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 the Claims
Amendments dated 02/19/2026 are entered.
Claims 1, 3, 10, 13-15, 28-29, 31, 37, 43-44, 68, 72-73, 75-76, 81, 86-87, 92, and 103 are pending and are examined in this Office action.
Status of Objections and Rejections
All previous objections and rejections not set forth below have been withdrawn in view of Applicant’s amendments and/or upon consideration of Applicants’ arguments.
The text of those sections of Title 35 U.S. Code, not included in this action, can be found in a prior Office action.
Claim Rejections - 35 USC § 112(b)
Response to Applicants’ arguments:
Amendments made to the claims filed in Applicants’ response submitted on 19 February 2026 overcame the rejection of record.
Claim Rejections - 35 USC § 103
Claims 1, 3, 10, 13-15, 28-29, 31, 37, 43-44, 68, 72-73, 75-76, 81, 86-87, 92, and 103 remain rejected under 35 U.S.C. § 103 as being unpatentable over ROSBASH (Rosbash et al., United States Patent Application Publication No. 2019/0390186 A1, published December 26, 2019) in view of KEENE (Keene and Lager, United States Patent Application Publication No. 2017/0327866 A1, published November 16, 2017), DICKINSON (Dickinson et al., PCT International Patent Application Publication No. WO 2020/142676 A1, published 09 July 2020), and BONG (Choi Sang Bong et al., Korean Patent Application Publication No. KR 101394333 B1, published May 1, 2014; English machine translation); for reasons of record stated on pages 4-14 in the Office action dated 11/19/2025.
The claims are drawn to an expression construct for tethering a protein of interest to a target RNA molecule, which comprises a promoter operably linked to a nucleic acid sequence encoding an engineered protein, the engineered protein comprising an RNA-binding polypeptide comprising RNA recognition motifs (RRMs) A-B of a Bruno-like RNA-binding protein, wherein the RNA-binding polypeptide is fused to a protein or polypeptide of interest, wherein the nucleic acid sequence encoding the engineered protein comprises: a. a first nucleic acid sequence encoding the RNA-binding polypeptide and a second nucleic acid sequence encoding the protein or polypeptide of interest upstream or downstream of the first nucleic acid sequence; or b. a first nucleic acid sequence encoding the RNA-binding polypeptide, and a second nucleic acid sequence comprising a cloning sequence upstream or downstream of the first nucleic acid sequence, whereby a third nucleic acid sequence encoding the protein or polypeptide of interest cloned into the cloning sequence generates the nucleic acid sequence encoding the engineered protein; wherein an amino acid sequence comprising an RRM C of the Bruno-like RNA-binding protein is absent from the RNA-binding polypeptide and wherein the RNA-binding polypeptide recognizes and specifically binds an RNA sequence comprising one or more Bruno-like protein binding sites in the target RNA molecule to thereby tether the protein or polypeptide of interest to the target RNA molecule.
ROSBASH teaches compositions and methods for identifying RNA binding polypeptide targets, and teaches fusion polypeptides comprising an RNA binding polypeptide operationally linked to an RNA modifying enzyme ( e.g., adenosine deaminase, cytidine deaminase ), and methods of use therefore (entire document; see Title, Abstract, ¶0008, for example).
Regarding instant claim 1, ROSBASH teaches a vector containing a fusion polypeptide operably linked to a promoter positioned for expression in a cell (i.e., expression construct) (¶0015). The invention uses targets of RNA-binding proteins identified by editing system, a method that couples an RBP (RNA binding protein) to the catalytic domain of the RNA-editing enzyme and expresses the fusion polypeptide in vivo. RBP targets are marked with novel RNA editing events and identified by sequencing RNA. The system was used to identify the targets of three RBPs (¶0159).
ROSBASH teaches that the expression vector can include a native or nonnative promoter operably linked to the nucleotide sequence encoding the fusion polypeptide (including functional portions and functional variants thereof), or to the nucleotide sequence which is complementary to or which hybridizes to the nucleotide sequence encoding the fusion polypeptide (¶0055). By "fusion polypeptide" is meant a polypeptide or protein that combines at least two amino acid sequences that are not naturally contiguous (i.e., engineered protein comprising a RNA-binding polypeptide fused to a protein or polypeptide of interest; i.e., first, second, and third nucleic acid sequence encoding the engineered protein) (¶0058). The fusion polypeptide is preferably produced by standard recombinant DNA techniques. For example, a DNA molecule encoding the first polypeptide is ligated to another DNA molecule encoding the second polypeptide, and the resultant hybrid DNA molecule is expressed in a host cell to produce the fusion polypeptide (i.e., engineered protein comprising a RNA-binding polypeptide fused to a protein or polypeptide of interest; i.e., first, second, and third nucleic acid sequence encoding the engineered protein). The DNA molecules are ligated to each other in a 5' to 3' orientation such that, after ligation, the translational frame of the encoded polypeptides is not altered, e.g., the DNA molecules are ligated to each other in-frame (i.e., a first nucleic acid sequence encoding the RNA-binding polypeptide and a second nucleic acid sequence encoding the protein or polypeptide of interest upstream or downstream of the first nucleic add sequence) (¶0059).
ROSBASH teaches RNA recognition motifs (RRMs). For example, FIGS. 1A-1D show schematic representations of TRIBE, a fusion polypeptide of an RNA-binding polypeptide (RBP) and the catalytic domain of Adenosine Deaminases Acting on RNA (ADAR) that can edit target transcripts of the RNA-Binding Protein (¶0086). Fig.1C provides a schematic depicting how the dsRBDs of ADAR (i.e., RNA modifying enzyme) were replaced with the RBP of interest. The editing specificity of the fusion polypeptide was determined by the RNA recognition features of the RBP, and the target transcript was permanently marked by a novel editing event (¶¶0089, 0180).
ROSBASH also teaches mutations of RNA recognition motifs (i.e., an amino acid sequence comprising an RRM is absent from the RNA-binding polypeptide) (¶0236).
ROSBASAH teaches the use of various linkers, for example edited sites for Thor-ADAR and Thor-linker-ADAR fusion polypeptides (¶¶0150-0151).
ROSBASH further teachers tethering of the ADARcd to its targets by an RBP (¶0226)
ROSBASH does not explicitly teach an engineered protein comprising an RNA-binding polypeptide comprising RNA recognition motifs (RRMs) A-B of a Bruno-like RNA-binding protein. However, such claimed compositions and methods would have been prima facie obvious to a person of ordinary skill in the art at the time of filing the instant application for the following reasons.
KEENE teaches methods for in vivo identification of endogenous mRNA targets of microRNAs (entire document; see Title, Abstract, for example).
KEENE teaches the engineering of specific cell types in an animal with one or more cell - type specific gene promoters to express a RBP (RNA-binding protein) or RAP (RNA-associated protein) in the cell type of interest. The gene promoter and the RBP or RAP may be carried on one or more vectors and transformed into the cell, where the RBP or RAP is expressed (¶¶0052-0053).
KEENE teaches that the ligand used to carry out the invention is an RNA binding protein selected from the RNA Recognition Motif (RRM) family of cellular proteins involved in pre-messenger RNA processing. More than 200 members of the RRM superfamily have been reported, the majority of which are ubiquitously expressed and conserved in phylogeny. They include hnRNP proteins (A, B, C, D, E, F, G, H, I, K, L), RRM proteins CArG, DT-7, PTB, K1, K2, K3, HuD, HUC, rbp9, elF4B, sxl, tra-2, AUBF, AUF, 32KD protein, ASF/SF2, U2AF, SC35, and other hnRNP proteins.
KEENE specifically teaches that tissue-specific members of the RRM family include Bruno (¶0055).
KEENE further teaches that ncRNAS and miRNAs (or subsets and combinations thereof) identified by the methods of the invention, together with the RNABPs and corresponding mRNAs to which they bind or with which they are associated (or subsets thereof), are useful in providing confirming data, validating data, or training data to refine models and algorithms for identifying or generating hypothetical or proposed miRNAs from known corresponding mRNAs (¶0062).
DICKINSON teaches systems and methods for modulating RNA, and provides methods for modifying a target RNA of interest (entire document; see Title, Abstract, for example).
In Table 2, DICKINSON teaches a finite number of RNA regulatory domains from proteins that include Bruno-like RNA binding proteins, specifically BRUNOL4, BRUNOL5, and BRUNOL6.
DICKINSON teaches RNA recognition motifs (RRMs), and protein fusion to a nucleotide linker. To minimize endogenous effects of the inventors' fusion constructs, DICKINSON teaches only including the minimal RRM necessary for hairpin recognition in the system, and omitting regions of potential interactions with other proteins or nucleic acids. This keeps the required RNA hairpin as small as possible to avoid potential endogenous interactions, as the minimally required region necessary for binding to a hairpin, resulting in a gRNA with less than half the original hairpin length. This knowledge can be leveraged as the basis to engineer mutants that retain the highly charged nature required, but abolish endogenous functions, in order to engineer an orthogonal RNA targeting system (¶¶0072, 0234).
DICKINSON teaches that one or more proteins of the disclosure may be operably linked to another protein through linkage to a pair of accessory proteins that have a strong affinity for each other. Such accessory proteins are known in the art. For example, the Sun Tag is one such system that includes an antibody with a strong affinity for a peptide. One protein, polypeptide, or domain of the disclosure may be linked to a SunTag peptide and another protein, polypeptide, or domain of the disclosure may be linked to an antibody to allow operable linkage of the two proteins, polypeptides, or domains through the interaction of the Sun Tag peptide and antibody. Further examples include biotin and avidin/streptavidin and spytag and spycatcher (¶0021) (cf. instant claims 3, 10, 14). DICKINSON also teaches oligonucleotide analogs with modifications that improve binding affinity, and/or improve binding specificity (¶0122).
DICKINSON teaches an RNA targeting system that comprises (1) an RNA hairpin-binding protein that serves as the core of the system and is a selective, high affinity binder to a specific RNA structure displayed on an engineered gRNA, (2) a gRNA that features both the structure that interacts with the engineered hairpin-binding protein and a sequence with complementarity to the target RNA of interest, and (3) an effector protein, such as a nuclease or epitranscriptomic regulator, that acts on the targeted RNA in a proximity-dependent manner (¶0196).
DICKINSON teaches the engineering of a Cas13-inspired system that uses a defined protein-RNA interaction to display a gRNA sequence to deliver protein cargoes to a target RNA, similar to previous RNA tethering assays with overexpressed reporter constructs (¶0211).
DICKINSON teaches an RNA targeting system that comprises (1) an RNA hairpin-binding protein that serves as the core of the system and is a selective, high affinity binder to a specific RNA structure displayed on an engineered gRNA, (2) a gRNA that features both the structure that interacts with the engineered hairpin-binding protein and a sequence with complementarity to the target RNA of interest, (3) a charged protein that could bind to the displayed gRNA sequence non-specifically to stabilize and protect the guiding RNA prior to target engagement, and (4) an effector protein, such as a ribonuclease or epitranscriptomic regulator, that acts on the targeted RNA in a proximity-dependent manner (FIG. 12A). While Cas13 houses all of these functional components in a single protein domain, DICKINSON envisioned engineering a system that combines multiple protein domains that each perform one of these functions, which the inventors termed CRISPR/Cas-inspired RNA targeting system (CIRTS). CIRTS vary in their module composition and are uniquely numbered as listed in FIG. 12A and FIG. 21 (¶0212) (cf. instant claims 73, 75-76, 86-87).
DICKINSON teaches the use of a flag tag in the system, as SEQ ID NO:14 (see Table with sequences), and teaches the separate delivery of each gRNA along with CIRTS-0 fused to a 3x FLAG-tag (cf. instant claims15, 28, 37).
DICKINSON teaches the use of reporter proteins (¶0200) (cf. instant claim 44).
DICKINSON further teaches and claims (claim 93 of DICKINSON, for example) a kit comprising the taught and claimed systems (cf. instant claim 103).
BONG teaches the effects of AtBRN (Arabidopsis thaliana Bruno RNA-binding protein) in transgenic plants (entire document; see Title, Abstract, for example).
BONG teaches AtBRN1 (At4g03110) and AtBRN2 (At1g03457), previously reported as AtBRUL-1 or AtBRUI-2, which belong to the RNA binding protein-family with Bruno proteins. Bruno protein was first reported in Drosophila, an RNA-binding protein containing RNA-motif, which selectively splices in a variety of organisms, regulates mRNA translation inhibition and migration. Bruno protein binds to eIF4E, a synthesis initiator (Background section).
BONG teaches that, among the Bruno proteins present in Arabidopsis, AtBRN1 or AtBRN2 is an RNA binding protein having two RNA-bearing motif domains at the N-terminus and one RNA-recognizing motif domain at the C-terminus (Example One). Figure 1 shows the analysis of Bruno protein expression. (a) represents the protein structure ofAtBRN1 or AtBRN2, wherein each protein contains three RNA motifs (RRM) (DRAWING DESCRIPTION).
BONG further teaches that transcriptional regulation, including mRNA transport, stability and translation, plays an important role in plant growth and development, and most of these processes are directly or indirectly mediated by RNA binding proteins (RBPs). The KH- and RNA-sensing motif (RRM)-like RNA binding proteins are known to be involved in plant flowering. In the step of inhibiting translation of the target RNA, Bruno protein binds to eIF4E, a synthesis initiator, and inhibits formation of eIF4E-eIF4G complex, ultimately inhibiting 40S ribosomal formation. The Bruno protein functions as a Bruno-CUP-eIF4E complex, and Bruno genomic homologues of Arabidopsis are FCA, AtBRN1 and AtBRN2 (Background section).
Figure 1 of BONG depicts the protein structure of AtBRN1 or AtBRN2 (a), wherein each protein contains three RNA motifs (RRMs). It also depicts the genomic DNA structure and T-DNA insertion site (left) of the gene coding for AtBRN1 or AtBRN2, and atbrn1 / atbrn2-3 duplexes (d). See excerpts of Figure 1 below (cf. instant claims 72, 81, 92).
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The AtBRN2 protein taught by BONG is 72.6% (i.e., about 75%) similar to instant SEQ ID NO:33; see alignment below (cf. instant claim 10).
ALIGNMENT OF INSTANT SEQ ID NO:33 AND SEQ ID NO:4 FROM BONG
RESULT 24
BBH02698
ID BBH02698 standard; protein; 438 AA.
XX
AC BBH02698;
XX
DT 25-SEP-2014 (first entry)
XX
DE Arabidopsis thaliana Bruno RNA-binding protein 2 (AtBRN2), SEQ 4.
XX
KW BRN2 protein; Bruno RNA-binding protein 2; antigen; crop improvement;
KW flowering; plant; seed; transgenic plant.
XX
OS Arabidopsis thaliana.
XX
CC PN KR1394344-B1.
XX
CC PD 13-MAY-2014.
XX
CC PF 14-FEB-2013; 2013KR-00015905.
XX
PR 14-FEB-2013; 2013KR-00015905.
XX
CC PA (UYMY-) UNIV MYONGJI IND & ACAD COOP FOUND.
XX
CC PI Abbasi N, Bong CS, Sae KH;
XX
DR WPI; 2014-J95678/57.
DR N-PSDB; BBH02696.
XX
CC PT Controlling flowering time in plants, preferably dicotyledonous plants,
CC PT by isolating Arabidopsis thaliana Bruno RNA-binding protein from
CC PT Arabidopsis, introducing gene into vector, and transforming vector into
CC PT plant cell.
XX
CC PS Claim 2; SEQ ID NO 4; 20pp; Korean.
XX
CC The present invention relates to a novel method for controlling flowering
CC time in plants, preferably dicotyledonous plants. The method involves
CC isolating Arabidopsis thaliana Bruno RNA-binding protein (AtBRN) gene,
CC introducing the gene into a vector, and transforming the vector into a
CC plant cell. The invention further provides: (1) a method for producing a
CC transgenic plant for controlling flowering time of the plants; (2) a
CC method for regulating the flowering time in the transgenic plant; (3) a
CC seed of the transgenic plant; and (4) a composition for controlling
CC flowering time of the plants. The present sequence represents a
CC specifically claimed AtBRN2 protein (At1g03457), whose coding sequence is
CC used in the vector for preparing the transgenic plant of the invention
CC for controlling flowering time.
XX
SQ Sequence 438 AA;
Query Match 76.2%; Score 772.5; Length 438;
Best Local Similarity 72.6%;
Matches 151; Conservative 23; Mismatches 19; Indels 15; Gaps 2;
Qy 1 MAEAKEENREKNEEEESVKLFVGQIPKHMSESQLLTLFQEFAVVDEVNIIKDKITRASRG 60
||| | | || |||||||:||||:| ||||||:||::|:||||||:| ||| ||
Db 1 MAE------ETMENEERVKLFVGQVPKHMTEIQLLTLFREFSIVNEVNIIKEKTTRAPRG 54
Qy 61 CCFLLCPSREEADKLVNACHNKKTLPGANSLLQVKYADGELERL---------EHKLFVG 111
|||| ||:||:|||::|: |||||||||:| ||||||||||||| |||||||
Db 55 CCFLTCPTREDADKVINSFHNKKTLPGASSPLQVKYADGELERLDVLDCSCNPEHKLFVG 114
Qy 112 MLPKNVSEAEVQSLFSKYGTIKDLQILRGAQQTSKGCAFLKYETKEQAVSAMESINGKHK 171
|||||||| |||||||:||||||||||||: |||||| |||||:|||||:|||::||:|
Db 115 MLPKNVSETEVQSLFSEYGTIKDLQILRGSLQTSKGCLFLKYESKEQAVAAMEALNGRHI 174
Qy 172 MEGSTVPLVVKWADTERERHTRRLQKAQ 199
|||: |||:|||||||:|| ||| | |
Db 175 MEGANVPLIVKWADTEKERQARRLLKVQ 202
BONG teaches vectors constructed using the pRH5 'and pYESTrp3 vectors (Invitrogen) as hybrid RNA (MS2-SOC1) and fusion protein (VP16 AD-AD-AtBRNs) plasmids. The full-length SOC1 cDNA (1,293 bp, SEQ ID NO: 5) contained 5 'UTR and 3' UTR and was amplified by RT-PCR using primers 126F (SEQ ID NO: 18) and 126R (SEQ ID NO: 19) Cloning into Aat II and Sma I sites of pRH5 'vector resulted in pMS2-SOC1. PCR was performed using primers containing restriction enzyme sequences for cloning. PCR primers were 124F (SEQ ID NO: 20) and 124R (SEQ ID NO: 21) for AtBRN1, 125F (SEQ ID NO: 22) and 125R (SEQ ID NO: 23) for AtBRN2. The amplified DNA fragments to the AtBRN1 cut by treatment with restriction enzymes Eco R1 and Not I, to the AtBRN2 After a cloned into pYESTrp3 vector after cutting by treatment with restriction enzymes Hind III and Not I pVP16-AtBRN1 or pVP16-AtBRN2 (Plasmid structure section).
BONG teaches transforming plant cells with a recombinant vector comprising a gene encoding Arabidopsis thaliana Bruno RNA-binding protein (ATBRN) derived from Arabidopsis thaliana, and also teaches transgenic plants comprising double BRN1/BRN2 mutants (Description of Embodiments section).
In Example 3, BONG teaches the AtBRN1 or AtBRN2 overexpression of the gene SOC1 101-D to inhibit the extremely early flowering phenotype. This showed that AtBRN2 interacts with SOC1 mRNA in the plant body (cf. instant claim 68).
BONG specifically teaches the use of plant promoters and terminators. A "plant promoter" is a promoter capable of initiating transcription in plant cells, where constitutive promoters (i.e., UBQ10, ubiquitin) do not limit selectivity. BONG teaches that, in the plant expression vectors of the invention, conventional terminators can be used. Examples thereof include nopaline synthase (NOS), rice α-amylase RAmy1 A terminator, phaseoline terminator, Agrobacterium and the terminator of the Octopine gene of tumefaciens (i.e., OCS). Regarding the need for terminators, it is generally known that such regions increase the certainty and efficiency of transcription in plant cells. Therefore, the use of a terminator is highly desirable in the context of the invention (Description of Embodiments section) (cf. instant claims 37, 43).
Given the teachings of ROSBASH, DICKINSON, KEENE, and BONG as described above, it would have been prima facie obvious to a person of ordinary skill in the art at the time of filing the instant application to use and to modify the compositions and methods taught by ROSBASH, DICKINSON, KEENE, and BONG, and this would result in the Applicants’ invention; with a reasonable expectation of success, and without any surprising results. Obviously, one of ordinary skill in the art would have been motivated to do so for the purpose of identification of mRNA targets and RNA binding polypeptide targets, as taught by ROSBASH, DICKINSON, KEENE, and BONG.
Although ROSBASH, DICKINSON, KEENE, and BONG do not explicitly reduce to practice every single limitations of all of the instant claims (e.g., the full-length instantly claimed SEQ ID NOs: 3, 5, 18-19, 33, 38), these particular embodiments would be considered routine optimization and a design choice that would be readily apparent to one of ordinary skill in the art.1 The cited art teaches the instantly claimed inventive concept, and in general the recited elements of the instant claims. Thus the recited limitations (nucleic acid and amino acid sequences) would be desirable optimization(s) of the compositions and methods taught by the cited references, and merely a design choice that would be readily apparent to one of ordinary skill in the art, absent evidence to the contrary.
Response to Applicant’s arguments:
Applicants’ arguments filed February 19, 2026 have been carefully considered but they are not persuasive. Applicants argue that the claimed invention is not a mere substitution of one known RNA-binding protein into a known fusion system; rather, it is a functional re-engineering of a regulatory protein into a neutral tethering molecule. The inventors engineered a construct that uses two of the three Bruno RNA recognition motifs (i.e., RRMs A-B). This system circumvents unintended RNAi silencing in plants (Remarks, pages 8-9).
The Examiner disagrees with Applicant’s characterization of the cited prior art, and of the state of the art in general. The main issue in the present obviousness analysis is the concept of engineered proteins, constructs for expressing the engineered proteins, and methods of using the engineered proteins and constructs for tethering a protein of interest to an RNA molecule. It is in this context that the combined teachings of the cited references ROSBASH, DICKINSON, KEENE, and BONG precisely teach, suggest, and provide motivation for the instantly claimed compositions and methods. For example, in contrast to Applicants’ arguments, to minimize endogenous effects of the fusion constructs, DICKINSON teaches only including the minimal RRM necessary. As well, BONG teaches Bruno proteins present in Arabidopsis, as RNA binding proteins having two RNA-bearing motif domains at the N-terminus (i.e., RRMs A-B), and one RNA-recognizing motif domain at the C-terminus (i.e., RRM C). See excerpt below.
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Applicants are reminded that the test for obviousness is not whether the features of a secondary reference may be bodily incorporated into the structure of the primary reference; nor is it that the claimed invention must be expressly suggested in any one or all of the references. Rather, the test is what the combined teachings of the references would have suggested to those of ordinary skill in the art. In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981).
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).
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 combining the teachings of the cited art as discussed above.
Thus, Applicants’ argument is not found to be persuasive. For the reasons of record and those reasons indicated above, the rejection is maintained.
Summary
No claim is allowed.
THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicants are 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.
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BRATISLAV STANKOVIC, JD, PhD
Supervisory Patent Examiner
Art Units 1661 & 1662
/BRATISLAV STANKOVIC/SPE, Art Units 1661 & 1662
1 For example, instant SEQ ID NO:5 is only seven nucleotides long.
Prosecution Insights