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
Applicant’s election without traverse of Group I, claims 1 and 4-14, in the reply filed on May 29th, 2026 is acknowledged.
Applicant’s election without traverse of the species of SEQ ID No: 1, as in claim
1(a), and at least about 90% identity as in claims 1(o) in the reply filed on May 29th, 2026 is also acknowledged.
Claims 2-3 and 15-21 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on May 29th, 2026.
Priority
The instant application claims priority to 371 National Stage Application PCT/NZ2020/050092, filed August 24th, 2020, under 35 U.S.C. 119(a)-(d), and claims benefit to provisional application NZ756630, filed August 23rd, 2019, under 35 U.S.C.119 (e). The priority date of August 23rd, 2019 is acknowledged.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on October 25th, 2023 and October 17th, 2024 are being considered by the examiner
The information disclosure statement filed October 17th, 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. NPL reference #24 cited in the IDS filed on October 17th, 2024 is not attached.
Also, the citation for attached reference-Engelhardt H. (2007). Are S-layers exoskeletons? The basic function of protein surface layers revisited. Journal of structural biology, 160(2), 115–124. https://doi.org/10.1016/j.jsb.2007.08.003 - was missing, and has been added by the examiner to the IDS filed October 17th, 2024.
Claims Status
The claims listing filed on May 29th, 2026 is pending. Claims 2-3 and 15-21 are withdrawn from further consideration for the reasons set forth in 37 CFR 1.142(b). Claims 1 and 4-14 are being examined on the merits in this office action.
Claim Objections
Claims 1 and 5 are objected to because of the following informalities: polypeptide b) has the same sequence as e) and h); polypeptide c) has the same sequence as f) and i); and polypeptide d) has the same sequence as g) and j). The claim limitations b)-j) are repetitive because the ranges of amino acids claimed comprise of the same sequence. The alignment of peptide b) and e) and b) and h) is below.
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964
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Figure 1: peptide b) and e) alignment
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984
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Figure 2: pepide b) and h) alignment
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, 4-5, 8, 13-14 are rejected under 35 U.S.C. 101 because the claimed composition is a product of nature without any markedly different characteristics from any naturally occurring counterparts:
Laws of nature and natural phenomena, as identified by the courts, include
naturally occurring principles/relations and nature-based products that are
naturally occurring or that do not have markedly different characteristics
compared to what occurs in nature. The courts have often described these
exceptions using other terms, including "physical phenomena," "scientific
principles", "natural laws," and "products of nature." [MPEP 2106.04(c)]
Regarding claim 1, claim 1 recites elected species SEQ ID NO: 1, as in claim
1(a), and at least about 90% identity as in claims 1(o), which is a product of nature. See analysis below.
Step 1: Does the claim fall into a statutory category of invention?
Yes, the claim is directed to a composition of matter, which falls into a category of invention.
Step 2A: Is the claim directed to a law of nature, a natural phenomenon (product of nature) or an abstract idea?
Yes, the claim is directed to a product of nature because the sequence can be derived from A0A518V3N2.
Instant SEQ ID NO: 1 shares a 91.6% query match with A0A518V3N2, the S-layer homology domain-containing protein of Bacillus laterosporus strain 1821L. This falls under the elected claim limitations.
The markedly different characteristic analysis is part of Step 2A: Prong One. The
markedly different characteristic analysis compares the nature-based product limitation
to its naturally occurring counterpart in its natural state, the first step in the analysis is
to select the appropriate counterpart(s) to the nature-based product.
Step 2A Prong One: Does the claim recite an abstract idea, law of nature, or
natural phenomenon?
In the present case, the answer is yes because when a nature-based product is derived from a naturally occurring thing, then the naturally occurring thing is the
counterpart. Section 2106.04 (b) recites:
When a law of nature or natural phenomenon is claimed as a physical product, the courts have often referred to the exception as a "product of nature". For example, the isolated DNA of Myriad and the primers of Ambry Genetics were described as products of nature by the courts. Ass’n for Molecular Pathology v. Myriad Genetics, Inc., 569 U.S. 576, 580, 106 USPQ2d 1972, 1975 (2013); University of Utah Research Foundation v. Ambry Genetics, 774 F.3d 755, 758-59, 113 USPQ2d 1241, 1243 (Fed. Cir. 2014). As explained in those decisions, products of nature are considered to be an exception because they tie up the use of naturally occurring things, but they have been labeled as both laws of nature and natural phenomena. See Myriad Genetics, Inc., 569 U.S. at 590- 91, 106 USPQ2d at 1979 (claims to isolated DNA held ineligible because they claim “naturally occurring phenomena" and are "squarely within the law of nature exception")
Step 2A Prong Two: Does the claim recite additional elements that integrate
the judicial exception into a practical application?
Because the markedly different characteristics analysis is based on comparing the
characteristics of the claimed nature-based product and its counterpart, the second step
in the analysis is used to identify appropriate characteristics to compare. Appropriate
characteristics must be possessed by the claimed product, because it is the claim that
must define the invention to be patented. In the present case, each component found in
nature is unmodified by a defining quantity as the natural product is indistinguishable from an isolated, purified, recombinant or synthetic polypeptide of 91.6% identity to SEQ ID NO: 1.
Regarding claim 4, a composition comprising a peptide with 90% identity to instant SEQ ID NO: 1 and a carrier is a natural product as the broadest reasonable interpretation of a carrier includes anything found in nature, such as water.
Regarding claim 5, a composition comprising a peptide with 90% identity to instant SEQ ID NO: 1, and about 1 % to about 80% w/w cellular extract obtained from B. laterosporus NMI No. V12/001945, or the composition grown in 1 to 80% B. laterosporus NMI No. V12/001 945 is a product of nature because the composition with 1 to 80% B. laterosporus NMI No. V12/001 945 does not possess markedly different characteristics [MPEP 2106.05]. Both components are found in nature and there is no evidence of record that the specific weight percentage combined with a peptide with 90% identity to instant SEQ ID NO: 1 change the functional characteristics otherwise present in both components.
Regarding claim 8, composition comprising a peptide with 90% identity to instant SEQ ID NO: 1, and about 1 % to about 80% w/w cellular extract obtained from B. laterosporus NMI No. V12/001946 or NMI No. V12/001944; or the composition grown in 1 to 80% B. laterosporus NMI No. V12/001 947 or NMI No. V12/001944 is a product of nature because the composition with 1 to 80% of B. laterosporus NMI No. V12/001944 or NMI No. V12/001946 does not possess markedly different characteristics [MPEP 2106.05]. Both components are found in nature and there is no evidence of record that the specific weight percentage combined with a peptide with 90% identity to instant SEQ ID NO: 1 change the functional characteristics otherwise present in both components.
Regarding claim 13, a composition comprising a peptide with 90% identity to instant SEQ ID NO: 1 and dillapiole is a natural product as dillapiole is found in nature. Dillapiole oil is also known as Anethum graveolens and is a natural insecticide (Joffe, T. et al. (2012). Investigating the potential of selected natural compounds to increase the potency of pyrethrum against houseflies Musca domestica. Pest management science, 68(2), 178–184) [Abstract Results line 3 and pg 2 pgh 7 line 10]. Each component is unmodified by a defining quantity, such as a weight percentage, and is therefore a product of nature.
Regarding claim 14, a composition comprising a peptide with 90% identity to instant SEQ ID NO: 1 and dillapiole is a natural product as dillapiole is found in nature. Dillapiole oil is also known as Anethum graveolens and is a natural insecticide (Joffe et al.) [Abstract Results line 3 and pg 2 pgh 7 line 10]. Each component is unmodified by a defining quantity, such as a weight percentage, and is therefore a product of nature.
Claims 6-7 and 9-10 are not rejected because the state of the art shows that sub-3 kDa fractions of B. laterosporus NMI No. V12/001945 contribute substantially more to a composition than B. laterosporus NMI No. V12/001945 would do otherwise (Ormskirk, M. Brevibacillus laterosporus as a potential bio-control agent of the diamondback moth and other insects. thesis submitted at Lincoln University, (2017)), evidenced by (Babar, T.K., Glare, T.R., Hampton, J.G. et al. Linocin M18 protein from the insect pathogenic bacterium Brevibacillus laterosporus isolates. Appl Microbiol Biotechnol 107, 4337–4353 (2023).
Ormskirk states that a high larvicidal activity was observed against DBM larvae in the culture supernatant of one particular culture of Brevibacillus laterosporus 1951 [pg 208 pgh 3 line 1]. This sample had a negligible amount of protein and still had 100% mortality 24 hours after incubation after being heated at 95°C for 30 minutes. The low protein content of this sample and the heat stability suggest that the insecticidal activity caused was most likely not of proteinaceous nature. Ormskirk states that scientists at DuPont Pioneer confirmed that the toxic substance was smaller than 3 kDa [pg 209 pgh 1 line 1]. Ormskirk does not evidence that BI 1951 is the same strain as instant NMI No. V12/0001945.
Baber et al. evidences that the strain BI 1951 researched by Ormskirk is the same as NMI No. V12/0001945 taught by Glare et al.
Therefore, a sub-3 kDa fraction of B. laterosporus strains has markedly different characteristics than natural products as it contributes high larvicidal activity to the compositions claimed.
Claims 11 and 12 are not rejected because water dispersible granules are formed by an unnatural process and define the structure of the composition. (Water Dispersible Granules. (2023). In Azelis. https://www.azelis.com/en/markets/specialty-agrihorti/products/crop-protection/water-dispersible-granules)
Water-dispersible granules (WG) are obtained by blending and agglomerating a ground solid active ingredient with surfactants and other formulation ingredients, using water (or water + surfactants) as the agglomerating agent. A drying step is necessary to reduce moisture to 1-2%. [Definitions and interest].
Therefore, a water dispersible granule has markedly different characteristics affecting the structure and the way the compositions functions.
Claim Rejections - 35 USC § 112
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.
Claims 1 and 4-14 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(s) 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. While the applicant does have support for isolated peptides derived from full-length S-layer proteins of B. laterosporus NMI V12/001945 (SEQ ID NO:1), B. laterosporus NMI V12/001944 (SEQ ID NO: 32) and B. laterosporus NMI V12/001944 (SEQ ID NO: 58), they do not have support for the polypeptides of claim 1 defined by 1 a)-q).
Claim 1 recites “polypeptide selected from the group comprising” a)-q). However, the specification does not support that the inventors possess the complete recited genus.
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the inventor was in possession of the claimed genus [MPEP 2163 ii)].
The inventors provide direction by disclosing the B. laterosporus strain, protein sequence and domain from which SEQ ID NOs: 1-87 are derived from [pg 20 line 25 to pg 25 line 2]. The inventors assessed from where the insecticidal activity occurred from B. laterosporus strain NMI No. V12/001945 and found that the main activity was located within the culture supernatant. [pg 48 line 13]. The compounds within the supernatant have some that are proteinaceous, as its activity is partly heat-sensitive [pg 53 line 21]. They identified the protein to be the surface layer protein using ESI-mass spectrometry [pg 63 top]. Then, they went one to perform alignments to shows that the S-layer protein is highly conserved within the BI species and Brevibacillus genus [pg 63 line 30]. The inventor states that the gene located upstream the S-layer protein encoding gene may be an adhesin-like protein that facilitates adherence to the insect host cells, and therefore could be an important virulence factor of BI45 [pg 69 line 1]. They compared sequence homology of the S-layer protein from BI45 to the structurally elucidated Paenibacillus chitinase and C. thermocellum cellobiohydrolase [pg 75 line 27]. From this, they tested the insecticidal activity of B. laterosporus NMI No. V12/001946 and NMI No. V12/001944 and isolated its S-layer proteins [pg 79-80 and Fig 21-22].
However, the full-length S-layer proteins reduced to practice by the applicant are not representative of the entire genus of polypeptides claimed. Nor, would one of ordinary skill in the art be able to attest that the applicant possessed the complete genus. For example, the broadest reasonable interpretation of the claim encompasses a peptide comprising any 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to show the complete genus.
Also, the applicant uses the S-layer protein gene identified to analyze adjacent genes on Contig 54, leading to the identification of the adhesin-like encoding gene and efflux pump encoding gene [pg 66 line 12]. Yet, the inventors merely show the isolation of the full-length S-layer proteins of B. laterosporus NMI V12/001945 (SEQ ID NO:1), B. laterosporus NMI V12/001944 (SEQ ID NO: 32) and B. laterosporus NMI V12/001944 (SEQ ID NO: 58). While this, along with the contemplated functional domains are representative of the sequences derived from domains of the S-layer protein (SEQ ID NO: 1-7, 32-37, and 58-63 and peptides b)-j) [pg 20-pg 24], there is not adequate support for the possession of isolated peptides derived from the full-length adhesion fimbriae protein and efflux pump protein as the applicant does not describe the process by which the peptides are isolated and only its discovery and potential relevance on the gene. Thus, while the applicant has support for the specific sequences reduced to practice, peptides derived from the domains of full-length S-layer proteins, they do not have support for the complete genus of isolated polypeptides of claim 1 selected from a) to q).
Regarding claim 4, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 1, selected from a)-q).
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 5, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides, selected from a)-p).
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 6, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 4 selected from a)-q), and a sub-3 kDa fraction from B. laterosporus NMI No. V12/001945.
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 7, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 5 selected from a)-p), and a sub-3 kDa non-proteinaceous fraction from B. laterosporus NMI No. V12/001945.
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 8, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 4 selected from a)-q), and cellular extract from either B. laterosporus NMI No. V12/001946 or B. laterosporus NMI No. V12/001944.
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 9, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 4 selected from a)-q), and sub 3-kDa fraction from either B. laterosporus NMI No. V12/001946 or B. laterosporus NMI No. V12/001944.
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 10, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 4 selected from a)-q), and a non-proteinaceous sub-3-kDa fraction from either B. laterosporus NMI No. V12/001946 or B. laterosporus NMI No. V12/001944.
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 11, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 4 selected from a)-q).
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 12, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 1 selected from a)-q).
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 13, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 1 selected from a)-q).
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
Regarding claim 14, the specification does not support that the inventors, at the time of filing, possessed the complete recited genus of a composition comprising of one or more polypeptides of claim 1 selected from a)-q).
There is substantial variation within the genus because the broadest reasonable interpretation comprises of a polypeptide comprising at least 10 contiguous amino acids with 90% amino acid identity to SEQ ID NO: 1-87. Full-length S-layer proteins of SEQ ID NO: 1, 32, and 58 are not a representative number of species to represent the complete claimed genus. Thus, while the specification supports possession of peptides derived from the domains of the isolated full-length S-layer protein, there is not adequate support for the scope of the claim encompassed by the broadest reasonable interpretation.
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 and 4-14 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.
Claims 1 and 5 recite the term “isolated.” It is unclear if the use of this term is used to limit the amino acid length to consist of polypeptides a)-q) or if it used to describe that the polypeptides comprising of a)-q) are separated from its source. In either scenario, the term renders the claim indefinite. In the former scenario, the claim is indefinite because the polypeptide can comprise or consist of polypeptides a) to q). The latter scenario is indefinite because the dependent claims of claim 1 and 5 place the peptides in a composition comprising of cellular extracts of B. laterosporus. The polypeptide(s) are no longer than “isolated” from other bacterial material.
Dependent claims 4 and 6-14 are rejected as the fail to overcome the indefiniteness caused by base claims 1 and 5.
Claims 1 and 5 are also indefinite because the state the “polypeptide selected from the group comprising.” The word “comprising” is open-ended language, thus making the scope of the group from which the polypeptides are selected from indefinite.
A Markush grouping is a closed group of alternatives, i.e., the selection is made from a group "consisting of" (rather than "comprising" or "including") the alternative members. Abbott Labs., 334 F.3d at 1280, 67 USPQ2d at 1196. If a Markush grouping requires a material selected from an open list of alternatives (e.g., selected from the group "comprising" or "consisting essentially of" the recited alternatives), the claim should generally be rejected under 35 U.S.C. 112(b) as indefinite because it is unclear what other alternatives are intended to be encompassed by the claim. See In re Kiely, 2022 USPQ2d 532 at 2* (Fed. Cir. 2022) [MPEP 2173.05 (h)].
This may be corrected by replacing the word “comprising” with “consisting.”
Dependent claims 4 and 6-14 do not overcome the indefinite language of base claims 1 and 5 and are therefore, also rejected.
The term “about” in claims 1 and 5 is a relative term which renders the claim indefinite. The term “about” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention.
In determining the range encompassed by the term "about," one must consider the context of the term as it is used in the specification and claims of the application [MPEP 2173.05(b)].
The term about is used to describe the amino acid identity of polypeptides a) to n). This term renders the claims indefinite as there is nothing in the specification, prosecution history, or the prior art to provide any indication as to what range of specific activity is covered by the term "about."
Dependent claims 4 and 6-14 are rejected as the fail to overcome the indefiniteness caused by base claims 1 and 5.
The term “about” in claims 5, 8, and 12 is a relative term which renders the claim indefinite. The term “about” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention.
In determining the range encompassed by the term "about," one must consider the context of the term as it is used in the specification and claims of the application [MPEP 2173.05(b)].
The term about is used to describe the weight percentage of cellular extract and compositions of strains of B. laterosporus and amount ingredients in a water dispersible granule. This term renders the claims indefinite as there is nothing in the specification, prosecution history, or the prior art to provide any indication as to what range of specific activity is covered by the term "about."
Dependent claim 7 is rejected as the fail to overcome the indefiniteness caused by base claim 5.
Claims 6-7 and 9 recite the phrase “or a culture thereof.” It is unclear which other culture the claim language is referring to and what scope the recited claim limitation embodies. Thus, the claims are indefinite.
The term “substantially” in claims 7 and 10 is a relative term which renders the claim indefinite. The term “substantially” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention.
The use of relative terminology in claim language, including terms of degree, does not automatically render the claim indefinite under 35 U.S.C. 112(b) or pre-AIA 35 U.S.C. 112, second paragraph. Seattle Box Co., Inc. v. Industrial Crating & Packing, Inc., 731 F.2d 818, 221 USPQ 568 (Fed. Cir. 1984). Acceptability of the claim language depends on whether one of ordinary skill in the art would understand what is claimed, in light of the specification. Clearone, Inc. v. Shure Acquisition Holdings, Inc., 35 F.4th 1345, 1349, 2022 USPQ2d 509 (Fed. Cir. 2022) ("Based on the intrinsic record alone, we conclude that the written description provides, with reasonable certainty, the scope of the term self-similar [MPEP 2173.05(b)].
The use of the term “substantially” is indefinite because one of ordinary skill in the art would not be able to understand by what degree the sub-3 kDa fractions are non-proteinaceous.
Claim 10 recites the limitation "one or more of the sub-3 kDa fractions" as “claimed in claim 4”. However, there is no sub-3 kDa fractions in base claim 4. There is insufficient antecedent basis for this limitation in the claim. Therefore, claim 10 is indefinite.
Claim Rejections - 35 USC § 103
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 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
In reply filed May 29th, 2026, the species of SEQ ID No: 1, as in claim 1(a), and at least about 90% identity as in claims 1(o) was elected. The following rejection is based on the election.
Claims 1 and 4 are rejected under 35 U.S.C. 103 as being unpatentable over Ormskirk et al (Ormskirk, M. Brevibacillus laterosporus as a potential bio-control agent of the diamondback moth and other insects. thesis submitted at Lincoln University, (2017)), as evidenced by UniProt Accession Number A0A518V3N2.
Ormskirk isolated two New Zealand strains of Brevibacillus laterosporus (Bl), 1821 and 1951, from brassica seeds that displayed high activity toward larvae of the diamondback moth (DBM) [pg 5 pgh 1 line 1]. Brevibacillus laterosporus 1821 produced crystalline parasporal bodies in the sporangia, and these were hypothesized to contain the DBM toxins [pg 5 pgh 2 line 3]. However, no DBM activity was displayed by the vegetative cells and spores of Bl 1821 and 1951, or in the case of Bl 1821, in the parasporal crystalline bodies [pg 5 pgh 5 line 1]. The main DBM activity of Bl 1951 was located in the culture supernatant (CSN) and a surface layer (S-layer) protein, derived from the CSN, was identified as a putative DBM toxin [pg 5 pgh 5 line 5]. Ormskirk et al. states that the same S-layer gene was identified in Bl 1821 and may be responsible for the DBM toxicity displayed [pg 6 pgh 2 line 11]. The S-layer protein may represent a novel class of toxins that can be exploited for DBM control. Ormskirk does not evidence that the S-layer protein of BI 1821 has at least 90% amino acid identity to instant SEQ ID NO: 1.
In certain circumstances, references cited to show a universal fact need not be available as prior art before the effective filing date of applicant’s claimed invention. In re Wilson, 311 F.2d 266, 135 USPQ 442 (CCPA 1962). Such facts include the characteristics and properties of a material or a scientific truism [MPEP 2124].
A0A518V3N2 evidences the sequence of the S-layer homology domain-containing protein of Brevibacillus laterosporus 1821L. The sequence of the S-layer homology domain-containing protein of BI 1821 is evidentiary and not prior art as it is a universal fact that the sequence of A0A518V3N2 was so prior to the effective filing date. SEQ ID NO:1 shares 91.6% identity with the S-layer protein of BI 1821.
Therefore, it was obvious prior to the effective filing date to isolate a sequence with at least 90% identity to instant SEQ ID NO: 1, such as A0A518V3N2 because Ormskirk motivates one of ordinary skill in the art to isolate the S-layer protein of B. laterosporus 1821 to use as a toxin for the diamondback moth as the S-layer protein of BI 1951 demonstrates DBM activity and BI 1821 shares the same S-layer gene. One of ordinary skill in the art would have had a high expectation of the S-layer protein of BI 1821L, A0A518V3N2, being successful at DBM toxicity.
Regarding claim 4, LCMS performed by Ormskirk for the identification of the S-layer protein was done with a gradient elution performed from 2% solvent A (0.1% formic acid) to 45% B (98% acetonitrile, 0.1% formic acid) [pg 135 pgh 1]. By the broadest reasonable interpretation, the solvent in which the S-layer protein fractions eluted in is a carrier. Therefore, prior to the effective filing date, it would have been obvious to one of ordinary skill in the art to make a composition of a sequence with 90% identity to the instant SEQ ID NO: 1 and a carrier.
Claims 5-10 are rejected under 35 U.S.C. 103 as being unpatentable over Ormskirk and A0A518V3N2 as applied to claims 1 and 4 above, and further in view of Glare et al. (US10004236B2; published 2018), as evidenced by Babar et al. (Babar, T.K., Glare, T.R., Hampton, J.G. et al. Linocin M18 protein from the insect pathogenic bacterium Brevibacillus laterosporus isolates. Appl Microbiol Biotechnol 107, 4337–4353 (2023).
Ormskirk, as evidenced by A0A518V3N2, teaches a composition with a sequence with 90% identity to the instant SEQ ID NO: 1. Ormskirk does not teach that the composition comprises of about 1% to about 80% of B. laterosporus NMI No. V12/001945.
Glare et al. claims a method comprising contacting at least one pest with a composition comprising at least one strain of Brevibacillus laterosporus and an agriculturally acceptable carrier, wherein the strain is selected from Brevibacillus laterosporus strain NMI No. V12/001946, Brevibacillus laterosporus strain NMI No. V12/001945, and Brevibacillus laterosporus strain V12/001944 [claim 1]. The at least one pest may be a diamondback moth [claims 2-4 and 6]. Glare et al. specifies that when formulated for application, the composition of the invention will typically be present in the formulation at a concentration of from 1 to 99% by weight, 5 to 95%, 10 to 90%, 15 to 85%, 20 to 80%, 30 to 70%, or 40 to 60% by weight [Col 9 line 51]. Glare’s concentration encompasses the instant range of about 1% to about 80% w/w.
Therefore, prior to the effective filing date, it would have been obvious to one of ordinary skill in the art to combine Glare’s composition with the S-layer protein of Bl 1821 as taught by Ormskirk as each element merely performs the same function of controlling diamondback moths as it does separately [MPEP 2143(I)(A)].
Regarding claim 6, Glare et al. state that the “B. laterosporus cells may also be processed prior to use to produce active cell extracts, cell suspensions, cell homogenates, cell lysates, cell supernatants, cell filtrates, cell pellets or may be used as whole cell preparations” [Col 8 line 3]. Glare et al. does not state specifically using a sub- 3 kDa cell filtrate and the motivation to do so.
Ormskirk states that a high larvicidal activity was observed against DBM larvae in the culture supernatant of one particular culture of Brevibacillus laterosporus 1951 [pg 208 pgh 3 line 1]. This sample had a negligible amount of protein and still had 100% mortality 24 hours after incubation after being heated at 95°C for 30 minutes. The low protein content of this sample and the heat stability suggest that the insecticidal activity caused was most likely not of proteinaceous nature. Ormskirk states that scientists at DuPont Pioneer confirmed that the toxic substance was smaller than 3 kDa [pg 209 pgh 1 line 1]. Ormskirk does not evidence that BI 1951 is the same strain as instant NMI No. V12/0001945.
Baber et al. evidences that the strain BI 1951 researched by Ormskirk is the same as NMI No. V12/0001945 taught by Glare et al.
Therefore, prior to the effective filing date, it would have been obvious to one of ordinary skill in the art to use a sub-3 kDa fraction of B. laterosporus NMI No. V12/0001945 in combination with the S-layer protein of Bl 1821 as taught by Ormskirk as the sub-3 kDa fraction contains contents toxic to diamondback larvae and the S-layer protein is toxic to diamondback moths. There is a reasonable expectation that the combined teachings would be successful as each element merely performs the same function of controlling diamondback moths as it does separately.
Regarding claim 7, Glare et al. state that the “B. laterosporus cells may also be processed prior to use to produce active cell extracts, cell suspensions, cell homogenates, cell lysates, cell supernatants, cell filtrates, cell pellets or may be used as whole cell preparations” [Col 8 line 3]. Glare et al. does not state specifically using a sub- 3 kDa cell filtrate and the motivation to do so.
Ormskirk states that a high larvicidal activity was observed against DBM larvae in the culture supernatant of one particular culture of Brevibacillus laterosporus 1951 [pg 208 pgh 3 line 1]. This sample had a negligible amount of protein and still had 100% mortality 24 hours after incubation after being heated at 95°C for 30 minutes. The low protein content of this sample and the heat stability suggest that the insecticidal activity caused was most likely not of proteinaceous nature. Ormskirk states that scientists at DuPont Pioneer confirmed that the toxic substance was smaller than 3kDa [pg 209 pgh 1 line 1]. Ormskirk does not evidence that BI 1951 is the same strain as instant NMI No. V12/0001945.
Baber et al. evidences that the strain BI 1951 researched by Ormskirk is the same as NMI No. V12/0001945 taught by Glare et al.
Therefore, prior to the effective filing date, it would have been obvious to one of ordinary skill in the art to use a non-proteinaceous sub-3 kDa fraction of B. laterosporus NMI No. V12/0001945 in combination with the S-layer protein of Bl 1821 as taught by Ormskirk as the sub-3 kDa fraction contains non-proteinaceous contents toxic to diamondback larvae and the S-layer protein is toxic to diamondback moths. There is a reasonable expectation that the combined teachings would be successful as each element merely performs the same function of controlling diamondback moths as it does separately.
Regarding claim 8, Glare et al. claims a method comprising contacting at least one pest with a composition comprising at least one strain of Brevibacillus laterosporus and an agriculturally acceptable carrier, wherein the strain is selected from Brevibacillus laterosporus strain NMI No. V12/001946, Brevibacillus laterosporus strain NMI No. V12/001945, and Brevibacillus laterosporus strain V12/001944 [claim 1]. The at least one pest may be a diamondback moth [claims 2-4 and 6]. Glare et al. specifies that when formulated for application the composition of the invention will typically be present in the formulation at a concentration of from 1 to 99% by weight, 5 to 95%, 10 to 90%, 15 to 85%, 20 to 80%, 30 to 70%, or 40 to 60% by weight [Col 9 line 51]. Glare’s concentration encompasses the instant range of about 1% to about 80% w/w.
Therefore, prior to the effective filing date, it would have been obvious to one of ordinary skill in the art to combine Glare’s composition with the S-layer protein of Bl 1821 as taught by Ormskirk as each element merely performs the same function of controlling diamondback moths as it does separately.
Regarding claim 9, Glare et al. state that the “B. laterosporus cells may also be processed prior to use to produce active cell extracts, cell suspensions, cell homogenates, cell lysates, cell supernatants, cell filtrates, cell pellets or may be used as whole cell preparations” [Col 8 line 3]. Glare et al. does not state specifically using a sub- 3 kDa cell filtrate and the motivation to do so.
Ormskirk states that a high larvicidal activity was observed against DBM larvae in the culture supernatant of one particular culture of Brevibacillus laterosporus 1951 [pg 208 pgh 3 line 1]. This sample had a negligible amount of protein and still had 100% mortality 24 hours after incubation after being heated at 95°C for 30 minutes. The low protein content of this sample and the heat stability suggest that the insecticidal activity caused was most likely not of proteinaceous nature. Ormskirk states that scientists at DuPont Pioneer confirmed that the toxic substance was smaller than 3 kDa [pg 209 pgh 1 line 1]. Ormskirk does not evidence that BI 1951 is the same strain as instant NMI No. V12/0001945 and BI 1821 is the same as NMI No. V12/0001946.
Baber et al. evidences that the strain BI 1951 researched by Ormskirk is the same as NMI No. V12/0001945 taught by Glare et al. and BI 1821L is the same as NMI No. V12/0001946.
Therefore, prior to the effective filing date, it would have been obvious to one of ordinary skill in the art to use a sub-3 kDa fraction of B. laterosporus NMI No. V12/0001946 in combination with the S-layer protein of Bl 1821 as taught by Ormskirk as the sub-3 kDa fraction of B. laterosporus NMI No. V12/0001945 contains contents toxic to diamondback larvae and therefore, there is a reasonable expectation that the B. laterosporus NMI No. V12/0001946, also researched by Ormskirk (BI 1821) will also be successfully toxic. The combined composition of the S-layer protein and sub-3 kDa fraction of B. laterosporus NMI No. V12/0001946 would merely perform the same function of controlling diamondback moths as each element does separately.
Regarding claim 10, Glare et al. state that the “B. laterosporus cells may also be processed prior to use to produce active cell extracts, cell suspensions, cell homogenates, cell lysates, cell supernatants, cell filtrates, cell pellets or may be used as whole cell preparations” [Col 8 line 3]. Glare et al. does not state specifically using a sub- 3 kDa cell filtrate and the motivation to do so.
Ormskirk states that a high larvicidal activity was observed against DBM larvae in the culture supernatant of one particular culture of Brevibacillus laterosporus 1951 [pg 208 pgh 3 line 1]. This sample had a negligible amount of protein and still had 100% mortality 24 hours after incubation after being heated at 95°C for 30 minutes. The low protein content of this sample and the heat stability suggest that the insecticidal activity caused was most likely not of proteinaceous nature. Ormskirk states that scientists at DuPont Pioneer confirmed that the toxic substance was smaller than 3kDa [pg 209 pgh 1 line 1]. Ormskirk does not evidence that BI 1951 is the same strain as instant NMI No. V12/0001945 and BI 1821 is the same as NMI No. V12/0001946.
Baber et al. evidences that the strain BI 1951 researched by Ormskirk is the same as NMI No. V12/0001945 taught by Glare et al and BI 1821L is the same as NMI No. V12/0001946.
Therefore, prior to the effective filing date, it would have been obvious to one of ordinary skill in the art to use a non-proteinaceous sub-3 kDa fraction of B. laterosporus NMI No. V12/0001946 in combination with the S-layer protein of Bl 1821 as taught by Ormskirk as the non-proteinaceous sub-3 kDa fraction of B. laterosporus NMI No. V12/0001945 contains contents toxic to diamondback larvae and therefore, there is a reasonable expectation that the B. laterosporus NMI No. V12/0001946, also researched by Ormskirk (BI 1821) will also be successfully toxic. The combined composition of the S-layer protein and sub-3 kDa fraction of B. laterosporus NMI No. V12/0001946 would merely perform the same function of controlling diamondback moths as each element does separately.
Claim 11 is rejected under 35 U.S.C. 103 as being unpatentable over Ormskirk and A0A518V3N2 as applied to claims 1 and 4 above, and further in view of Yanagisawa et al. (Yanagisawa, K., Muroi, T., Ohtsubo, T., & Watano, S. (2017). Effect of binder composition on physicochemical properties of water dispersible granules obtained through direct granulation of agrochemical suspension using fluidized bed. Journal of pesticide science, 42(3), 112–115).
Ormskirk, as evidenced by A0A518V3N2, teaches a composition with a sequence with 90% identity to the instant SEQ ID NO: 1 in an elution buffer (carrier). Ormskirk does not teach that the composition formulated as a water dispersible granule.
Yanagisawa et al. state that the demand for water dispersible granules (WDGs) in the pesticide market has been increasing since the 1980s, mainly due to their good flowability and low risk of dust inhalation when used as compared to the conventional wettable powder (WP) formulation [pg 112 line 1].
Therefore, it was obvious prior to the effective filing date to isolate a sequence with at least 90% identity to instant SEQ ID NO: 1, such as A0A518V3N2, and formulate it as a water dispersible granule because Ormskirk teaches that the S-layer protein of B. laterosporus 1821 can be used as a toxin for the diamondback moth and Yanagisawa teaches that water dispersible granules allow for good flowability and lower risk of dust inhalation.
Claim 12 is rejected under 35 U.S.C. 103 as being unpatentable over Ormskirk and A0A518V3N2 as applied to claims 1 and 4 above, and further in view of Glare et al. (US10004236B2; published 2018), and Yanagisawa et al. (Yanagisawa, K., Muroi, T., Ohtsubo, T., & Watano, S. (2017). Effect of binder composition on physicochemical properties of water dispersible granules obtained through direct granulation of agrochemical suspension using fluidized bed. Journal of pesticide science, 42(3), 112–115).
Ormskirk, as evidenced by A0A518V3N2, teaches a composition with a sequence with 90% identity to the instant SEQ ID NO: 1. Ormskirk does not teach that the composition comprises of about 1% to about 80% of B. laterosporus NMI No. V12/001945.
Glare et al. claims a method comprising contacting at least one pest with a composition comprising at least one strain of Brevibacillus laterosporus and an agriculturally acceptable carrier, wherein the strain is selected from Brevibacillus laterosporus strain NMI No. V12/001946, Brevibacillus laterosporus strain NMI No. V12/001945, and Brevibacillus laterosporus strain V12/001944 [claim 1]. The at least one pest may be a diamondback moth [claims 2-4 and 6]. Glare et al. specifies that when formulated for application the composition of the invention will typically be present in the formulation at a concentration of from 1 to 99% by weight, 5 to 95%, 10 to 90%, 15 to 85%, 20 to 80%, 30 to 70%, or 40 to 60% by weight [Col 9 line 51]. Glare’s concentration encompasses the instant range of about 2% to about 80% w/w. Glare et al. also specifies that the composition may be formulated as dusts, granules, seed coatings, wettable powders, or the like. However, Glare et al. does not specifically state that the composition may be formulated as a water dispersible granule and the motivation to do so.
Yanagisawa et al. state that the demand for water dispersible granules (WDGs) in the pesticide market has been increasing since the 1980s, mainly due to their good flowability and low risk of dust inhalation when used as compared to the conventional wettable powder (WP) formulation [pg 112 line 1].
Therefore, prior to the effective filing date, it would have been obvious to one of ordinary skill in the art to combine Glare’s composition with the S-layer protein of Bl 1821 as taught by Ormskirk as each element merely performs the same function of controlling diamondback moths as it does separately and formulate as a water dispersible granule for good flowability and lower risk of dust inhalation.
Claims 13 and 14 are rejected under 35 U.S.C. 103 as being unpatentable over Ormskirk and A0A518V3N2 as applied to claims 1 and 4 above, and further in view of Joffe et al. (Joffe, T., Gunning, R. V., Allen, G. R., Kristensen, M., Alptekin, S., Field, L. M., & Moores, G. D. (2012). Investigating the potential of selected natural compounds to increase the potency of pyrethrum against houseflies Musca domestica (Diptera: Muscidae). Pest management science, 68(2), 178–184.)
Ormskirk, as evidenced by A0A518V3N2, teaches a composition with a sequence with 90% identity to the instant SEQ ID NO: 1 in an elution buffer (carrier). Ormskirk does not teach a composition comprising one or more of piperonyl butoxide, safrole, apiole, parsley oil, and dillapiole.
Joffe et al. undertake a study to determine the efficacy of seven natural compounds compared with piperonylbutoxide (PBO) in synergizing pyrethrum [Abstract Background line 1]. They found that the most effective natural synergists against house flies were dillapiole oil, grapefruit oil and parsley seed oil, with 59, 50 and 41% mortality respectively, compared with 18% mortality with synergized pyrethrum.
Therefore, prior to the effective filing date, it would have been obvious to combine the S-layer protein taught by Ormskirk with at least 90% identity to instant SEQ ID NO: 1 with a natural insecticide such as dillapiole for the most reasonable success at insect mortality.
Regarding claim 14, Joffe et al. undertake a study to determine the efficacy of seven natural compounds compared with piperonylbutoxide (PBO) in synergizing pyrethrum [Abstract Background line 1]. They found that the most effective natural synergists against house flies were dillapiole oil, grapefruit oil and parsley seed oil, with 59, 50 and 41% mortality respectively, compared with 18% mortality with synergized pyrethrum.
Therefore, prior to the effective filing date, it would have been obvious to combine the S-layer protein taught by Ormskirk with at least 90% identity to instant SEQ ID NO: 1 with a natural insecticide such as dillapiole that acts synergistically for the most reasonable success at insect mortality.
Conclusion
Claims 1 and 5 are objected to. Claims 1, 4-5, 8 and 13-14 are rejected under 35 U.S.C. 101. Claims 1 and 4-14 are rejected under 35 U.S.C. 112(a). Claims 1 and 4-14 are rejected under 35 U.S.C. 112(b). Claims 1 and 4-14 are rejected under 35 U.S.C. 103.
Correspondence
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/SACHI JAUHARI/Examiner, Art Unit 1654
/LIANKO G GARYU/Supervisory Patent Examiner, Art Unit 1654
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