DETAILED ACTION
Claims 1 and 3-20 are pending.
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
The objection to claim 1 is withdrawn in light of Applicant’s amendment to the claim.
The rejection of claims 1-20 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the subject matter that the inventor or a joint inventor, or for pre-AIA the applicant, regards as the invention is withdrawn in light of Applicant’s amendment to the claims.
The rejection of claim 19 under 35 U.S.C. 112(d) or 35 U.S.C. 112(pre-AIA ), fourth paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends is withdrawn in light of Applicant’s amendment to the claim.
Claim Rejections - 35 USC § 103
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.
Claims 1, 3-4, 6-16 and 18-20 are rejected under 35 U.S.C. 103(a) as being unpatentable over Bing et al (2008, US 7,323,556) in view of Lukoyanova et al (2015, PLoS Biol 13(2): e1002049. doi: 10.137 1/journal.pbio. 1002049), Sakurai et al A (2008, GenBank BAD66666), Sakurai et al B (2008, GenBank BAD66669), and Centre for Advanced Molecular Imaging (2015, https://imagingcoe.org/carnivorous-mushrooms-reveal-human-immune-trick/).
The rejection is repeated for the reasons of record as set forth in the Office action mailed 17 March 2026, as applied to claims 1-4, 6-16 and 18-20. Applicant’s arguments filed 17 June 2026 have been fully considered but they are not persuasive.
The claims are drawn to a method comprising expressing a pleurotolysin A, including one with 95% identity to SEQ ID NO:2, and a pleurotolysin B, including one with 95%-100% identity to SEQ ID NO:4, in a plant, including maize.
Bing et al teach transformation of maize with a construct encoding both subunits of the Cry34/35Ab1 binary toxin to produce western corn rootworm resistance plants (example 1). Bing et al do not teach transforming maize with a construct encoding pleurotolysin A and pleurotolysin B.
Lukoyanova et al teach pleurotolysin subunits pleurotolysin A (PlyA) and pleurotolysin B (PlyB), where PlyB is the MACPF subunit (pg 3, (4) which act together to form a lytic pore (Figure 6). PlyA and PlyB have 98.7% and 100% identity to SEQ ID NO:2 and 4, respectively:
Q8X1M9_PLEOS
ID Q8X1M9_PLEOS Unreviewed; 138 AA.
AC Q8X1M9;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE SubName: Full=Pleurotolysin A {ECO:0000313|EMBL:BAD66666.1};
DE SubName: Full=PriA {ECO:0000313|EMBL:AAL57035.1};
GN Name=PlyA {ECO:0000313|EMBL:BAD66668.1};
GN Synonyms=plyA {ECO:0000313|EMBL:BAD66666.1};
OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5322 {ECO:0000313|EMBL:AAL57035.1};
RN [1] {ECO:0000313|EMBL:AAL57035.1}
RP NUCLEOTIDE SEQUENCE.
RA Ma A.M., Kwan H.S.H.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAD66666.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15245918;
RA Sakurai N., Kaneko J., Kamio Y., Tomita T.;
RT "Cloning, expression, and pore-forming properties of mature and precursor
RT forms of pleurotolysin, a sphingomyelin-specific two-component cytolysin
RT from the edible mushroom Pleurotus ostreatus.";
RL Biochim. Biophys. Acta 1679:65-73(2004).
RN [3] {ECO:0007829|PDB:4OEB, ECO:0007829|PDB:4V2T}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=25654333; DOI=10.1371/JOURNAL.PBIO.1002049;
RA Lukoyanova N., Kondos S.C., Farabella I., Law R.H., Reboul C.F.,
RA Caradoc-Davies T.T., Spicer B.A., Kleifeld O., Traore D.A., Ekkel S.M.,
RA Voskoboinik I., Trapani J.A., Hatfaludi T., Oliver K., Hotze E.M.,
RA Tweten R.K., Whisstock J.C., Topf M., Saibil H.R., Dunstone M.A.;
RT "Conformational changes during pore formation by the perforin-related
RT protein pleurotolysin.";
RL PLoS Biol. 13:e1002049-e1002049(2015).
CC -!- SIMILARITY: Belongs to the aegerolysin family.
CC {ECO:0000256|ARBA:ARBA00010795}.
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DR EMBL; AF331453; AAL57035.1; -; mRNA.
DR EMBL; AB177869; BAD66666.1; -; mRNA.
DR EMBL; AB177871; BAD66668.1; -; Genomic_DNA.
DR PDB; 4OEB; X-ray; 1.85 A; A/B/C/D=1-138.
DR PDB; 4V2T; EM; 11.00 A; 0/2/3/5/6/8/9/B/C/E/F/H/I/K/L/N/O/Q/R/T/U/W/X/Z/b/c=2-136.
DR PDB; 4V3A; EM; 15.00 A; A/B=2-136.
DR PDB; 4V3M; EM; 17.00 A; A/B=2-136.
DR PDB; 4V3N; EM; 14.00 A; A/B=2-136.
DR PDBsum; 4OEB; -.
DR PDBsum; 4V2T; -.
DR PDBsum; 4V3A; -.
DR PDBsum; 4V3M; -.
DR PDBsum; 4V3N; -.
DR TCDB; 1.C.97.1.1; the pleurotolysin pore-forming (pleurotolysin) family.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1090164; -.
DR GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:InterPro.
DR InterPro; IPR009413; Aegerolysin-typ.
DR Pfam; PF06355; Aegerolysin; 1.
DR PIRSF; PIRSF007951; PIRSF007951; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4OEB, ECO:0007829|PDB:4V2T}.
SQ SEQUENCE 138 AA; 15136 MW; D8925B0E6AE1968C CRC64;
Query Match 98.7%; Score 739; DB 12; Length 138;
Best Local Similarity 98.6%;
Matches 136; Conservative 0; Mismatches 2; Indels 0; Gaps 0;
Qy 1 MAYAQWVIIIIHNVGSKDVKIVNLKPSWGKLHADGDKDTEVSASKYEGTVIKPDEKLQIN 60
||||||||||||||||||||| ||||||||||||||||||||||||||||||||||||||
Db 1 MAYAQWVIIIIHNVGSKDVKIKNLKPSWGKLHADGDKDTEVSASKYEGTVIKPDEKLQIN 60
Qy 61 ACGRSDAAEGTTGTFDLVDPADGDKQVRHFYWDCPWGSKANTWTVSGSNTKWMIEYSGQN 120
||||||||||||||||||||||||||||||||||||||| ||||||||||||||||||||
Db 61 ACGRSDAAEGTTGTFDLVDPADGDKQVRHFYWDCPWGSKTNTWTVSGSNTKWMIEYSGQN 120
Qy 121 LDSGALGTITVDTLKKGN 138
||||||||||||||||||
Db 121 LDSGALGTITVDTLKKGN 138
Q5W9E8_PLEOS
ID Q5W9E8_PLEOS Unreviewed; 523 AA.
AC Q5W9E8;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 19-JAN-2022, entry version 46.
DE SubName: Full=Pleurotolysin B {ECO:0000313|EMBL:BAD66667.1};
DE SubName: Full=Precursor of pleurotolysin B {ECO:0000313|EMBL:BAD66669.1};
GN Name=plyB {ECO:0000313|EMBL:BAD66669.1};
OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5322 {ECO:0000313|EMBL:BAD66669.1};
RN [1] {ECO:0000313|EMBL:BAD66669.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15245918;
RA Sakurai N., Kaneko J., Kamio Y., Tomita T.;
RT "Cloning, expression, and pore-forming properties of mature and precursor
RT forms of pleurotolysin, a sphingomyelin-specific two-component cytolysin
RT from the edible mushroom Pleurotus ostreatus.";
RL Biochim. Biophys. Acta 1679:65-73(2004).
RN [2] {ECO:0007829|PDB:4OEJ, ECO:0007829|PDB:4OV8}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 49-523.
RX PubMed=25654333; DOI=10.1371/JOURNAL.PBIO.1002049;
RA Lukoyanova N., Kondos S.C., Farabella I., Law R.H., Reboul C.F.,
RA Caradoc-Davies T.T., Spicer B.A., Kleifeld O., Traore D.A., Ekkel S.M.,
RA Voskoboinik I., Trapani J.A., Hatfaludi T., Oliver K., Hotze E.M.,
RA Tweten R.K., Whisstock J.C., Topf M., Saibil H.R., Dunstone M.A.;
RT "Conformational changes during pore formation by the perforin-related
RT protein pleurotolysin.";
RL PLoS Biol. 13:e1002049-e1002049(2015).
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CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB177870; BAD66667.1; -; mRNA.
DR EMBL; AB177872; BAD66669.1; -; Genomic_DNA.
DR PDB; 4OEJ; X-ray; 2.20 A; A=1-523.
DR PDB; 4OV8; X-ray; 2.15 A; A=49-523.
DR PDB; 4V2T; EM; 11.00 A; 1/4/7/A/D/G/J/M/P/S/V/Y/a=50-523.
DR PDB; 4V3A; EM; 15.00 A; C=49-523.
DR PDB; 4V3M; EM; 17.00 A; C=1-523.
DR PDB; 4V3N; EM; 14.00 A; C=49-523.
DR PDBsum; 4OEJ; -.
DR PDBsum; 4OV8; -.
DR PDBsum; 4V2T; -.
DR PDBsum; 4V3A; -.
DR PDBsum; 4V3M; -.
DR PDBsum; 4V3N; -.
DR SMR; Q5W9E8; -.
DR TCDB; 1.C.97.1.1; the pleurotolysin pore-forming (pleurotolysin) family.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1090161; -.
DR InterPro; IPR020864; MACPF.
DR InterPro; IPR040971; PlyB_C.
DR Pfam; PF01823; MACPF; 1.
DR Pfam; PF18684; PlyB_C; 1.
DR PROSITE; PS51412; MACPF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4OEJ, ECO:0007829|PDB:4OV8}.
FT DOMAIN 34..356
FT /note="MACPF"
FT /evidence="ECO:0000259|PROSITE:PS51412"
FT REGION 499..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 57094 MW; 67B9713731376D51 CRC64;
Query Match 100.0%; Score 2694; DB 12; Length 523;
Best Local Similarity 100.0%;
Matches 523; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MEAVLSRQAATAEAIGRFQDSSTSVGLVAGSPSTRIRRQADNVVLKSTSQAGDTLNDVIQ 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MEAVLSRQAATAEAIGRFQDSSTSVGLVAGSPSTRIRRQADNVVLKSTSQAGDTLNDVIQ 60
Qy 61 DPTRRNKLINDNNLLKGIIMGRDGPVPSSRELIVRPDTLRAIINNRATIETTTMEAEFTE 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 DPTRRNKLINDNNLLKGIIMGRDGPVPSSRELIVRPDTLRAIINNRATIETTTMEAEFTE 120
Qy 121 TLMESNYNSASVKVSAPFITANSEYSESSSFKNTETEKSMYTSSRYLFPQGRIDFTTPDS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 TLMESNYNSASVKVSAPFITANSEYSESSSFKNTETEKSMYTSSRYLFPQGRIDFTTPDS 180
Qy 181 GFDDVIKLSPQFTSGVQAALAKATGTEKREALQNLFQEYGHVFRTKVHIGGVLSAHTMET 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 GFDDVIKLSPQFTSGVQAALAKATGTEKREALQNLFQEYGHVFRTKVHIGGVLSAHTMET 240
Qy 241 FSRSENETEVKQDVKAGLEGAVKGWGGGATAGHGNTQGTITTSQNRKLNVKYIVNGGDYT 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 FSRSENETEVKQDVKAGLEGAVKGWGGGATAGHGNTQGTITTSQNRKLNVKYIVNGGDYT 300
Qy 301 KIQNTEEWVASTNQSEHWRVIEVTEVTAVADLLPQPIRGQVKDLLKPLLGKWVDVEKVPG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 KIQNTEEWVASTNQSEHWRVIEVTEVTAVADLLPQPIRGQVKDLLKPLLGKWVDVEKVPG 360
Qy 361 LESLPVSVYRPKGAIPAGWFWLGDTADASKALLVKPTLPARSGRNPALTSLHQGSGMTEQ 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 LESLPVSVYRPKGAIPAGWFWLGDTADASKALLVKPTLPARSGRNPALTSLHQGSGMTEQ 420
Qy 421 PFVDLPQYQYLSTYFGSFAHDTPPGSTLRGLRPDHVLPGRYEMHGDTISTAVYVTRPVDV 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 PFVDLPQYQYLSTYFGSFAHDTPPGSTLRGLRPDHVLPGRYEMHGDTISTAVYVTRPVDV 480
Qy 481 PFPEDECFDLKSLVRVKLPGSGNPPKPRSALKKSMVLFDSGEK 523
|||||||||||||||||||||||||||||||||||||||||||
Db 481 PFPEDECFDLKSLVRVKLPGSGNPPKPRSALKKSMVLFDSGEK 523
Centre for Advanced Molecular Imaging suggests expressing the genes for these pleurotolysins in plants to kill pests (pg 2, paragraph 4).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to replace the nucleic acids encoding the Cry34/35Ab1 binary toxin, in the construct taught by Bing et al, with nucleic acids encoding pleurotolysin A and B. One of ordinary skill in the art would have been motivated to do so because Centre for Advanced Molecular Imaging suggests expressing the genes for these pleurotolysins in plants to kill pests (pg 2, paragraph 4).
Because Bing teaches that it is possible to transform plants with multiple constructs that express proteins that interact with each other, one of ordinary skill in the art would have had a reasonable expectation of success in transforming plants with other multiple constructs that express proteins that interact with each other, like those encoding pleurotolysin A and B.
The resulting plants would be inherently protected against pests, including those of the family Chrysomelidae, insects, including larvae, imagos, those the genus Leptinotarsa, including Leptinotarsa decemlineata, and those the genus Diabrotica, including Diabrotica virgifera virgifera.
Response to Arguments
Applicant urges that Bing is directed to a specific Cry34Ab1/Cry35Ab1 maize event does not teach or suggest transforming a plant with a nucleic acid construct encoding pleurotolysin A and pleurotolysin B, much less the other elements of claim 1 (response pg 7).
This is not found persuasive because this is not an anticipation rejection or an obviousness rejection based on a single reference; this is a rejection based on a combination of references.
Bing is not cited for teaching a specific Cry34Ab1/Cry35Ab1 maize event. It is cited for teaching expressing multiple pest resistance proteins in a plant.
Applicant urges that Bing demonstrates the unpredictability of the Examiner's proposed modification, explaining that expression of foreign genes in plants is influenced by the location of insertion in the plant genome, that it is often necessary to screen a large number of events to identify an event having optimal expression of an introduced gene of interest, and recognizing that expression levels and spatial or temporal expression patterns may vary among event; thus, Bing does not teach a plug-and-play platform in which unrelated toxin components may be substituted with a reasonable expectation of success (response pg 7).
This is not found persuasive. The instant claims do not require optimal expression of the proteins, nor are they drawn to a specific transformation event. Bing is cited for their teaching of expression of multiple proteins in a plant.
Applicant urges that Bing's working example further confirms this event-specific unpredictability; their description of the transformation, selection of transformants, plant regeneration, molecular verification, confirmation of protein expression, whole-plant bioassay, and field evaluation is not a disclosure that any binary protein system can be substituted into Bing's construct with predictable success; it is a disclosure of a specific Bt event that required event generation, screening, and selection (response pg 7-8).
This is not found persuasive because the instant claims are not drawn to a specific transformation event. Bing’s teaching of transformation, selection of transformants, plant regeneration, molecular verification, confirmation of protein expression, whole-plant bioassay, and field evaluation demonstrates the methods needed to express pest resistance proteins in plants, including pleurotolysin A and pleurotolysin B, are within the abilities of those of ordinary skill in the art.
Applicant urges that the rejection improperly generalizes from Bing's bacterial system to the unrelated fungal protein complexes recited in the claims, which concern fungal aegerolysin-based complexes from Pleurotus; this is not a proposed substitution among closely related homologs as Cry34Ab1 has no significant similarity to representative Pleurotus aegerolysins and the proteins have a mechanistic distinction, as they target different membranes. Thus, Bing's Bt Cry34Ab1/Cry35Ab1 event would not have provided a reasonable expectation of success for the presently claimed fungal aegerolysin/PyB transformation system (response pg 8).
This is not found persuasive because Bing et al teach a method for expressing multiple pest resistance proteins in plants. Applicant does not explain why they think that the instant proteins or fungal proteins in general would behave differently and provide no evidnce to back up their assertions. Applicant is reminded that evidence submitted after final will not be considered unless Applicant provides a showing of good and sufficient reasons of why it is necessary and not earlier presented.
Proteins of multiple kingdoms, including plant, animal, fungal and bacterial, are routinely expressed in plants. Applicant has not provided any evidence that fungal proteins cannot be expressed in plants using methods like those in Bing, and cannot. See, for example, Ferrari et al (2008, Plant Physiol. 146:669-681), who expressed a fungal polygalacturonase in tobacco (paragraph spanning the columns on pg 670), Lorito et al (1998, PNAS 95:7860-7865), who expressed a Trichoderma endochitinase in tobacco (paragraph spanning pg 7860-7861), and Martinez et al (2015, Planta 242:39-52) who expressed a fungal protein in Arabidopsis using the fungal promoter (pg 44, left column, paragraphs 1-2).
These references and the thousands of patents to expressing heterologous proteins in plants show that such expression requires nothing more than routine experimentation. Bing's role in the rejection is teaching transforming multiple constructs encoding toxin proteins in plants. One of ordinary skill in the art would expect that fungal proteins, animal proteins, or proteins from any kingdom to be expressible in plants using routine methods, like those of Bing.
Applicant urges that Lukoyanova is directed to structural and mechanistic studies of pore formation by pleurotolysin but does not teach or suggest transforming a plant with nucleic acid constructs encoding PIyA/PIyB or ostreolysin/PIyB; Lukoyanova does not teach that such components could be expressed in a viable transformed plant, that they would assemble or function in planta after expression by a transformed plant, that the resulting transformed plant would have resistance against a plant pest, or teach subjecting such a transformed plant to an assay for verifying resistance against the plant pest (response pg 8).
This is not found persuasive because this is not an anticipation rejection or an obviousness rejection based on a single reference; this is a rejection based on a combination of references.
Applicant urges that Sakurai A and Sakurai B l are GenBank records providing sequence information for pleurotolysin A and pleurotolysin B from Pleurotus ostreatus; they do not teach plant transformation, expression of the recited fungal bi-component complex in a transformed plant, plant viability, pest resistance, or an assay verifying resistance of a transformed plant against a plant pest (response pg 8-9).
This is not found persuasive because this is not an anticipation rejection or an obviousness rejection based on a single reference; this is a rejection based on a combination of references.
Applicant urges that the Centre article is a public-facing article discussing the Lukoyanova structural study of pleurotolysin pore formation; it does not disclose any plant transformation experiment, does not disclose any construct for expressing PlyA/PlyB or ostreolysin/PIyB in plants, does not disclose any transformed plant, and does not disclose any assay verifying resistance of such a transformed plant against a plant pest (response pg 9).
This is not found persuasive because this is not an anticipation rejection or an obviousness rejection based on a single reference; this is a rejection based on a combination of references.
Applicant urges that at most, Centre includes a speculative statement that, in agriculture, such proteins "could be introduced into plants and crops" to help plants fight pests; that statement is not accompanied by experimental data, construct design, plant-expression data, transformed plant viability data, pest-resistance data, or any assay of the type recited in claim 1; such a speculative statement does not provide a reasonable expectation of success in modifying Bing's event-specific maize system by replacing the bacterial Cry34Ab1/Cry35Ab1 components with unrelated fungal aegerolysin/PIyB components, obtaining a viable transformed plant expressing a functional bi-component protein complex, and subjecting that plant to an assay verifying resistance against a plant pest (response pg 9).
This is not found persuasive because Centre provides the motivation to express these proteins in plants. Bing teaches that expressing multiple proteins in plants is possible and teaches subjecting transformed plants to an assay to verify resistance against a plant pest.
Applicant urges that the cited art has not been shown to provide direct experimental evidence that, before Applicant's work, a fungal aegerolysin-based protein complex would provide insecticidal activity against the claimed plant pests, much less that nucleic acid constructs encoding such components could be introduced into a plant genome to produce a viable transformed plant having verified pest resistance, and reflected unpredictability of this field, including testing in non-plant-pest biological systems that did not establish predictable activity against the claimed agricultural pests. Thus, Centre's speculative statement would not have provided a reasonable expectation of success (response pg 9-10).
This is not found persuasive because Centre’s speculation provides motivation to investigate these proteins in providing pests resistance to plants. Bing provides evidence that expressing multiple proteins in plants and testing them for pest resistance requires nothing more than routine experimentation. Applicant has not provided any evidence of unpredictability.
Applicant urges that the assay limitation in claim 1 in combination with the recited transformation using nucleic acid constructs encoding the fungal ostreolysin/PIyB or pleurotolysin A/PIyB bi-component protein complex, is not taught or suggested by the cited references; this limitation is significant in the context of plant transformation, where the expression and phenotype of transformed events are unpredictable and must be empirically evaluated. Although Bing describes bioassays for its specific Cry34Ab1/Cry35Ab1 maize event, the cited references do not teach or suggest transforming a plant with constructs encoding the recited fungal bi- component protein complex and then verifying resistance of that transformed plant against the plant pest (response pg 10).
This is not found persuasive because Bing’s teaching of assays provides the general methodology; an obviousness rejection over multiple references does not require that any one of those references teach all the elements of the claimed invention. Applicant has not shown that assaying for pest resistance cause by the claimed proteins required any undue experimentation.
Applicant urges that the cited references do not teach or suggest the method of amended claim 1, and do not provide a reasonable expectation of success in obtaining a transformed plant expressing the recited fungal bi-component protein complex and verifying resistance against a plant pest (response pg 10).
This is not found persuasive because the refences in combination suggest the claimed method as presented above.
Applicant urges that claims 19-20 are directed to a transgenic plant or progeny thereof that expresses or is capable of expressing the recited bi-component protein complex; the cited references do not teach or suggest transforming a plant to express the presently recited fungal ostreolysin/PIyB or pleurotolysin A/PIyB bi-component protein complex, and do not provide a reasonable expectation that such a transformed plant would be viable, would express a functional fungal bi-component protein complex, or would have plant pest resistance. Bing's disclosure of a specific Bt Cry34Ab1/Cry35Ab1 maize event does not render obvious the claimed transgenic plants expressing or capable of expressing the unrelated fungal bi-component protein complex (response pg 10-11).
This is not found persuasive. The refences in combination suggest the claimed method as presented above. Applicant has not explained why they think that these references, in combination, do not do so.
Claim 5 is rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Bing et al in view of Lukoyanova et al, Sakurai et al, Sakurai et al, and Centre for Advanced Molecular Imaging as applied to claims 1, 3-4, 6-16 and 18-20 above, and further in view of Ota et al (2013, Biochimie 95:1855-1864, including supplemental material).
The rejection is repeated for the reasons of record as set forth in the Office action mailed 17 March 2026. Applicant’s arguments filed 17 June 2026 have been fully considered but they are not persuasive.
The claim is drawn to a method comprising expressing an ostreolysin, including one with 95% identity to SEQ ID NO:1, and a pleurotolysin B with 95%-100% identity to SEQ ID NO:4 in a plant.
The teachings of Bing et al in view of Lukoyanova et al, Sakurai et al, Sakurai et al, and Centre for Advanced Molecular Imaging are discussed above. Bing et al in view of Lukoyanova et al, Sakurai et al, Sakurai et al, and Centre for Advanced Molecular Imaging do not teach use of a nucleic acid encoding ostreolysin.
Ota et al teach an ostreolysin with 100% identity to SEQ ID NO:1 (Figure S3):
ID OLYA6_PLEOS Reviewed; 138 AA.
AC P83467; M4QNV2;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 23-FEB-2022, entry version 43.
DE RecName: Full=Ostreolysin A6;
GN Name=OlyA6;
OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5322;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=23806422; DOI=10.1016/j.biochi.2013.06.012;
RA Ota K., Leonardi A., Mikelj M., Skocaj M., Wohlschlager T., Kunzler M.,
RA Aebi M., Narat M., Krizaj I., Anderluh G., Sepcic K., Macek P.;
RT "Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory
RT for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin
RT B.";
RL Biochimie 95:1855-1864(2013).
RN [2]
RP PROTEIN SEQUENCE OF 2-51, FUNCTION, SUBUNIT, AND DEVELOPMENTAL STAGE.
RC STRAIN=Plo 5; TISSUE=Fruiting body;
RX PubMed=12020804; DOI=10.1016/s0304-4165(02)00190-3;
RA Berne S., Krizaj I., Pohleven F., Turk T., Macek P., Sepcic K.;
RT "Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in
RT fungal fruiting.";
RL Biochim. Biophys. Acta 1570:153-159(2002).
CC -!- FUNCTION: Has hemolytic activity against bovine erythrocytes at
CC nanomolar concentrations in vitro. Promotes active pleurotolysin B
CC (PlyB)-dependent permeabilization of membranes rich in cholesterol and
CC sphingomyelin. May play an important role in the initial phase of
CC fungal fruiting. {ECO:0000269|PubMed:12020804,
CC ECO:0000269|PubMed:23806422}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12020804}.
CC -!- DEVELOPMENTAL STAGE: Expression begins during formation of the
CC primordia, increases remarkably as the fruiting bodies develop and
CC declines as they mature. {ECO:0000269|PubMed:12020804}.
CC -!- SIMILARITY: Belongs to the aegerolysin family. {ECO:0000305}.
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DR EMBL; KC012711; AGH25589.1; -; mRNA.
DR PDB; 6MYI; X-ray; 1.15 A; A/B/C/D=1-138.
DR PDB; 6MYJ; X-ray; 1.33 A; A/B/C/D=1-138.
DR PDB; 6MYK; X-ray; 1.80 A; A/B/C/D=1-138.
DR PDBsum; 6MYI; -.
DR PDBsum; 6MYJ; -.
DR PDBsum; 6MYK; -.
DR SMR; P83467; -.
DR TCDB; 1.C.119.1.2; the aegerolysin (aegerolysin) family.
DR TCDB; 1.C.97.3.2; the pleurotolysin pore-forming (pleurotolysin) family.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1090164; -.
DR GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:InterPro.
DR InterPro; IPR009413; Aegerolysin-typ.
DR Pfam; PF06355; Aegerolysin; 1.
DR PIRSF; PIRSF007951; PIRSF007951; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Hemolysis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12020804"
FT CHAIN 2..138
FT /note="Ostreolysin A6"
FT /id="PRO_0000156988"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 19..33
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:6MYI"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6MYI"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:6MYI"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:6MYI"
FT TURN 80..84
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6MYI"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:6MYI"
SQ SEQUENCE 138 AA; 15093 MW; F2A51BD2DC21426A CRC64;
Query Match 100.0%; Score 748; DB 1; Length 138;
Best Local Similarity 100.0%;
Matches 138; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MAYAQWVIIIIHNVGSQDVKIKNLKASWGKLHADGDKDAEVSASNYEGKIVKPDEKLQIN 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MAYAQWVIIIIHNVGSQDVKIKNLKASWGKLHADGDKDAEVSASNYEGKIVKPDEKLQIN 60
Qy 61 ACGRSDAAEGTTGTFDLVDPADGDKQVRHFYWDCPWGSKTNTWTVSGSNTKWMIEYSGQN 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ACGRSDAAEGTTGTFDLVDPADGDKQVRHFYWDCPWGSKTNTWTVSGSNTKWMIEYSGQN 120
Qy 121 LDSGALGTITVDTLKKGN 138
||||||||||||||||||
Db 121 LDSGALGTITVDTLKKGN 138
Ota et al teach that ostreolysin is homologous to pleurotolysin A (pg 1858, left column, paragraph 4) and interacts with pleurotolysin B to form pores (paragraph spanning the columns on pg 1858). Ota et al teach primers used for cloning the ostreolysin gene (Table S1).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to replace the pleurotolysin A in the plants taught by Bing et al in view of Lukoyanova et al, Sakurai et al, Sakurai et al, and Centre for Advanced Molecular Imaging with the ostreolysin described in Ota et al. One of ordinary skill in the art would have been motivated to do so because like pleurotolysin A, ostreolysin forms pores with pleurotolysin B (Ota et al, paragraph spanning the columns on pg 1858). Thus, one of skill in the art would expect that ostreolysin could be substituted for pleurotolysin B in the plants of Centre for Advanced Molecular Imaging and that the plants would still kill or control pests.
Response to Arguments
Applicant urges that Ota is directed to biochemical and membrane-based studies concerning the role of membrane cholesterol, sphingomyelin, and ostreolysin A in pore formation by pleurotolysin B. Ota may show that ostreolysin A can function with PIyB in certain biochemical pore-formation contexts, but Ota does not teach transforming a plant with nucleic acid constructs encoding ostreolysin and PIyB, does not teach expression of those proteins in a viable transformed plant, and does not teach subjecting such a transformed plant to an assay for verifying resistance against a plant pest (response pg 11).
This is not found persuasive because Bing teaches methods of plant transformation and assays for pest resistance. Ota is cited for teaching an ostreolysin with 100% identity to SEQ ID NO:1.
Applicant urges that Ota's experimental work is materially different from the presently claimed method; it concerns recombinant or native proteins, erythrocytes, lipid vesicles, membrane permeabilization, binding assays, and structural or biochemical characterization. Ota does not disclose a transformed plant, a plant genome comprising constructs encoding ostreolysin and PlyB, a transformed plant expressing a functional ostreolysin/PlyB bi- component protein complex, a plant pest resistance assay, or resistance of a transformed plant to Colorado potato beetle, Western corn rootworm, or any other plant pest (response pg 11-12).
This is not found persuasive. Bing, Lukoyanova, Sakurai A, Sakurai B, and Centre teach expressing PlyA/PlyB in plants. Ota et al teach that ostreolysin is homologous to pleurotolysin A (pg 1858, left column, paragraph 4) and interacts with pleurotolysin B to form pores (paragraph spanning the columns on pg 1858). One of skill in the art would expect that ostreolysin could be substituted for pleurotolysin A in those plants.
Applicant urges that Ota provides information concerning ostreolysin/PlyB pore formation under biochemical assay conditions, but that information does not provide a reasonable expectation that the Examiner's proposed modification of Bing's event-specific Cry34Ab1/Cry35Ab1 maize system would yield a viable plant transformed with nucleic acid constructs encoding the recited fungal components and having verified resistance against a plant pest (response pg 12).
This is not found persuasive. Bing is not cited for teaching a specific Cry34Ab1/Cry35Ab1 maize event. It is cited for teaching expressing multiple pest resistance proteins in a plant. Applicant has not explained why Ota’s teaching of the structural and functional similarity between ostreolysin and PlyA would not lead one of ordinary skill in the art to have a reasonable expectation that the two proteins would behave similarly when expressed in a plant with PlyB.
Claim 17 is rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Bing et al in view of Lukoyanova et al, Sakurai et al, Sakurai et al, and Centre for Advanced Molecular Imaging as applied to claims 1, 3-4, 6-16 and 18-20 above, and further in view of Perlak et al (1993, Plant Mol. Biol. 22:313-321).
The rejection is repeated for the reasons of record as set forth in the Office action mailed 17 March 2026. Applicant’s arguments filed 17 June 2026 have been fully considered but they are not persuasive.
The claims are drawn to a method comprising expressing a pleurotolysin A and a pleurotolysin B in a potato plant.
The teachings of Bing et al in view of Lukoyanova et al, Sakurai et al, Sakurai et al, and Centre for Advanced Molecular Imaging are discussed above. Bing et al in view of Lukoyanova et al, Sakurai et al, Sakurai et al, and Centre for Advanced Molecular Imaging do not teach expressing pleurotolysin A and pleurotolysin B in potato.
Perlak et al teach transformation of potato with a nucleic acid encoding CryIIIA (pg 315, left column, paragraph 2, to pg 316, left column, paragraph 3).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to transform potato plants with nucleic acid encoding pleurotolysin A and pleurotolysin B to make plants like the maize plants taught by Bing et al in view of Lukoyanova et al, Sakurai et al, Sakurai et al, and Centre for Advanced Molecular Imaging. One of ordinary skill in the art would have been motivated to do so because potato is subject to pest damage (Perlak et al, pg 313); one of ordinary skill in the art would want to control the damage to reduce growing costs.
The resulting plants would be inherently protected against pests, including herbivorous insects, larvae and imagos, and Colorado potato beetle because the instant specification teaches that these proteins inherently are toxic to the herbivorous pest Colorado potato beetle (I on pg 37).
Response to Arguments
Applicant urges that Perlak is directed to potato plants transformed with a modified crylllA gene encoding a Bacillus thuringiensis var. tenebrionis insect-control protein and therefore concerns a Bt Cry protein system, not the fungal ostreolysin/PIyB or pleurotolysin A/PIyB bi-component protein complexes (response pg 12).
This is not found persuasive Applicant has not explained why Perlak’s teaching of potato transformation would not lead one of ordinary skill in the art to have a reasonable expectation that the proteins could be expressed in potato.
Applicant urges that Perlak also underscores the unpredictability of expressing pesticidal proteins in plants; Perlak explains that expression of Bt genes in plants had been problematic and that the wild-type cryIIIA gene was poorly expressed in tomato and potato plants and therefore used a modified cryIIIA coding sequence that was extensively altered for plant expression while preserving the amino acid sequence. Even then, Perlak reports screening hundreds of transgenic potato plants to identify a subset showing complete protection in bioassays (response pg 13).
This is not found persuasive. Perlak teaches that even more than 20 years before the filing of the instant application, those of ordinary skill in the art knew how to successfully proteins in plants and screen for plants with desired expression levels.
Applicant urges that Perlak confirms that plant expression of pesticidal proteins can require extensive coding-sequence modification, transformation, screening, and bioassay work; Perlak does not teach transforming potato with nucleic acid constructs encoding ostreolysin/PIyB or pleurotolysin A/PIyB, does not teach expression of a functional fungal bi-component protein complex in potato, and does not teach the claimed method of verifying pest resistance in a potato plant transformed with such constructs (response pg 13).
This is not found persuasive because coding-sequence modification, transformation, screening, and bioassay work are all routine methods in the art; see Bing.
With respect to Applicant’s argument that Perlak does not anticipate the claimed invention, this is not an anticipation rejection or an obviousness rejection based on a single reference; this is a rejection based on a combination of references.
Applicant urges that Perlak may show that potato transformation with a particular modified Bt crylllA gene was known, but it does not provide the missing motivation or reasonable expectation of success necessary to arrive at claim 17 (response pg 13).
This is not found persuasive because the motivation to express the protein in plant comes from Centre and the motivation to extent that to potato comes from the desire to protect potato from pest damage, and reducing growing costs.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1, 3-16 and 18-20 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 12,049,637 in view of Bing et al (2008, US 7,323,556) and Centre for Advanced Molecular Imaging (2015, https://imagingcoe.org/carnivorous-mushrooms-reveal-human-immune-trick/).
The rejection is repeated for the reasons of record as set forth in the Office action mailed 17 March 2026, as applied to claims 1-16 and 18-20. Applicant’s arguments filed 17 June 2026 have been fully considered but they are not persuasive.
‘637, the parent of the instant application, claims a method of protecting a plant from a plant pest by applying a composition comprising applying to a plant a pleurotolysin B with 95% identity to SEQ ID NO:4 and either an ostreolysin with 95% identity to SEQ ID NO:1 or a pleurotolysin A with 95% identity to SEQ ID NO:2.
‘637 does not claim expressing the protein combinations in a plant.
The teachings of each of Bing et al and Centre for Advanced Molecular Imaging are discussed in the 35 USC 103 rejections above.
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to transform nucleic acids encoding pleurotolysin A and B or nucleic acids encoding ostreolysin and pleurotolysin B in a plant using the transformation methods taught in Bing et al. One of ordinary skill in the art would have been motivated to do so because Centre for Advanced Molecular Imaging suggests expressing the genes for these pleurotolysins in plants to kill pests (pg 2, paragraph 4).
Because Bing teaches that it is possible to transform plants with multiple constructs that express proteins that interact with each other, one of ordinary skill in the art would have had a reasonable expectation of success in transforming plants with other multiple constructs that express proteins that interact with each other, like those encoding pleurotolysin A and B or ostreolysin and pleurotolysin B.
Because the claims of ‘637 treat ostreolysin and pleurotolysin A as equivalents, one of ordinary skill in the art would expect plants transformed with constructs encoding ostreolysin and pleurotolysin B to also be protected from insect pests.
The resulting plants would be inherently protected against pests, including those of the family Chrysomelidae, insects, including larvae, imagos, those the genus Leptinotarsa, including Leptinotarsa decemlineata, and those the genus Diabrotica, including Diabrotica virgifera virgifera.
Response to Arguments
Applicant urges that claims 1-21 of’637 are directed to methods of protecting a plant against a plant pest and/or controlling or treating a plant pest by applying a composition comprising the recited protein components and a suitable carrier to the plant, while the instant claims are are directed to materially different subject matter, expression of the proteins in a plant (response pg 14).
This is not found persuasive. The claims of ‘637, indicate that pleurotolysin B plus either an ostreolysin or pleurotolysin A protect plants from plant pests. Centre suggests expressing the genes for the pleurotolysins in plants to kill pests. Bing teaches how to express multiple proteins that interact with each other in plants. The combination make obvious the instantly claimed invention.
Applicant urges that the '637 patent claims require exogenous application of a composition to a plant using spraying, dropping, or drenching, whereas the present claims require genetic transformation and assay-based verification of pest resistance in the transformed plant; these are not the same inventions (response pg 14).
This is not found persuasive because '637 in view of Bing and Centre make the claimed invention obvious, for the reasons cited above.
Applicant urges that Bing and Centre do not provide a teaching or reasonable expectation of success sufficient to render the presently claimed transformed plants and transformation/assay methods obvious; Bing is directed to an event-specific Cry34Ab1/Cry35Ab1 maize system, and Centre provides at most a speculative public-facing statement regarding possible agricultural use. Neither reference supplies the missing teaching that a plant could be transformed with nucleic acid constructs encoding the presently recited fungal bi-component protein complex and then assayed to verify resistance against a plant pest (response pg 14-15).
This is not found persuasive. Centre suggests expressing the proteins in plants. What more does Applicant want for a teaching that a plant could be transformed with nucleic acids constructs encoding pleurotolysins?
Claim 17 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 3-20 of U.S. Patent No. 12,049,637 in view of Bing et al (2008, US 7,323,556) and Centre for Advanced Molecular Imaging (2015, https://imagingcoe.org/carnivorous-mushrooms-reveal-human-immune-trick/) and further in view of Perlak et al (1993, Plant Mol. Biol. 22:313-321).
The rejection is repeated for the reasons of record as set forth in the Office action mailed 17 March 2026. Applicant’s arguments filed 17 June 2026 have been fully considered but they are not persuasive.
What is made obvious by ‘637 in view of Bing et al and Centre for Advanced Molecular Imaging is discussed above. ‘637 in view of Bing et al and Centre for Advanced Molecular Imaging alone do not make obvious expressing the proteins in potato.
Perlak et al teach transformation of potato with a nucleic acid encoding CryIIIA (pg 315, left column, paragraph 2, to pg 316, left column, paragraph 3).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to transform potato plants with nucleic acid encoding pleurotolysin A and pleurotolysin B or ostreolysin and pleurotolysin B. One of ordinary skill in the art would have been motivated to do so because potato is subject to pest damage (Perlak et al, pg 313); on of ordinary skill in the art would want to control the damage to reduce growing costs.
The resulting plants would be inherently protected against pests, including herbivorous insects, larvae and imagos, and Colorado potato beetle because the instant specification teaches that these proteins inherently are toxic to the herbivorous pest Colorado potato beetle (I on pg 37).
Response to Arguments
Applicant urges that Perlak is directed to potato plants transformed with a modified Bt cryIIIA gene, not to potato plants transformed with nucleic acid constructs encoding the presently recited fungal bi- component protein complex (response pg 15).
This is not found persuasive. Anticipation is not the standard for obviousness.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Anne R. Kubelik, Ph.D., whose telephone number is (571) 272-0801. The examiner can normally be reached Monday through Friday, 9:00 am - 5:00 pm Eastern.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Amjad Abraham, can be reached at (571) 270-7058. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/Anne Kubelik/Primary Examiner, Art Unit 1663
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