERLGFRSIAQWRIYNQFRRELTLTVL 240 Qy 241 DIVALFPNYDSRLYPIQTFSQLTREIVTSPVSEFYYGVINSGNINGTLTEQQIRRPHLMD 300 |||||||||||||||||||||||||||||||||||||||||||| ||||||||||||||| Db 241 DIVALFPNYDSRLYPIQTFSQLTREIVTSPVSEFYYGVINSGNIIGTLTEQQIRRPHLMD 300 Qy 301 FFNSMIMYTSDNRREHYWSGLEMTAYFTGFAGAQVSFPLVGTRGESAPPLTVRSVNDGIY 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 FFNSMIMYTSDNRREHYWSGLEMTAYFTGFAGAQVSFPLVGTRGESAPPLTVRSVNDGIY 360 Qy 361 RILSAPFYSAPFLGTIVLGSRGEKFDFALNNISPPPSTIYRHPGTVDSLVSIPPQDNSVP 420 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 361 RILSAPFYSAPFLGTIVLGSRGEKFDFALNNISPPPSTIYRHPGTVDSLVSIPPQDNSVP 420 Qy 421 PHRGSSHRLSHVTMRASSPIFHWTHRSATTTNTINPNAIIQIPLVKAHTLQSGTTVVRGP 480 ||||||||||||||||||||||||||||||||||||||||||||||| | || |||||| Db 421 PHRGSSHRLSHVTMRASSPIFHWTHRSATTTNTINPNAIIQIPLVKAFNLHSGATVVRGP 480 Qy 481 GFTGGDILRRTSGGPFAYTIVNINGQL-PQRYRARIRYASTTNLRIYVTVAGERIFAGQF 539 ||||||:||||: | || ||: | |||| ||||||||:|: : : | : | | Db 481 GFTGGDLLRRTNTGTFADIRVNVPSSLFSQRYRVRIRYASTTDLQFFTRINGTSVNQGNF 540 Qy 540 NKTMDTGDPLTFQSFSYATINTAFTFPMSQSSFTVGADTFSSGNEVYIDRFELIPVTATF 599 :|||| || | ::| | :| | | ||:||:| ||: |||||| | :| || Db 541 SKTMDRGDKLKSENFRTAGFSTPFRFSNFQSTFTLGTQAFSN-QEVYIDRIEFVPAEVTF 599 Qy 600 EAESDLERAQKAVNALFTSTNQLGLKTDVTDYQIDQVSNLVECLSDEFCLDEKRELSEKV 659 |||||||||||||| ||||:||:||||||||| ||||||||||||||||||||:|||||| Db 600 EAESDLERAQKAVNELFTSSNQIGLKTDVTDYHIDQVSNLVECLSDEFCLDEKKELSEKV 659 Qy 660 KHAKRLSDKRNLLQDPNFTSINRQLDRGWRGSTDITIQGGNDVFKENYVTLPGTFDECYP 719 ||||||||:||||||||| ||||||||||||||||||||:|||||||||| |||||||| Db 660 KHAKRLSDERNLLQDPNFRGINRQLDRGWRGSTDITIQGGDDVFKENYVTLLGTFDECYP 719 Qy 720 TYLYQKIDESKLKAYTRYELRGYIEDSQDLEVYLIRYNAKHETVNVPGTGSLWPLSVESP 779 ||||||||||||||||||:||||||||||||:|||||||||||||||||||||||| || Db 720 TYLYQKIDESKLKAYTRYQLRGYIEDSQDLEIYLIRYNAKHETVNVPGTGSLWPLSAPSP 779 Qy 780 IGRCGEPNRCVPHIEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKI 839 || |||||||||||||||||||||||||||||||| Db 780 IG--------------------------KCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKI 813 Qy 840 KTQDGHARLGNLEFLEEKPLLGEALARVKRAEKKWRDKREQLQFETNIVYKEAKESVDAL 899 ||||||||||||||||||||:|||||||||||||||||||:|::|||||||||||||||| Db 814 KTQDGHARLGNLEFLEEKPLVGEALARVKRAEKKWRDKREKLEWETNIVYKEAKESVDAL 873 Qy 900 FVDSHYNRLQADTNITMIHAADKRVHRIREAYLPELSVIPGVNADIFEELEGLIFTAFSL 959 ||:| |:|||||||| |||||||||| ||||||||||||||||| ||||||| ||||||| Db 874 FVNSQYDRLQADTNIAMIHAADKRVHSIREAYLPELSVIPGVNAAIFEELEGRIFTAFSL 933 Qy 960 YDARNIIKNGDFNNGLSCWNVKGHVDI-QQNDHRSVLVVPEWESEVSQEVRVCPGRGYIL 1018 |||||:||||||||||||||||||||: :||:|||||||||||:|||||||||||||||| Db 934 YDARNVIKNGDFNNGLSCWNVKGHVDVEEQNNHRSVLVVPEWEAEVSQEVRVCPGRGYIL 993 Qy 1019 RVTAYKEGYGEGCVTIHEIEDNTDELKFSNCIEEEVYP--TDTGNDYTA----HQGTTGC 1072 ||||||||||||||||||||:||||||||||:|||||| | | ||||| ::|| Db 994 RVTAYKEGYGEGCVTIHEIENNTDELKFSNCVEEEVYPNNTVTCNDYTATQEEYEGT--- 1050 Qy 1073 ADACNSRNVGYEDGYEINTTASVNYKPTYEEEMYTDVRRDNHCEYDRGYGNHTPLPAGYV 1132 ||| ||: || |:: :| |||: ||| |||| || :||||::|||||||| Db 1051 ---YTSRNRGYDGAYESNSSVPADYASAYEEKAYTDGRRDNPCESNRGYGDYTPLPAGYV 1107 Qy 1133 TKELEYFPETDTVWIEIGETEGTFIVDSVELLLMEE 1168 ||||||||||| |||||||||||||||||||||||| Db 1108 TKELEYFPETDKVWIEIGETEGTFIVDSVELLLMEE 1143 Regarding instant claims 8, 10-14, an 17-19 Baum et al discloses a polynucleotide encoding said chimeric insecticidal protein, wherein the polynucleotide is operably linked to a heterologous promoter; vectors, dicotyledonous or monocotyledonous plant cells, transgenic plants and seeds comprising said polynucleotide or chimeric insecticidal protein; and commodity products of said transgenic plants (claims 4-5, 6, 8, 13, 15, 17-18; Examples 5-6, paragraphs 0211-0222, Tables 4-5). Regarding instant claim 9, while Baum does not explicitly disclose a polynucleotide comprising a sequence that comprises a nucleotide sequence of at least two consecutive nucleotides from SEQ ID NOs: 28-33, a polynucleotide encoding the chimeric insecticidal protein of Baum et al, as disclosed in claims 4 and 5, for example, would inherently comprise such a nucleotide sequence. Regarding instant claims 21 and 22, Baum et al discloses a method of producing transgenic plants with increased lepidopteran resistance by transforming a plant cell with a polynucleotide encoding the chimeric insecticidal protein (Examples 5-6, paragraphs 0211-0222, Tables 4-5). Baum discloses that transgenic soybean plants comprising said insecticidal protein were allowed to self-pollinate and produce seed, which was harvested and sowed to produce transgenic soybean progeny comprising the insecticidal protein (Example 6, paragraphs 0220, Table 6). Regarding instant claims 20 and 25, Baum et al discloses an insect inhibitory composition comprising the chimeric insecticidal protein and discloses that said composition may comprise an agriculturally-acceptable carrier and can be applied to a plant or seed (claim 9; paragraphs 0185 and 0187). Thus, Baum et al anticipates all the limitations of instant claims 1, 8-9, 10-14, 17-22 and 25. Conclusion No claims are allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to ALEKSANDAR RADOSAVLJEVIC whose telephone number is (571)272-8330. The examiner can normally be reached Monday--Friday 8-5:30. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Bratislav Stankovic can be reached at 571-270-0305. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /ALEKSANDAR RADOSAVLJEVIC/ Examiner, Art Unit 1662 /BRENT T PAGE/ Primary Examiner, Art Unit 1663
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Prosecution Timeline

Feb 21, 2025
Application Filed
Oct 06, 2026
Non-Final Rejection mailed — §101, §102, §112 (current)

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2y 10m (~1y 2m remaining)
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