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 .
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.
Status of Claims
Claims 1-20 are pending and under examination.
Claim Objections
Claims, 5, 8 and 17 are objected to because of the following informalities:
Claims 5 and 17 recite a sequence without an identifier. These claims must be accompanied with a SEQ ID NO. In this case, the sequence needs to be accompanied with the phrase SEQ ID NO: 15.
Claim 8 recites “Table 1 Sequence ID Listing No. 5” should be – SEQ ID NO: 5 – because incorporation by reference is a necessity doctrine, not for applicant’s convenience. In this case, the phrase Table 1 may be viewed as incorporation by reference. Meanwhile, by reciting SEQ ID NO: 5 would capture the meaning without incorporation by reference. Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-20 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 1, 9, and 18 contain the trademark/trade names of mNeonGreen and NanoLuc. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade names are used to identify/describe proteins and, accordingly, the identification/description is indefinite. Claims 2-8, 10-17, 19-20 are rejected as being dependent from claims 1, 9 and 18.
Claims 1, 9, and 18 further recite the limitation of “x repeats of an N-terminal autocleavage peptide sequence of Mpro” is unclear to what is the structure that it represents. Does the phrase “x repeats” represent a single amino acid or a sequence? Additionally, the claim is unclear to the phrase “repeats”. Meanwhile, claims 5 and 17 do not represent repeating amino acid residues nor repeating peptides. Also, claim 2 recites two, which indicates that there is no repeat for x. Thus, the phrase “repeat” is unclear to the structural limitation imposed by the phrase x repeats to be auto cleaved by Mpro. Therefore, the dependent claims are also unclear for the same reasons stated above.
Claims 10 and 13 recite the limitations of “NB2D10” and “NB2E3” are unclear to what is the meaning of these abbreviations with respect to the structure of the nanobodies. These identifications do not represent any structural meaning to the nanobodies as claimed. Thus, it is unclear to the structures that represent these numbers. Meanwhile, numbers can be changed. Thus, to clearly represent the structures of the nanobodies, sequences are required. Claims 11-12 and 14-15 are rejected as being dependent on claims 10 and 13.
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 10-15 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.
As stated above, the recitations of “NB2D10” and “NB2E3” do not provide additional structural limitations to claim 9. Therefore, claims 10 and 13 do not further limit the scope of the first nanobody and second nanobody.
Additionally, claims 11-12 and 14-15 recite “C-terminal fusion” and “N-terminal fusion” are intended use but have not identified structural differences from the first nanobody and second nanobody. Therefore, these claims do not further limit the scope of the first nanobody and second nanobody.
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 § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-4, 6, 18 and 20 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Hamer et al. (“Bright Bioluminescent BRET Sensor Proteins for Measuring Intracellular Caspase Activity”, ACS Sens. 2017, vol. 2, pgs. 729-734, published 05/31/2017).
Hamer teaches FRET-based caspase activity probes have become important tools to monitor apoptotic cell signaling and development of three caspase sensor proteins based on BRET that retain the advantages of genetically encoded, ratiometric optical probes but do not require external illumination and the sensors consist of the bright and stable luciferase NanoLuc and the fluorescent protein mNeonGreen, fused together via a linker containing a recognition site (see abstract). Fig. 1 shows an mNeonGreen reporter protein, a NanoLuc reporter protein and x repeats of an N-terminal autocleavage peptide sequence of Mpro. Hamer teaches a 17-amino-acid linker containing a tetrapeptide caspase recognition site was chosen to allow easy access (at pg. 730, left col., bottom of para. 3). Note that the limitation of a 17-amino-acid linker containing a tetrapeptide caspase recognition site would read on the structure of x repeat peptide sequence.
With respect to claims 2-4 and 6, Hamer teaches a 17-amino-acid linker containing a tetrapeptide caspase recognition site was chosen to allow easy access (at pg. 730, left col., bottom of para. 3), which would read on the structure of x repeat peptide sequence of 2-12. Note that the recitation of “x repeat” is unclear as stated above.
With respect to claim 18, Fig. 1 shows the process of that placed a peptide sequence between mNeonGreen and NanoLuc.
With respect to claim 20, Hamer teaches a 17-amino-acid linker containing a tetrapeptide caspase recognition site was chosen to allow easy access (at pg. 730, left col., bottom of para. 3), which would read on comprising a structure of x repeat peptide sequence of 2.
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Claims 1-4, 6, 9-16, 18 and 20 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Cao et al. (“Nanobody-based sandwich reporter system for living cell sensing influenza A virus infection”, Scientific Reports, (2019), vol. 9:15899, pgs. 1-7, published 11/04/2019), as evidenced by Manicassamy et al. (“Analysis of in vivo dynamics of influenza virus infection in mice using a GFP reporter virus”, PNAS, vol. 107, no. 5, pgs. 11531-11536, published 06/22/2010).
With respect to claims 1, 9, and 18, Cao teaches a novel influenzaA nucleoprotein (NP) dependent reporter gene transcription activation module using NP-specific nanobodies and the results demonstrated that modular design allowed reporter genes (mNeonGreen fluorescent protein and Gaussia luciferase) specifically expressing to detect intracellular NP protein, and therefore acts as a universal biosensor to monitor infection of various influenza A subtypes in living cells (at abstract and Fig. 1). Cao teaches in order to utilize intracellular NP protein as a dimerizer scaffolding DBD and AD domains, DBD-VHH and V16AD-VHH fusion constructs with various NP nanobodies such as NP170 and NP54 (at pg. 2, para. 1 under Results). Fig. 3 shows NP170 with DBD-NP54 with mNeonGreen and Gaussia luciferase (Gluc) was selectively fused to the C-terminal of mNeonGreen with a 2Apeptide (at pg. 3, under para. 2). Cao further teaches that self-cleaving 2A peptide (at pg. 3, para. 2 and pg. 5, para. 1), which would read on the structure of “x”, as claimed.
With respect to claims 2-4 and 6, Cao teaches that in a single polyprotein via a self-cleaving 2A peptide, allowing functional NEP releasing (see pg. 5, para. 1). Meanwhile, the evidentiary teachings of Manicassamy indicate that 2A peptide has 19 amino acids (see Fig. 1), which would read on x is an autocleavage peptide sequence.
With respect to claim 10-15, Cao teaches in order to utilize intracellular NP protein as a dimerizer scaffolding DBD and AD domains, DBD-VHH and V16AD-VHH fusion constructs with various NP nanobodies such as NP170 and NP54 (at pg. 2, para. 1 under Results), which would read on the first nanobody and second nanobody. Meanwhile, NP170 and NP54 nanobodies would read on the structures of NB1D10, NB2E3, and capable of performing as C-terminal and N-terminal fusions.
With respect to claims 16 and 20, Cao teaches that in a single polyprotein via a self-cleaving 2A peptide, allowing functional NEP releasing (see pg. 5, para. 1). Meanwhile, the evidentiary teachings of Manicassamy indicate that 2A peptide has 19 amino acids (see Fig. 1), which would read on x is an autocleavage peptide sequence.
Claims 1-7, 18 and 20 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Geethakumari et al. (“A genetically encoded BRET-based SARS-CoV-2 Mpro protease activity sensor”. Communications Chemistry, (2022), vol. 5:117, pgs. 1-13, IDS submitted 06/21/2024, cite no. 41).
With respect to claims 1 and 5, Geethakumari teaches a pair of genetically encoded bioluminescence resonance energy transfer (BRET)-based sensors for detecting Mpro proteolytic activity in living cells as well as in vitro, and the sensors were generated by sandwiching peptides containing the Mpro N-terminal autocleavage sites, either AVLQSGFR (short) or KTSAVLQSGFRKME (long), in between the mNeonGreen and NanoLuc proteins (at abstract and Fig. 1). Fig. 1 shows the x repeats of an N-terminal autocleavage peptide sequence of Mpro are located between the mNG reporter protein and the NLuc reporter protein.
With respect to claims 2-4, Geethakumari teaches the sensors were generated by sandwiching peptides containing the Mpro N-terminal autocleavage sites, either AVLQSGFR (short) or KTSAVLQSGFRKME (long), which read on 2, 4, 8, 12 sites of an autocleavage peptide sequence. There are at least 12 amino acid sites in the peptide sequence.
With respect to claim 7, Geethakumari teaches Mpro recognizes a highly conserved core sequence with a critical Gln residue for cleavage (at pg. 2, left col., bottom of para. 1).
With respect to claim 18, Fig. 1 shows placing x repeats of an N-terminal autocleavage peptide sequence of Mpro between an mNeonGreen (mNG) reporter protein and a NanoLuc (NLuc) reporter protein.
With respect to claim 20, Geethakumari teaches the sensors were generated by sandwiching peptides containing the Mpro N-terminal autocleavage sites, either AVLQSGFR (short) or KTSAVLQSGFRKME (long), which read on 2 sites of an autocleavage peptide sequence.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 1-7 and 9-20 are rejected under 35 U.S.C. 103 as being unpatentable over Hamer et al. (“Bright Bioluminescent BRET Sensor Proteins for Measuring Intracellular Caspase Activity”, ACS Sens. 2017, vol. 2, pgs. 729-734, published 05/31/2017) in view of Mahdi et al. (“Analysis of the efficacy of HIV protease inhibitors against SARS‑CoV‑2′s main protease”, Virology Journal, vol. 17:190, pgs. 1-8, published 2020) and Sun et al. (“An extended conformation of SARS-CoV-2 main protease reveals allosteric targets”, PNAS, 2022, vol. 119, no. 15, e2120913119, pgs. 1-9, published 03/24/2022).
Hamer teaches FRET-based caspase activity probes have become important tools to monitor apoptotic cell signaling and development of three caspase sensor proteins based on BRET that retain the advantages of genetically encoded, ratiometric optical probes but do not require external illumination and the sensors consist of the bright and stable luciferase NanoLuc and the fluorescent protein mNeonGreen, fused together via a linker containing a recognition site (see abstract). Fig. 1 shows an mNeonGreen reporter protein, a NanoLuc reporter protein and x repeats of an N-terminal autocleavage peptide sequence of Mpro. Hamer teaches a 17-amino-acid linker containing a tetrapeptide caspase recognition site was chosen to allow easy access (at pg. 730, left col., bottom of para. 3).
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However, Hamer does not teach the autocleavage peptide sequence of Mpro comprises a peptide sequence AVLQSGFR (claims 5 and 17) and the biosensor comprising a first nanobody and a second nanobody (claims 9-17 and 19).
Mahdi teaches in-depth analysis of the efficacy of HIV Pls against the main protease of SARS-CoV-2 (Mpro) in cell culture and in vitro enzymatic assays (at abstract under methods). Mahdi teaches the sequence representing the N-terminal autoproteolytic cleavage site of SARS-CoV-2 Mpro is TSAVLQSGFRKM and a synthetic oligopeptide used in the in vitro enzymatic assay representing the N-terminal autoproteolytic cleavage site of SARS-CoV-2 Mpro is AVLQSGFR (at pg. 2, right col., under Materials and methods). Mahdi teaches to measure Mpro activity in cell culture experiments, GFP reporter substrate was adapted for SARS-CoV-2 Mpro and the recombinant substrate consists of an N-terminal GFP, followed by a natural proteolytic cleavage site of SARS-CoV-2 polyprotein, and a C-terminal hydrophobic tail and the proteolysis at the inserted cleavage site releases the tail that serves as a hydrophobic quencher of fluorescence and facilitates tetramerization of GFP (at pg. 4, left col., under Results and Fig. 1).
Sun teaches coronavirus main protease (Mpro) is required for viral replication and has enzymatical activity as a homodimer and Nanoluc binary technology (NanoBiT)-based high-throughput allosteric inhibitor assay based on the rearranged conformation and identified as set of allosteric inhibitory nanobodies against Mpro (at abstract). Sun teaches enzymatic activity and inhibition assay with the activity of SARS-CoV-2 Mpro was measured by a continuous kinetic assay with the substrate MCA-AVLQSGFR, a peptide similar to the N-terminal or C-terminal amino acid sequence of the nsp5 to nsp16 of SARS-CoV2 (at pg. 8, right col., under Enzymatic Activity and inhibition Assay). Sun teaches nanobodies (at Table 1 and Fig. 2, caption). Table 1 shows NB1D10 and NB2E3. Sun teaches the two nanobodies captured two distinct transient conformations of Mpro in the inactive monomer state (at pg. 7, right col., para. 1 of Conclusion).
It would have been obvious to the person of ordinary skill in the art before the effective filing date of the claimed invention to have used the method of BRET-based activity as taught by Hamer with the autoproteolytic cleavage peptide as taught by Mahdi and Sun for monitoring SARS-CoV-2 Mpro activity because Hamer teaches that its sensor consists of the bright and stable luciferase NanoLuc and a fluorescent protein mNeonGreen fused together by a cleavable linker for protease enzyme activity and Mahdi teaches the recombinant green fluorescent protein substrate conjugates to a natural proteolytic cleavage site (AVLQSGFR) for monitoring Mpro protease activity. Thus, it would have been obvious to have fused the NanoLuc and the mNeonGreen fluorescent protein with Mpro cleavable site because Hamer teaches that its sensor protein is based on BRET that retain the advantages of genetically encoded, ratiometric optical probes but do not require external illumination while providing a bright and stable reaction (at abstract and Fig. 1).
Additionally, it would have been obvious to have incorporated the use of nanobodies of Sun into the BRET sensor of Hamer because Sun teaches monitoring the activity of Mpro protease by the nanobodies capturing Mpro protease. Thus, it would have been obvious to have attached each NanoLuc and mNeonGreen to a nanobody for binding to Mpro protease after proteolytic activity.
The person would have a reasonable expectation of success in using proteolytic cleavage site AVLQSGFR with the BRET sensor because it has been well understood in the art to attach AVLQSGFR peptide to a fluorescent protein for protease activity, as taught by Mahdi. Additionally, it would have been obvious to have used nanobodies because nanobodies bind to a specific targets of the protease.
With respect to claims 2-4, 6, 16 and 20, as stated above, Hamer does not teach Mpro cleavage site. Mahdi teaches the sequence representing the N-terminal autoproteolytic cleavage site of SARS-CoV-2 Mpro is TSAVLQSGFRKM (at pg. 2, right col., under Materials and methods), which would read on 2-12 of x amino acids of peptide sequence.
With respect to claims 7-8, as stated above, Hamer does not teach Mpro cleavage site. Mahdi teaches the sequence representing the N-terminal autoproteolytic cleavage site of SARS-CoV-2 Mpro is AVLQSGFR (at pg. 2, right col., under Materials and methods), which would read on the claimed Gln (Q).
With respect to claims 10-15, as stated above, Hamer does not teach first nanobody and second nanobody. Sun teaches nanobodies (at Table 1 and Fig. 2, caption). Note Sun teaches in Table 1 NB1D10 and NB2E3 nanobodies, which would be capable of performing as a C-terminal fusion and N-terminal fusion.
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 1-7 and 9-20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-4, 7-11, and 14-15 of copending Application No. 18/562772 (‘772) in view of Hamer et al. (“Bright Bioluminescent BRET Sensor Proteins for Measuring Intracellular Caspase Activity”, ACS Sens. 2017, vol. 2, pgs. 729-734, published 05/31/2017) and Sun et al. (“An extended conformation of SARS-CoV-2 main protease reveals allosteric targets”, PNAS, 2022, vol. 119, no. 15, e2120913119, pgs. 1-9, published 03/24/2022).
Copending Application ‘772 recites a sensor comprising J1 connected by a linker to J2, wherein:the linker comprises EFGTENLYAVLQSGFRGSGGS (SEQ ID NO:3) or EFGTENLYKTSAVLQSGFRKMEGSGGS (SEQ ID NO:4);J1 comprises a bioluminescence donor protein; and J2 comprises a resonance energy acceptor protein, which would read on the x repeats of an N-terminal autocleavage peptide sequence of Mpro. However, the reference does not teach mNeonGreen reporter protein and NanoLuc reporter protein (claim 1) and first nanobody and second nanobody (claim 9).
Hamer and Sun have been discussed above. It would have been obvious to the person of ordinary skill in the art at the time of filing to have the sensor as recited in the copending Application ‘772 with mNeonGreen reporter protein and NanoLuc reporter protein because the copending Application recites bioluminescence donor protein and a resonance energy acceptor protein and Hamer teaches that its sensor consists of the bright and stable luciferase NanoLuc and a fluorescent protein mNeonGreen fused together by a cleavable linker for protease enzyme activity Thus, it would have been obvious to have fused the NanoLuc and the mNeonGreen fluorescent protein with Mpro cleavable site because Hamer teaches that its sensor protein is based on BRET that retain the advantages of genetically encoded, ratiometric optical probes but do not require external illumination while providing a bright and stable reaction (at abstract and Fig. 1).
Additionally, it would have been obvious to have incorporated the use of nanobodies of Sun into the BRET sensor because Sun teaches monitoring the activity of Mpro protease by the nanobodies capturing Mpro protease. Thus, it would have been obvious to have attached each NanoLuc and mNeonGreen to a nanobody for binding to Mpro protease after proteolytic activity.
The person would have a reasonable expectation of success in using proteolytic cleavage site AVLQSGFR with the BRET sensor of Hamer because it has been well understood in the art to attach AVLQSGFR peptide to bioluminescence donor protein and a resonance energy acceptor protein for protease activity. Additionally, it would have been obvious to have used nanobodies because nanobodies bind to a specific target of the protease.
This is a provisional nonstatutory double patenting rejection.
Allowable Subject Matter
Claim 8 would be allowable if rewritten to overcome the objection and the rejection(s) under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), 2nd paragraph, set forth in this Office action and to include all of the limitations of the base claim and any intervening claims.
The closest prior art references of record are Hamer and Geethakumari (see above). However, the references fail to teach or reasonably suggest SEQ ID NO: 5.
Conclusion
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
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