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 .
Continued Examination under 37 CFR § 1.114
A request for continued examination under 37 CFR § 1.114, including the fee set forth in 37 CFR § 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR § 1.114, and the fee set forth in 37 CFR § 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR § 1.114.
Applicants’ submission filed on October 06, 2025 has been entered.
Status of the Claims
Applicants’ remarks submitted on October 06, 2025 have been entered.
No new claim amendments have been presented.
Claims 1-4, 6-12, 18-23, and 29 are examined in this Office action.
Response to Amendment
The Declarations under 37 CFR § 1.132 filed on 10/06/2025 by Dr. Jerry J. Hjelle and Dr. Cesar Moises Camilo are acknowledged. These Declarations provide arguments and experimental data in favor or the patentability of the instant claims vs. the prior art teachings of the BAUM reference.
Claim Interpretation
Instant SEQ ID NO:4 is a 24-bp-long nucleotide sequence: aaaaatgccg cgacttgcgg acgt. See sequence listing.
Instant SEQ ID NO:5 is a 34-bp-long nucleotide sequence: cccgccttca gtttaaactt tggcatttgt ggaa. See sequence listing.
Claim Rejections - 35 USC § 103
Claims 1-4, 6-12, 18-23, and 29 are rejected under 35 U.S.C. § 103 as being unpatentable over BAUM (Baum et al., United States Patent Application Publication No. 2018/0087068 A1, published 29 March 2018).
The claims are drawn to a nucleic acid molecule comprising a nucleotide sequence unique to maize event ME240913,which is SEQ ID NO:4 or SEQ ID NO:5, which nucleic acid molecule encodes a truncated Cry1Da protein comprising the amino acid sequence of SEQ ID NO:3, wherein the nucleic acid comprises a nucleotide sequence of SEQ ID NO:8; wherein the nucleic acid molecule is contained in a maize seed deposited with the American Type Culture Collection under accession number PTA-126224, to a maize plant, cell. Or plant tissue comprising the nucleic acid, high level of protection to maize plant leaves against Lepidoptera pests, including S. frugiperda, and to a method for detecting the presence of a nucleic acid molecule that is unique to Event ME240913 in a sample comprising maize nucleic acids.
BAUM teaches corn (maize) plants, which may be used to make commodity products (¶0016); in the context of compositions containing insect inhibitory amounts of engineered Cry1Da proteins (as “engineered toxin proteins”), recombinant plants, plant parts, and seeds containing polynucleotide constructs encoding one or more of the improved engineered Cry1Da proteins, for in planta resistance management and Lepidopteran insect pest control (Abstract, ¶0007, for example).
BAUM teaches that several amino acid sequence variants of the Cry1Da protein have been identified that exhibit markedly improved activity (compared to the Cry1Da1 native toxin) towards Helicoverpa zea while retaining excellent activity towards Spodoptera frugiperda. The improved variants of Cry1Da have been engineered (“engineered toxin proteins”) to be expressed in crop plants, e.g., corn, and provide novel options for in planta resistance management and Lepidopteran insect pest control in view of the apparent unique mode-of-action of Cry1Da coupled with the engineered improvement in activity against Helicoverpa zea. The engineered insecticidal proteins of the invention each contain at least one amino acid substitution, one amino acid addition, or one amino acid deletion (i.e., truncation) compared to the scaffold proteins set forth in any of SEQ ID NO:2 or SEQ ID NO:14. (¶¶0007-0008).
BAUM teaches and claims specific commodity products which may be made from the maize plants of their disclosure including oil, meal, sugar, animal feed, flour, flakes, bran, lint, hulls, processed seed, and seed (¶0091; Claim 19 of BAUM).
The instant specification describes that the maize plants of the instant disclosure comprise Event ME240913, which comprises a nucleic acid encoding the claimed protein of SEQ ID NO:3 (Pg. 8, Lines 10-28). The instant specification also describes SEQ ID NO:3 as corresponding to an insecticidal Cry1Da protein (Pg. 8 Lines 10-28); thus paralleling the teachings of BAUM.
BAUM additionally teaches insecticidal Cry1Da proteins which exhibit activity against lepidopteran insect pests, as well as polynucleotide sequences encoding said insecticidal Cry1Da proteins (Abstract). One such insecticidal protein taught by BAUM is the disclosed SEQ ID NO:28 (Table 2). The instantly claimed truncated Cry1Daprotein comprising the amino acid sequence of SEQ ID NO:3 shows 100% identity to the SEQ ID NO:28 disclosed by BAUM (Bacillus thuringiensis Cry1Da1 protein); see alignment at pages 4-5 in the Office action dated 05/08/2024; and at page 5 in the Office action dated 05/05/2025.
BAUM teaches polynucleotides encoding the insecticidal proteins of the disclosure. The nucleic acid sequence of SEQ ID NO:27 (i.e., nucleic acid molecule) taught by BAUM encodes the corresponding protein of SEQ ID NO:28 (¶0049, ¶0050).
BAUM also teaches SEQ ID NO:2 as a Cry1Da1 protein toxin.
BAUM further teaches a method of inhibiting Lepidopteran pests from feeding on a crop plant comprising modifying one or more amino acid residue(s) of SEQ ID NO:2 through substitution of the one or more amino acid residue(s) to produce a modified SEQ ID NO:2; and
making available a Lepidopteran-inhibiting amount of the modified SEQ ID NO:2 (¶0018).
In Example 1 on pages 10-11, BAUM devotes an entire section to teachings regarding the design of modified test proteins. In Example 3 on pages 11-12, BAUM describes how the modified tests proteins created from the engineering efforts described in Example 1 were tested in repetitive rounds in which the Lepidopteran species activities of the modified test proteins were compared to their respective parent scaffold protein (i.e., Cry1Da1 and TIC844). Of the three hundred and seventy (370) modified test proteins which demonstrated increased toxicity against CEW when compared to the scaffold proteins in single-dose assay screens, about one hundred eighty (180) of them were further tested in FAW bioassays to determine whether these modified test proteins maintained or exhibited increased FAW activity compared to their scaffold protein parents (¶0116).
In Table 2 on page 121, BAUM teaches individual amino acid mutations and activity data for scaffold proteins and engineered insecticidal proteins. The data begins with Cry1Da1 (SEQ ID NOs:2, 28).
BAUM teaches that maize may be transformed with the nucleic acid encoding the Cry1Da sequence SEQ ID NO:28, and also teaches that several transgenic maize events were derived in their analyses which comprised a nucleic acid encoding the protein of SEQ ID NO:28 of their disclosure (¶0127 – ¶0130; Table 6). BAUM further teaches that the transgenic maize plants expressing the Cry1Da protein corresponding to SEQ ID NO:28 were effective in inhibiting the growth of insect pests (Table 6). To test pesticidal activity, bioassays were performed in the presence of Lepidopteran pest larvae using plant leaf disks obtained from the transformed plants (¶0083) (i.e., expression in leaf tissue).
BAUM also teaches methods of making transgenic plants that comprise Lepidoptera-inhibitory amounts of engineered insecticidal proteins. Such plants can be made by introducing a polynucleotide that encodes the engineered insecticidal proteins provided in this application into a plant cell, and selecting a plant derived from said plant cell that expresses an insect or Lepidoptera-inhibitory amount of the engineered insecticidal protein. Plants can be derived from the plant cells by regeneration, seed, pollen, or meristem transformation techniques (¶0089).
BAUM teaches that plants expressing the engineered insecticidal proteins can be crossed by breeding (i.e., sexually crossing) with transgenic events expressing other insecticidal proteins and/or expressing other transgenic traits such as other insect control traits, herbicide tolerance genes, genes conferring yield or stress tolerance traits, and the like (i.e., to produce progeny plants containing the engineered insecticidal proteins) (¶0090).
BAUM further teaches that nucleotide sequences encoding the engineered insecticidal proteins can be used as probes and primers for screening to identify other members of the class using thermal-cycle or isothermal amplification and hybridization methods (i.e., amplicons). For example, oligonucleotides derived from sequences as set forth in SEQ ID NO: 3 can be used to determine the presence or absence of an engineered insecticidal transgene in a deoxyribonucleic acid sample derived from a commodity product (¶0099).
BAUM teaches that engineered insecticidal protein-encoding sequences and sequences having a substantial percentage identity to the engineered insecticidal proteins can be identified using methods known to those of ordinary skill in the art such as polymerase chain reaction (PCR), thermal amplification and hybridization (i.e., amplicon) (¶0099).
BAUM also teaches that the presence of the nucleic acids of their disclosure may be tracked in processed plant products (i.e. commodity products) produced from the disclosed maize plants by identifying nucleotide sequences specific to said nucleic acids (¶0091).
BAUM teaches that the engineered insecticidal proteins in some embodiments may include at least one amino acid modification of the following relative positions of TIC844 (SEQ ID NO:14) or CrylDal (SEQ ID NO:2): serine at position 282 replaced by lysine or valine, tyrosine at position 316 replaced by serine, isoleucine at position 368 replaced by praline or arginine, serine at 374 replaced by arginine, asparagine at position 375 replaced by histidine, and isoleucine at position 432 replaced by leucine. The engineered insecticidal proteins can also include at least two, three, four, or more of these amino acid substitutions or deletions within the same engineered insecticidal protein sequence (0078).
BAUM teaches fragments of the engineered insecticidal proteins, which can be truncated forms (¶0080). BAUM specifically teaches that “[f]ragments of the engineered insecticidal proteins described herein can be truncated forms wherein one or more amino acids are deleted from the N-terminal end, C-terminal end, the middle of the protein, or combinations thereof without a loss of insect inhibitory activity. These fragments should retain the insect inhibitory activity of the parent engineered insecticidal protein.” (paragraph 0080; emphasis supplied). Indeed, the instantly claimed SEQ ID NO:3 is precisely that, a truncated Cry1Da protein. See also BAUM’s Table 1 (and accompanying paragraph 0079), describing characteristics of TIC844, Cry1Da1, and the 40+ engineered insecticidal proteins. These vary in length from 1069 to 1165 amino acids.
BAUM teaches a plurality of experiments. In a first round, three hundred and seventy (370) different modified test proteins demonstrated increased toxicity against CEW relative to TIC844 or Cry1Da1 in diet bioassays (0115). Of the three hundred and seventy (370) modified test proteins which demonstrated increased toxicity against CEW when compared to the scaffold proteins in single-dose assay screens, about one hundred eighty (180) of them were further tested in FAW bioassays to determine whether these modified test proteins maintained or exhibited increased FAW activity compared to their scaffold protein parents. About forty (40) to fifty (50) of these modified test proteins exhibited similar or better FAW activity than their parent
scaffold proteins. These further-screened modified test proteins were also tested in additional CEW bioassays to confirm CEW activity. Table 2 identifies these engineered insecticidal proteins and the amino acid mutations in each engineered insecticidal protein (0116).
BAUM does not explicitly teach the instantly claimed nucleic acid molecule comprising a nucleotide sequence unique to maize event ME240913,which is SEQ ID NO:4 or SEQ ID NO:5, instant SEQ ID NO:8, and a method of producing a maize plant comprising maize event ME240913, whose seed is deposited with the ATCC under PTA-126224. However, such claimed compositions and methods practiced with them would have been prima facie obvious to a person of ordinary skill in the art at the time of filing. They are mere optimizations of the compositions and methods taught by BAUM, absent evidence to the contrary.
In this case, Applicants have simply taken the teachings of BAUM and have generated transgenic maize plants expressing the engineered Cry1Da proteins taught by BAUM. For example, Applicants claim a nucleic acid molecule that is unique to Event ME240913 (instant claim 1), and which also encodes a truncated Cry1Da protein comprising instant SEQ ID NO:3 = BAUM’s SEQ ID NO:28 (instant claim 2). Thus, the instantly claimed truncated Cry1Da protein of SEQ ID NO:3, which confers improved Lepidopteran insecticidal activity, is expressly taught by BAUM as SEQ ID NO:28, as an “amino acid sequence of Cry1Da1 encoded by a synthetic DNA sequence”; see annotation in the Sequence Listing in BAUM. The instantly claimed Event ME240913 in maize (and the associated SEQ ID NOs:4-5) follow(s) from the teachings of BAUM. The obtained transgenic maize plants could then obviously be deposited with the ATCC (under a given PTA number).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to modify a maize plant by transforming it with an engineered Cry1Da protein (as “engineered toxin protein”) taught by BAUM; with a reasonable expectation of improving Lepidopteran (including Spodoptera frugiperda) insecticidal activity, and without any surprising results. One of ordinary skill in the art would have been motivated to do so to improve Lepidopteran insecticidal activity of maize plants, as taught by BAUM.
Applicants are reminded that the burden is on Applicants to establish results that are unexpected and significant. The evidence relied upon should establish "that the differences in results are in fact unexpected and unobvious and of both statistical and practical significance." Ex parte Gelles, 22 USPQ2d 1318, 1319 (Bd. Pat. App. & Inter. 1992) (Mere conclusions in appellants’ brief that the claimed polymer had an unexpectedly increased impact strength "are not entitled to the weight of conclusions accompanying the evidence, either in the specification or in a declaration."); Ex parte C, 27 USPQ2d 1492 (Bd. Pat. App. & Inter. 1992) (Applicant alleged unexpected results with regard to the claimed soybean plant, however there was no basis for judging the practical significance of data with regard to maturity date, flowering date, flower color, or height of the plant.). See also In re Nolan, 553 F.2d 1261, 1267, 193 USPQ 641, 645 (CCPA 1977) and In re Eli Lilly, 902 F.2d 943, 14 USPQ2d 1741 (Fed. Cir. 1990) as discussed in MPEP § 716.02(c). Evidence of unexpected properties may be in the form of a direct or indirect comparison of the claimed invention with the closest prior art which is commensurate in scope with the claims. See In re Boesch, 617 F.2d 272, 205 USPQ 215 (CCPA 1980) and MPEP § 716.02(d) - § 716.02(e). See In re Blondel, 499 F.2d 1311, 1317, 182 USPQ 294, 298 (CCPA 1974) and In re Fouche, 439 F.2d 1237, 1241-42, 169 USPQ 429, 433 (CCPA 1971) for examples of cases where indirect comparative testing was found sufficient to rebut a prima facie case of obviousness. See MPEP § 716.02(b).
Regarding claim 29, instant SEQ ID NO:9 appears to be merely a larger construct sequence, which includes flanking regions (see annotations in the Sequence Listing). A translation product of the 6424-nucleotides-long SEQ ID NO:8 results in the following:
Translate results
>rf 1 Untitled
DTRHVIDGVVGEGTREGEVDGSNTNNRVAREFCAKNAATCGRF*CTELTPNCSSIRHSGC
ATVGKGDRCGPLRYYASWRKGDVLQGD*VG*RQGFPSHDVVKRRPVPS*FASRRAQITIS
TPLYFYCTPF*LFFITKMPWKMHSLFVFVFL*NDVVR*FICQSTMVAHYINSNCRSNRRR
RFSAFV*PRGFYDILY*LICKTYPIKDLICSKD*YLMITIFF**RKG*LVNMEQGQKIY*
SRVRDNK*VRGVS*VTYPHNIK*H*QT*LMLLFE*CISAYLITYR*EQTLARLLSRSR*R
AGPDGAVPAG*SPAARNPRHASSRA*SRPPAACRGGHIRAPRACARSGRWAAR*QRPRS*
SPVPPGTSAGGCRAWSPVPSAGGGGRRTRSTRPSSRRRCVPSRGPRRRCRRPRRPPRRRA
RDSAPADGRGRPSTPAVPAARYGS*PCLSRCSG*RWCRPPACPPRWHGGCRPGVVLGSW*
IPRS*MVKIFRKLLLL*KK*FKLLQ*K*NA*LLEIRLFCICCVEN*FSRSSPNEMNFLI*
RKGLAKDSGIVRHPLRQWRYHINPLALKTWLERLLFPRCSSWVGVHLWDHCRQRHLQRWP
FLYRNDGICRSHLPFPLSSQ*SDR*LGNGIRGGFRILPFVEKSQLPFGLLRLYL*YFWSR
QVCRAPPCYHINPLALKTWLERLLFPRCSSWVGVHLWDHCRQRHLQRWPFLYRNDGICRS
HLPFPLSSQ*SDR*LGNGIRGGFRILPFVEKSQLPFGLLRLYL*YFWSRQVCRAPPC*PA
GMQAC*PAVQRDPVVPLSRDNEHCMSKL*KITTYFFCHTCLKCSLSIFIHIFKLYSTNNI
IYSTTIISVF*RII*MNS*TWSKGQLSILTTGLYSFIFLVCMCSPFFLQIASPI*YFIHF
ISTSI*GLGLMVFID*FF*YIYFILF*PLN*EN*NSILVFLFNNLDIK*NKIK*LKIKQI
PFKKLKKLRKHFSCFE*IMPAC*TPSIDESNGHQPANQQRRVGPSEADGTASLSLPLDPS
REFRSTVGLAPLSASRNCVAERQT*AGTAGGLLLLSRHRQLRGIPFPPLLRFPFLARRNK
*TPPPHPLSPTSCCSERTHTQPDLPQIHPSAPPLQGTPLVLPPPPSLPSLDRRSGPWLGP
GSSTSVHVCVRSVFVLDPCC*RSYTDATCTSDTF*LLTCQCFSLGNPGMALAVPQTGSI*
DRYTC*CGFY*CIYMMAYAASIHML*P*VPIYYNKQVCFIIILILIYLDDGICSSYMWIF
LALPSYAIYLLGTVSFVDAHPVVWCYFCRGSELMEINNQNQCVPYNCLSNPKEIILGEER
LETGNTVADISLGLINFLYSNFVPGGGFIVGLLELIWGFIGPSQWDIFLAQIEQLISQRI
EEFARNQAISRLEGLSNLYKVYVRAFSDWEKDPTNPALREEMRIQFNDMNSALITAIPLF
RVQNYEVALLSVYVQAANLHLSILRDVSVFGERWGYDTATINNRYSDLTSLIHVYTNHCV
DTYNQGLRRLEGRFLSDWIVYNRFRRQLTISVLDIVAFFPNYDIRTYPIQTATQLTREVY
LDLPFINENLSPAASYPTFSAAESAIIRSPHLVDFLNSFTIYTDSLARYAYWGGHLVNSF
RTGTTTNLIRSPLYGREGNTERPVTITASPSVPIFRTLSYITGLDNSNPVAGIEGVEFQN
TISRSIYRKSGPIDSFSELPPQDASVSPAIGYSHRLCHATFLERISGPRIAGTVFSWTHR
SASPTNEVSPSRITQIPWVKAHTLASGASVIKGPGFTGGDILTRNSMGELGTLRVTFTGR
LPQSYYIRFRYASVANRSGTFRYSQPPSYGISFPKTMDAGEPLTSRSFAHTTLFTPITFS
RAQEEFDLYIQSGVYIDRIEFIPVTATFEAEYDLERAQKVVNALFTSTNQLGLKTDVT*V
DGSDRSNIWQ*SFLRLNPVAGLAMIII*FLLNYVKHVIINM*CMTLFMRWVFMIRVPQLY
I*YAIENKI*RAN*DKLSRAVSSMLLDRLTNS*SCHSCFLCEIVIRSQFHTTYEPEA*SV
KPGVPNE*ANSH*LRCAHCPLSSRETCRASCINESANARGEAVCVLELELGSDCRFPPSV
*TLAFVE*IPSLLQHKASPGAFTLSLCF*TPYHLN*CIR**
Again, there is 100% sequence identity to the SEQ ID NO:28 taught by BAUM (region shown in bold lettering).
Accordingly, even though BAUM does not explicitly teach the short instantly recited short junction sequences of instant SEQ NOs:4-5, or the long construct sequence of instant SEQ ID NO:8, these sequences follow from the teachings of BAUM, and from the finite number of choices, as described above. There is nothing unexpected about these claimed sequences. Similar reasoning applies to the resultant deposited maize seed (PTA-126224) that comprises the truncated modified Cry1Da protein.
Bioinformatic analysis, recombinant DNA technology, DNA sequencing, site-directed mutagenesis, DNA and protein engineering and synthesis, plant culture, morphological, biochemical, and physiological assays, and analysis of resistance to Lepidopteran pests are techniques that were routine in the art at the time the application was filed, as taught by the cited references and the state of the art in general.
Response to Applicants’ arguments:
The Applicants’ arguments in the response submitted on October 6, 2025 have been carefully considered but they were not found to be persuasive. The Applicants refer to the declarations of Drs. Camilo and Hjelle in support of patentability of the claims (Remarks, page 2). Referencing case law, Applicants contend that BAUM does not teach or suggest the nucleic acid molecule of the present claims (Id.). Applicants argue that the proper question in the obviousness analysis is whether one of ordinary skill in the art would have had a reasonable expectation of success based on the teachings of BAUM, to successfully produce a sequence that is unique to Event ME240913 (Id, page 3). Applicants argue that the disclosure of BAUM would have discouraged one of ordinary skill in the art from taking Cry1Da1 as a starting point for producing a commercially useful pest resistant plant (Id., pages 3-4). Applicants argue that BAUM provides no motivation to produce a truncated Cry1DA1 protein (of instant SEQ ID NO:3) (Id., page 4). Applicants argue that BAUM even teaches away from the nucleic acid molecule of the present claims (Id., page 5). Applicants argue that Event ME240913 produces unexpectedly superior toxicity (Id., page 6).
The Examiner disagrees with Applicants’ characterization of the prior art, and of the state of the art in general, vis-à-vis the instant claims.
The main issue in the present obviousness analysis is whether there was any reason based on prior art teachings that would have motivated one of ordinary skill in the art to use and to modify the teachings of BAUM for the engineering of Cry1Da protein toxin amino acid sequences that exhibit improved Lepidopteran insecticidal activity, polynucleotide sequences intended for use in expression of the improved proteins, as well as recombinant plants, plant parts, and seeds containing polynucleotide constructs encoding one or more of the improved engineered proteins. The answer to this question is obviously yes. It is in this context that the BAUM reference precisely teaches, suggests, and provides motivation for the instantly claimed compositions and methods.
For example, BAUM specifically teaches that “[f]ragments of the engineered insecticidal proteins described herein can be truncated forms wherein one or more amino acids are deleted from the N-terminal end, C-terminal end, the middle of the protein, or combinations thereof without a loss of insect inhibitory activity. These fragments should retain the insect inhibitory activity of the parent engineered insecticidal protein.” (paragraph 0080; emphasis supplied). Indeed, the instantly claimed SEQ ID NO:3 is precisely that, a truncated Cry1Da protein. See also BAUM’s Table 1, describing characteristics of TIC844, Cry1Da1, and the 40+ engineered insecticidal proteins. These vary in length from 1069 to 1165 amino acids.
As described above, even though BAUM does not explicitly teach the short instant junction sequences of instant SEQ NOs:4-5, or the long construct sequence of instant SEQ ID NO:8, these sequences follow – as obvious variants – from the teachings of BAUM. Instant SEQ ID NO:4 is only the 24-bp-long 5’ junction nucleotide sequence. Instant SEQ ID NO:5 is only the 34-bp-long 3’ junction nucleotide sequence. As BAUM extensively describes, the CrylDal protein is a Lepidopteran-active protein that was first described in 1990, i.e., decades ago. It has been very well studied. At the time of filing the instant application, a person of ordinary skill in the art would easily test the finite number of possibilities for mutations and truncations in the Cry1Da1 protein, thus arriving at the results of the instant patent application with a reasonable expectation of success.
Regarding alleged unexpected results, in contrast to Applicants’ arguments, BAUM explicitly teaches that “[w]hile the scaffold proteins TIC844 (SEQ ID NO:14) and CrylDal (SEQ ID NO:2) display low toxicity to H. zea, the engineered insecticidal proteins of the present invention exhibit surprising and unexpectedly improved insecticidal activity and an enhanced insecticidal spectrum against Lepidopteran insect pests including H. zea” (0008; emphasis supplied).
Applicants are also reminded that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In this case, one of ordinary skilled in the art would have arrived at the Applicants’ invention by modifying the teachings of the cited art as discussed above.
Summary
No claim is allowed.
Examiner’s Contact Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to BRATISLAV STANKOVIC whose telephone number is (571)270-0305. The examiner can normally be reached Monday-Friday, 08:00-17:00 h EST.
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BRATISLAV STANKOVIC, JD, PhD
Supervisory Patent Examiner
Art Units 1661 & 1662
/BRATISLAV STANKOVIC/SPE, Art Units 1661 & 1662
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