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 .
Status of Claims
The amendments received on 01/08/2026 have been entered. Claims 1-10, 12-25, and 27-32 are pending.
Claims 11 and 26 have been cancelled.
Claims 1, 7, 9-10, 13, 17, 22, 24-25, and 28 have been amended.
Claims 1-10, 12-25, and 27-32 are examined in this Office action.
Objections and Rejections that are Withdrawn
All objections to and rejections of claims 11 and 26 have been rendered moot by Applicant’s
cancellation of the claims.
The objections to claims 7, 9-10, 13, 24-25, and 28 have been withdrawn in light of
Applicant’s amendments to the claims. However, Applicant’s amendments have raised new grounds for objections.
The rejection of claims 1-10, 12-25, and 27-32 under 35 USC 102 has been withdrawn in light of
Applicant’s amendment to the claim. However, Applicant’s amendments have raised new grounds for a 35 USC 103 rejection.
Claim Objections
Claims 2, 13, 18, and 26 are objected to because of the following informalities:
Claims 2 and 18 recite “…the group consisting of…a dsRNA or a nucleotide…” in a Markush group, and this is not proper. A Markush group should not have “or”, but rather it should have a list with ---and--- between the last two terms in the list.
Claim 13 is objected to for not having an “and” or an “or” between the terms “SAW (Southern army worm, Spodoptera eridania)” and “FAW (Fall army worm)”.
Claim 26 is objected to because the claim status identifier (Cancelled) should not be followed by the text of the cancelled claim.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
Failure to Further Limit
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 8-9 and 23-24 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th 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.
Claims 1 and 17 recite “wherein the nucleotide sequence that encodes the transport peptide encodes a protein having between 70% and 100% sequence identity to any one of SEQ ID NOs: 1, 3-4”. SEQ ID NO: 1 is the Nezara viridula totivirus (NvTv-CP), SEQ ID NO: 3 is the Spodoptera frugiperda macula-like virus Tymoviridae (SfMLV-CP), and SEQ ID NO: 4 is the Spodoptera frugiperda rhabdovirus (SfRV-CP). Thus, the transport peptides of SEQ ID NOs: 1, 3-4 as recited in claims 1 and 17 are all derived from a plant pathogen virus, as required by claims 8 and 23. Additionally, claims 9 and 24 broaden the scope of claims 1 and 17, respectively, by including the limitation Omegatetravirus.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
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.
Claims 1-10, 12-25, and 27-32 are rejected under 35 U.S.C. 103 as being unpatentable over MILLER (Miller et al., International Publication Number: WO 00/15758, International Publication Date: 23 March 2000) in view of MA (Ma et al., 2014, Journal of Virology, Vol. 88(12), pp. 6576-6585; included on IDS dated 07/30/2024). Initially, it is noted that this is a new rejection necessitated by claim amendment.
Claim 1 recites “[a] plant comprising an expression construct wherein said expression construct contains a promoter operably linked to a nucleotide sequence that comprises a nucleotide sequence that encodes a transport peptide operably fused to a cargo molecule, wherein the nucleotide sequence that encodes the transport peptide encodes a protein having between 70% and 100% sequence identity to any one of SEQ ID NOs: 1, 3-4.”
MILLER teaches and claims a chimeric gene comprising DNA, said DNA having a first nucleotide sequence encoding a first polypeptide segment, said first polypeptide segment being a transport peptide (i.e., transport peptide) of a circulatively transmitted virus, and a second nucleotide sequence encoding a second polypeptide segment, said second segment being an insect-toxic peptide (i.e., cargo molecule), and a heterologous promoter sequence operatively linked to the DNA encoding the fusion protein (i.e., a promoter operatively linked to the nucleotide sequence) (Miller, Abstract and claim 35); a recombinant vector comprising the chimeric gene (i.e., an expression construct) (Miller, claim 37); a transgenic plant or plant tissue comprising the transgenic plant cell (i.e., a plant) (Miller, claim 40).
The “transport peptide” required by the claims is any of instant sequences SEQ ID NOs: 1, 3-4. Lepidopteran virus, Spodoptera frugiperda macula-like virus (Tymoviridae) encodes SfMLV-CP (coat protein), which is instant sequence SEQ ID NO: 3; Lepidopteran virus, Spodoptera frugiperda rhabdovirus encodes SfRV-CP (coat protein), which is instant sequence SEQ ID NO: 4.
MILLER further teaches and claims examples of virus groups that are transported across insect vector membranes include: tospoviruses, plant reoviruses, plant rhabdoviruses (i.e., Spodoptera frugiperda rhabdovirus), tenuiviruses, marafiviruses, luteoviruses, geminiviruses, enamoviruses, tymoviruses (i.e., Spodoptera frugiperda macula-like virus (Tymoviridae)), como viruses, and sobemoviruses (Miller, page 2, lines 6-9; claims 2 and 19).
MILLER does not explicitly teach instant sequences SEQ ID NOs: 1, 3-4.
However, MILLER teaches that any peptide having a toxic effect when present in the circulatory system of a target insect can, in principle, be incorporated into a toxic fusion protein. Virus proteins that cross the gut barrier of an insect or other pest organism can be exploited for direct delivery of a variety of toxic agents which are active only in the body cavity of that organism. The requirements for these toxic agents include that (1) the agent should be specific for the targeted pest without mammalian toxicity; (2) the agent should be active at low levels; (3) the agent should have a rapid effect on the host. These toxic agents include both toxins that act on the nervous system of insects , and physiological effectors which disrupt regulation of homeostasis in the insect, resulting in feeding inhibition and/or death. A variety of such toxins and physiological effectors have already been exploited specifically for the control of lepidopteran (moth) pests by recombinant baculovirus expression. The insect-specific neurotoxins have generally been considered to be more effective than physiological effectors, in part because of feed-back regulatory systems in the insect for the latter. There is an ongoing effort within commercial, government and academic laboratories to isolate toxins that specifically target the insect nervous system from a variety of organisms that use venoms to immobilize their prey. The virus coat protein delivery system can be exploited for delivery of all of these agents in an array of pest species (Miller, page 8, lines 3-19).
MILLER further teaches that the term "transport peptide" is defined as that peptide segment which is necessary for transport of a circulatively-transmitted virus from the gut to the hemocoel of an insect. A transport peptide can include all, or a portion of, a virus coat protein or other virus protein and can also include all or part of a readthrough domain. That portion of a coat protein or other virus protein which constitutes a transport peptide is termed a component of the coat or other protein. It will be understood in the art that a specific interaction exists between the transport peptide of a virus and the insect host of the virus. A peptide intended to serve as a transport peptide for a given insect species is obtained from a circulatively transmitted virus that is known to infect that insect, as would be understood in the art (Miller, page 14, lines 10-18).
MA teaches that rhabdoviruses are ubiquitous in nature and have a broad host range, including invertebrates, vertebrates, and plants. Over 200 rhabdoviruses have been identified, and a majority of the plant rhabdoviruses and some vertebrate rhabdoviruses use an insect vector for transmission. However, only a few rhabdoviruses have been directly isolated from insects or insect cell lines, including the discovery of a novel rhabdovirus in the Spodoptera frugiperda Sf9 cell line, which is the first rhabdovirus found in the order Lepidoptera (Ma, Discussion, page 6582).
MA further teaches that the Sf-rhabdovirus was seen in Sf9 cells by EM analysis of the filtered supernatant from Sf9 cells. The large number of extracellular particles produced from the cells indicated that the virus was most likely replicating in the cells, and its persistence indicated that it was constitutively produced from the Sf9 cell line. Furthermore, the virus had established a persistent infection in Sf9 cells, since Sf-rhabdovirus sequences were also detected in the parent Sf21 cell line (Ma, Discussion, page 6583, right column, last paragraph).
Ma teaches the Spodoptera frugiperda rhabdovirus sequence which shares 100% sequence identity with instant sequence SEQ ID NO: 4 (i.e., protein having between 70% and 100% sequence identity to any one of SEQ ID NOs: 1, 3-4).
MA SPODOPTERA FRUGIPERDA RHABDOVIRUS SEQUENCE ALIGNED WITH INSTANT SEQ ID NO:4
Qy 1 MVFLSLSTIIFILSLRAVTCSNPLSYPNGILTNNSTHNHPLSDFYIFYENSSLTYTQFPV 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MVFLSLSTIIFILSLRAVTCSNPLSYPNGILTNNSTHNHPLSDFYIFYENSSLTYTQFPV 60
Qy 61 APDCSSILDTRDEQYPTTVTLWKVDQESQAEWGLLLWQERIDTTCSWNFWGNYKGSIVSK 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 APDCSSILDTRDEQYPTTVTLWKVDQESQAEWGLLLWQERIDTTCSWNFWGNYKGSIVSK 120
Qy 121 SSVPLKDIPSGSARNGYWALSNDEVQEIDHVPYNLRYYCYWCRNEYPGSFYMRYVKKVRI 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SSVPLKDIPSGSARNGYWALSNDEVQEIDHVPYNLRYYCYWCRNEYPGSFYMRYVKKVRI 180
Qy 181 IRNPDGSIKTPRGSWVHELDNLWGDQMRYLVIRRFGGESSCPLKIYDVRAGVLSKSRSNF 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 IRNPDGSIKTPRGSWVHELDNLWGDQMRYLVIRRFGGESSCPLKIYDVRAGVLSKSRSNF 240
Qy 241 ILVSLPSLNLQFSVSLESTETKCSFGDKTYDIVQSMGGYLLSIDIGNANWRGPWDPTPQH 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 ILVSLPSLNLQFSVSLESTETKCSFGDKTYDIVQSMGGYLLSIDIGNANWRGPWDPTPQH 300
Qy 301 PGRERRSIMEFPDQTSFRYNQFINYHSSPRHKRHDQEFEFPLSLKSSYDYAQFRYEQNFI 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 PGRERRSIMEFPDQTSFRYNQFINYHSSPRHKRHDQEFEFPLSLKSSYDYAQFRYEQNFI 360
Qy 361 IRQINKNFGLLQKSICDIQFSKWQNLSPPNLAMKIAHYVTGSIHSIGGVHHGSYSIQRTE 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 IRQINKNFGLLQKSICDIQFSKWQNLSPPNLAMKIAHYVTGSIHSIGGVHHGSYSIQRTE 420
Qy 421 KSITKVNLVFPIVIVHGMYKCQREPSKEVVWAEPVTGILFKSPIPTHFSLSSSWLPGVNG 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 KSITKVNLVFPIVIVHGMYKCQREPSKEVVWAEPVTGILFKSPIPTHFSLSSSWLPGVNG 480
Qy 481 SSIVPLTGQILLPEITMDHLEVVQQVEAKMVKSMYTNVELFGSTEEFQRYQTQGITSDEQ 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 SSIVPLTGQILLPEITMDHLEVVQQVEAKMVKSMYTNVELFGSTEEFQRYQTQGITSDEQ 540
Qy 541 SNTVNPWIGLLIHGGVSIATGILVALLIPSILKLFRHIIEKGEASLEERLHLRETSRKEF 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 SNTVNPWIGLLIHGGVSIATGILVALLIPSILKLFRHIIEKGEASLEERLHLRETSRKEF 600
Qy 601 VKVRGKPWGV 610
||||||||||
Db 601 VKVRGKPWGV 610
At the time the instant application was filed, it would have been obvious and within the scope of one having ordinary skill in the art to use the Spodoptera frugiperda rhabdovirus sequence taught by MA as the transport peptide of the fusion protein taught by MILLER. One would have been motivated to use the Spodoptera frugiperda rhabdovirus sequence taught by MA as the transport peptide of the fusion protein taught by MILLER knowing that the Spodoptera frugiperda rhabdovirus can infect Spodoptera frugiperda cells, as taught by MA. Thus, one of ordinary skill in the art would have a high expectation of success by following the teachings of MILLER and MA, since using an expression construct comprising a promoter operably linked to a nucleotide sequence that comprises a nucleotide sequence that encodes a transport peptide operably fused to a cargo molecule for plant disease resistance is well-known in the art and has been employed in plant defense for decades.
In regard to claims 2 and 18, MILLER teaches that modified plant viruses can also be used as a spray on the surface of the crop plant, where ingestion by the target insect introduces the toxic protein to the insect gut. The invention therefore includes delivery of any protein to the hemocoel of any arthropod or other organism that takes up and transmits viruses in a circulative or non-circulative fashion. (i.e., wherein the cargo molecule is a nucleotide sequence encoding a protein) (Miller, page 13, lines 11-12 and 16-18).
In regard to claims 3-4 and 19-20, MILLER teaches and claims a fusion protein consisting of a second segment being a peptide toxin effective against insects (i.e., wherein the cargo molecule is active against a plant pathogen, instant claims 3 and 19; wherein the cargo molecule is insecticidal, instant claims 4 and 20) (Miller, Abstract; claims 1, 18, 35, 41, 43, 47, 51, and 55).
In regard to claims 5-6 and 21, MILLER teaches combining a peptide toxin effective against insects (i.e., small molecules with pesticidal activity, instant claim 5; the cargo molecule is a nucleotide sequence that encodes a pesticidal protein, instant claim 21) with a transport peptide capable of facilitating transfer of the peptide toxin from the gut of an insect to the hemocoel. The combination can be effected by a fusion of genetic material encoding the peptide toxin and the transport peptide, such that expression of the genetic material fusion results in synthesis of a fusion protein combining the functions of both the toxin and the transport protein (i.e., wherein the transport protein and the cargo molecule form a fusion peptide upon expression in a plant; instant claim 6) (Miller, page 7, lines 17-22).
In regard to claims 7 and 22, MILLER teaches that transgenic plants that resist insects have been constructed with agents that are active in the gut of insects. The most notable example is the use of the Bacillus thuringiensis toxin (Bt) genes (i.e., wherein the pesticidal protein is a Cry protein) (Miller, page 5, lines 14-16).
In regard to claims 8-9 and 23-24, MILLER teaches and claims a fusion protein, wherein the circulatively transmitted virus is a virus selected from the groups of viruses that include tospovirus, plant reovirus, plant rhabdovirus, tenui virus, marafivirus, luteovirus, geminivirus, enamovirus, tymovirus, como virus, and sobemo virus (i.e., wherein the transport peptide is derived from a plant pathogen virus, instant claims 8 and 23; wherein the plant pathogen virus is any virus selected from the group consisting of totivirus, Omegatetravirus, Tymoviridae, and rhabdovirus, instant claims 9 and 24) (Miller, page 2, lines 6-9; claims 2 and 19).
In regard to claims 10 and 25, MA teaches the discovery of a novel rhabdovirus in the Spodoptera frugiperda Sf9 cell line, which is the first rhabdovirus found in the order Lepidoptera (i.e., wherein the plant pathogen virus is Spodoptera frugiperda rhabdovirus) (Ma, Discussion, page 6582).
In regard to claims 12-13 and 27-28, MA teaches the Sf9 cell line, which was derived from pupal ovarian tissue of S. frugiperda. It is noted that the order of S. frugiperda is Lepidoptera. (i.e., wherein the plant pathogen is lepidopteran, instant claims 12 and 27; wherein the plant pathogen is Fall army worm Spodoptera frugiperda, instant claims 13 and 28) (Ma, Materials and Methods, page 6577, left column, first full paragraph).
In regard to claim 14, MILLER teaches that the invention allows the person or ordinary skill in the art to construct a fusion protein combining a transport peptide and an insect-toxic peptide for control of a large range of insects that damage a large variety of plants of commercial importance. Such plants include, but are not limited to, wheat, barley, oats, rice, corn, potato, sugar beet, soybean, tomato, citrus (orange, lemon, lime, grapefruit), Rosaceae (rose), fruit trees (plum, apple, cherry, peach, pear), lettuce, french bean, sugar cane, papaya, squash, cucurbits, banana, cassava, sweet potato, grape, all ornamentals and the like, including other members of the plant families to which the foregoing plants belong (i.e., wherein the plant is either a monocot or dicot) (Miller, page 12, lines 14-21).
In regard to claims 15 and 29, MILLER teaches combining a peptide toxin effective against insects with a transport peptide capable of facilitating transfer of the peptide toxin from the gut of an insect to the hemocoel (i.e., wherein the expressed fusion peptide enters the hemocoel of an insect) (Miller, page 7, lines 17-19).
In regard to claims 16 and 30, MILLER teaches and claims a method of producing an insect-resistant plant comprising introducing a DNA encoding a fusion protein, said DNA having a first nucleotide sequence encoding a first polypeptide segment, said first polypeptide segment being a transport peptide of a circulatively transmitted virus, and a second nucleotide sequence encoding a second polypeptide segment, said second segment being an insect-toxic peptide, into said plant, wherein said DNA is expressible in said plant in an effective amount to control said insect (Miller, claims 43, 47, and 51). To "control" insects means to inhibit, through a toxic effect, the ability of insect pests to survive, grow, feed, and/or reproduce, or to limit insect-related damage or loss in crop plants, to "control" insects may or may not mean killing the insects, although it preferably means killing the insects (wherein the expressed fusion peptide kills the insect or decreases the insects growth) (Miller, page 16, lines 1-4).
In regard to claims 31 and 32, MILLER teaches the expression of CP-RTD-AaIT fusion proteins in oat protoplasts and oat protoplast inoculation (i.e., a cell comprising the expression construct, instant claim 31; wherein the cell is a plant cell, instant claim 32) (Miller, pages 23-26).
Response to Applicant’s Arguments
Initially it is noted that the 35 USC 103 rejection above is a new rejection and does not rely upon the prior art argued against in the Remarks dated 01/08/2026.
Summary
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 nonprovisional extension fee (37 CFR 1.17(a)) 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 mailing date of this final action.
Correspondence
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHRISTINA MEADOWS whose telephone number is (703)756-1430. The examiner can normally be reached Monday - Friday 9:00 am - 5:00 pm.
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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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CHRISTINA MEADOWS
Examiner
Art Unit 1663
/CHRISTINA L MEADOWS/Examiner, Art Unit 1663
/Amjad Abraham/SPE, Art Unit 1663
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