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 .
This is a Final Office Action in response to amendment filed on June 17, 2026.
Claims 1, 2, 8, 11, 12, 20, and 22 have been amended. Claims 1-2, 6-9, 11-17, 20-23, 32, and 34-35 remain pending and are examined herein.
Response to Amendment
Rejection of Claims 8, 11, 12, 22 under 35 U.S.C. 112(b) is withdrawn in view of amendment to the claims.
Claim Rejections - 35 USC § 112
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 11-12 are newly 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.
Claim 11 recites “wherein the methionine in position 1, the alanine in position 2, …., separately, are either present or absent, and when present are each separately and respectively, methionine, alanine, …… substituted with any other amino acid linker of the same or different length and amino acid composition.”
Claim 12 recites “wherein the methionine in position 1, the alanine in position 2, …., separately, are either present or absent, and when present are each separately and respectively, methionine, alanine, …… substituted with any other amino acid linker of the same or different length and amino acid composition.”
These claims are indefinite because it is not clear whether, for example, Met at position is required to be present or not. If it were present it is required to be substituted to something else then it no longer is present. The metes and bounds are not clear.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 20-23 are newly rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The claims are broadly drawn to recombinant microbial cell engineered to be capable of expressing a non-native transcription factor that activates a non-native promoter in response to an organophosphate degradation product; wherein the non-native promoter expresses a reporter protein which is a component of an extracellular electron transfer (EET) system.
The claims are broad in scope, in for example, the genus of a reporter protein which is a component of an extracellular electron transfer (EET) system. Applicant has not provided an adequate description for the broad genus in the context of required function of sensing organophosphate degradation product.
The component of an extracellular electron transfer (EET) system is a broad and diverse genus. For example, Carducci teaches that electrons can be transferred either through a direct contact interface between the biological cell and electrode, known as direct extracellular electron transfer (DEET), or transferred using a redox mediator, known as mediated extracellular electron transfer (MEET) (p. 170).(Carducci, N.G.G., Dey, S., Hickey, D.P. (2023). Recent Developments and Applications of Microbial Electrochemical Biosensors. In: Lisdat, F., Plumeré, N. (eds) Trends in Biosensing Research. Advances in Biochemical Engineering/Biotechnology, vol 187. Springer, Cham.)
In contrast to the broad scope of the claims, Applicant has only provided description for p-NP induced expression of CymA in engineered S. oneidensis.
Applicant has not described any other EET systems or components commensurate to the full scope of the claims. The CymA in engineered S. oneidensis is not sufficient to represent the entire genus of the components of EET systems.
The state of art has not adequately taught the structure-function relationship of the components of EET systems. For example, Carducci teaches that the mechanisms underpinning microbial electron transfer have only just started to be understood. Furthermore, some aspects are the subject of considerable debate. Such deficiency is not remedied by the instant disclosure.
Therefore, it is not clear that Applicant was in possession of the claimed genus at the time this application was filed.
Claim Rejections - 35 USC § 102
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 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.
Due to Applicant’s amendment of the claims, the rejection is modified from the rejection as set forth in the previous Office Action. Applicant’s arguments have been fully considered but they are not persuasive.
Claims 1-2, 6-7, 9, 13-15, 32, and 34-35 remain rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Feng (CN 108486024 A, published on 2018-09-04).
Claim 1 is drawn to a recombinant microbial cell displaying on its surface a non-native protein capable of degrading an organophosphate, wherein the recombinant microbial cell is incapable of replication and provides an inert scaffold for displaying an active enzyme.
Regarding claim 1, Feng discloses recombinant Escherichia coli (bacterium) cells expressing an “OPH signal sensing module” which comprises an INPNC-OPH fusion protein for expressing on the cell surface (Section 2.1, e.g). OPH is organophosphate hydrolase (OPH), an efficient organic phosphorus degrading enzyme (Section “background technology”). Feng discloses the OPH-containing gene engineered bacteria lyophilized on the filter paper under sterile condition (Claim 9, e.g.). As understood by skilled artisan and defined by the instant Application (e.g., instant claim 2), lyophilization (or drying) is an effective means to inhibit bacterial replication. Therefore, instant claim 1 is anticipate by Feng.
Regarding claim 2, Feng discloses lyophilization. See above.
Regarding claims 6-7, Feng discloses the enzyme being OPH, a phosphate hydrolase (see above).
Regarding claim 9, Feng discloses the enzyme OPH linked to the signal peptide INPNC for expression in the cell surface (see above).
Regarding claim 13, Feng discloses controlling the expression of the OPH gene with a promoter, such as inducible tac promoter (Section 2.1, e.g.).
Regarding claims 14-15, Feng discloses the bacterium as E. coli (see above).
Regarding claim 32, Feng discloses the system (kit) “sensor-based system based on flora” comprising both modules described above in Sections 2.1 and 2.2, which reads on claim 32.
Regarding claim 34, Feng discloses the step of contacting the engineered E. coli containing the OPH protein with organophosphate compounds (Ops) such as paraoxon ethyl, ethyl parathion, etc., and the degradation of the Ops (Section 4, for example); or paraoxon ethyl from soil or apple samples (Experiment 4, e.g.).
Furthermore, regarding claim 35, Feng discloses the method of using the system comprising both modules, contacting with Ops and detecting the resulted blue signal. See relevant parts cited above, or additionally in Claims 1-9; Sections 2-4; and Experiment 4, or 5, and so on.
Response to Applicant’s Remarks:
Applicant argued that the amendment to the claims, introducing the limitation “wherein the recombinant microbial cell is incapable of replication and provides an inert scaffold for displaying an active enzyme” overcomes the rejection above.
This argument has been fully considered but not deemed persuasive.
Applicant asserted that “inventors thus deliberately rendered the degrader cell permanently non-viable” (Remarks, p. 9; emphasis added). However, the Specification does not support such assertion.
The Specification, at p. 28, under Section “Preparation of Lyophilized E. coli”, states: “After the final wash, cells were diluted in the same defined media with 100 mM trehalose as a cryoprotectant to a final OD600 of 0.1 or 2.0, depending upon the use. The defined media for resuspension was phosphate citrate buffer (pH 8.0) for colorimetric assays, phosphate buffered saline (pH 7.4) for fluorescence assays and MI minimal media (pH 7.0) for electrochemical measurements. 1 mL aliquots of the cell culture at specific OD600 were flash frozen with liquid N2, lyophilized under vacuum and stored at −20° C.”
Such conditions, especially with 100 mM trehalose as a cryoprotectant, does not render the lyophilized E. coli cells nonviable. Although Applicant claimed that such a treatment would bypass the need for maintaining viability, there is no evidence that the cells thus treated are actually nonviable.
On the other hand, both the instantly claimed method and the prior art method of Feng, requires the engineered E. coli to be lyophilized. Feng is silent regarding whether the viability is required while there is no evidence from the instant disclosure that the lyophilized E. coli cells are non-viable. Therefore, there is no evidence that the prior art does not teach an embodiment encompassed by the instantly claimed method.
Applicant further argued that Feng's assay design is structurally incompatible with the "inert scaffold" concept of amended claim 1 by citing Feng at para. 77.
This argument has been fully considered but not deemed persuasive.
Applicant failed to understand, that following the cited para. 77, the prior art disclosed preparing testing filter paper strip by spotting the (co-cultured) cell suspensions on Whatman filter paper strips which was then dried in a laminar air oven for 10 minutes, followed by vacuum drying at 20° C. in a lyophilizer. Thus, Feng discloses a method of preparing the engineered bacterial cells in a state that is inert—being dried on filter paper.
Applicant further argued that the specification confirms that the "inert scaffold" feature is the inventive design that distinguishes from the prior art. This argument has not been found persuasive, for the reasons stated above—that 1) the prior art teaches the engineered bacterial cells dried on filter paper, which is in an inert state; and 2) there is no evidence from the instant disclosure that the microbial cells treated in the instantly disclosed method would be completely non-viable.
Applicant argued that sodium azide treatment, an alternative recited in claim 2, is entirely absent from Feng. Applicant is reminded that sodium azide treatment, is an alternative.
Applicant argued again that Feng lyophilizes bacteria for a filter paper strip does not constitute an anticipating disclosure of a cell treated to render it incapable of replication. This argument has not been found persuasive for reasons already discussed above. Furthermore, Applicant has not provided any evidence that 1) the instantly disclosed method does indeed render the lyophilized cells non-viable and/or 2) the cells treated with Feng method would be viable. As such, there is no evidence showing the prior art method being not equivalent or anticipatory of the instantly claimed method.
For these reasons, the rejection is maintained.
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.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Due to Applicant’s amendment of the claims, the rejection is modified from the rejection as set forth in the previous Office Action. Applicant’s arguments have been fully considered but they are not persuasive.
Claims 8, 16, 17, remain rejected under 35 U.S.C. 103 as being unpatentable over Feng Feng (CN 108486024 A, 2018-09-04), in view of Tang (Tang, Xiangjiang, et al. "Cell surface display of organophosphorus hydrolase for sensitive spectrophotometric detection of p-nitrophenol substituted organophosphates." Enzyme and Microbial Technology 55 (2014): 107-112) with evidence from Genbank sequence P0A434.1 (sumitted by Applicant in IDS of 12/31/2024).
Claim 8 is drawn to the recombinant microbial cell of claim 1, wherein the protein comprises an amino acid sequence at least 75% identical to SEQ ID NO:1 or 3-5. Since the Met residue is allowed to be either absent or present, its presence or absence from the prior art has no impact.
Claims 16-17 are drawn to the recombinant microbial cell of claim 1, wherein the cell is E. coli displaying an enzymatically active portion of parathion hydrolase from Pseudomonas diminuta on its surface; or wherein the cell displays an enzymatically active portion of the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2 on its surface.
Claim 1 and the teachings of Feng regarding the recombinant microbial cell of claim 1 are discussed above.
Although Feng teaches the E. coli cell surface displaying organophosphate hydrolase, including parathion hydrolase, Feng does not explicitly teach the amino acid sequence of the hydrolase, or specifically hydrolase with at least 75% identity with any of SEQ ID NO:1-5 or more specifically SEQ ID NO: 1 or 2.
Tang teaches cell surface display of organophosphorus hydrolase for sensitive spectrophotometric detection of p-nitrophenol substituted organophosphates (Title). Tang teaches organophosphorus hydrolase (EC 3.1.8.1, OPH) which was initially isolated from Pseudomonas diminuta MG in 1980s by way of citing Serdar (Bio/technology 7.11 (1989): 1151-1155) which has cloned Parathion hydrolase gene from Pseudomonas diminuta and also taught expression of the mature portion of the enzyme in Escherichia coli. Tang teaches construction of INP–OPH fusion with the OPH-coding opd. The sequence of the OPH cloned as Parathion hydrolase gene from Pseudomonas diminuta by Sedar et al is 100% identical to the instant SEQ ID NO: 1. See sequence alignment below between the instant SEQ ID NO: 1 and the Genbank sequence P0A434.1 from Sedar. Note that regarding the instant SEQ ID NO: 2, the instant SEQ ID NO: 1 is the enzymatically active portion of SEQ ID NO: 2 (mature portion).
Therefore, it would have been prima facie obvious and within the scope of ordinary skill in the art at the time of filing of the instant application, to have utilized the Pseudomonas diminuta parathion hydrolase of sequence P0A434.1, which is 100% identical to the instant SEQ ID NO: 1 and the enzymatically active portion of SEQ ID NO: 2, in the detection method and apparatus of Feng, thereby arriving at the instantly claimed invention. It is also likely that Feng has used the same OPH or something highly similar. The ordinary skilled artisan with have been motivated to do so given the teachings of Feng regarding the detection for toxic compounds such as parathion, and Tang’s teaching that OPH can catalyze the hydrolysis reaction of p-nitrophenol (PNP) substituted organophosphorus compounds (OPs) such as paraoxon, parathion, and the cell surface display of the OPH in recombinant E. coli cell for the sensitive detection system, as well as Feng’s optimization with the two-part system. The artisan would have reasonable expectation of success given the teachings and success of both Feng and Tang.
The claimed invention as a whole is prima facie obvious in view of the combined teachings of the prior art.
Alignment of instant Seq ID NO: 1 with Sequence P0A434.1
Score:734 bits(1895), Expect:0.0,
Method:Compositional matrix adjust.,
Identities:364/364(100%), Positives:364/364(100%), Gaps:0/364(0%)
Query 1 QTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICGS 60
QTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICGS
Sbjct 2 QTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICGS 61
Query 61 SAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAAD 120
SAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAAD
Sbjct 62 SAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAAD 121
Query 121 VHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQE 180
VHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQE
Sbjct 122 VHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQE 181
Query 181 LVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLT 240
LVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLT
Sbjct 182 LVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLT 241
Query 241 ALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSND 300
ALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSND
Sbjct 242 ALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSND 301
Query 301 WLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSPT 360
WLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSPT
Sbjct 302 WLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSPT 361
Query 361 LRAS 364
LRAS
Sbjct 362 LRAS 365
Claim 11-12 are rejected under 35 U.S.C. 103 as being unpatentable over Feng (CN 108486024 A, 2018-09-04), as discussed above, and further in view of Cha (US9051586B2, 2015).
Claim 11 is drawn to the recombinant microbial cell of claim 9, wherein the domain comprises an amino acid sequence at least 75%, identical to the amino acid sequence of SEQ ID NO: 6 or 7 wherein for SEO ID NO:6, the methionine in position 1, the alanine in position 2, the arginine in position 180, and the serine in position 181, separately, are either present or absent and when present are each separately and respectively, methionine, alanine, arginine, or serine, or, each separately and respectively, methionine, alanine, arginine, or serine substituted with any other amino acid linker of the same or different length and amino acid composition.
Claim 12 is drawn to the recombinant microbial cell of claim 1, wherein the protein comprises an amino acid sequence at least 75% identical to SEQ ID NO:2;
wherein the methionine in position 1, the alanine in position 2, the arginine in position 180, the serine in position 181, the serine in position 230, the serine in position 231, the residues in positions 232-241, the leucine in position 242, the glycine in position 243, the alanine in position 244, the serine in position 245, the glycine in position 246, the serine in position 247, and the glycine in position 248, separately, are either present or absent, and when present are each separately and respectively, methionine, alanine, arginine, serine, serine, serine, residue in position 232-241, leucine, glycine, alanine, serine, glycine, serine, or glycine, or, each separately and respectively, methionine, alanine, arginine, serine, serine, serine, residue in position 232-241, leucine, glycine, alanine, serine, glycine, serine, or glycine substituted with any other amino acid linker of the same or different length and amino acid composition.
Claims 11 and 12 are interpreted based on “substituted with….. amino acid of the same length and amino acid composition”—i.e., substituted with the same aa at the same position.
Claim 1 and 9 and the teachings of Feng regarding the recombinant microbial cell of claims 1 and 9 are discussed above.
While Feng teaches using the ice-nucleation protein signal peptide for the surface display of the OPH protein, Feng does not explicitly teach the sequence of the INP peptide.
Cha teaches expressing a recombinant enzyme in the Escherichia coli cell surface by fusing an ice nucleation protein sequence as a surface anchoring motif for secretion, and the ice nucleation protein having the sequence of SEQ ID NO: 5 The prior art INP signal peptide is 100% identical with the instant SEQ ID NO: 6 (See sequence alignment below).
Therefore, it would have been prima facie obvious and within the scope of ordinary skill in the art at the time of filing of the instant application, to have utilized the INP of Cha, which is 100% identical to the instant SEQ ID NO: 6, in the detection method and apparatus of Feng as the required INP, thereby arriving at the instantly claimed invention. The ordinary skilled artisan with have been motivated to do so given the teachings of Feng regarding the detection for toxic compounds such as parathion by surface displaying OPH enzymes via INP peptide, and Cha’s teaching of successful cell surface display in recombinant E. coli cell. The artisan would have reasonable expectation of success given the teachings and success of both Feng and Cha.
The claimed invention as a whole is prima facie obvious in view of the combined teachings of the prior art.
RESULT 1
US-13-817-468A-5
Sequence 5, US/13817468A
Patent No. 9051586
GENERAL INFORMATION
APPLICANT: POSTECH ACADEMY-INDUSTRY FOUNDATION
TITLE OF INVENTION: Method for converting and producing carbonate minerals from
TITLE OF INVENTION: carbon dioxide using recombinant biocatalyst
FILE REFERENCE: LPP20124765US
CURRENT APPLICATION NUMBER: US/13/817,468A
CURRENT FILING DATE: 2013-02-18
PRIOR APPLICATION NUMBER: PCT/KR2012/002816
PRIOR FILING DATE: 2012-04-13
PRIOR APPLICATION NUMBER: KR10-2012-0023429
PRIOR FILING DATE: 2012-03-07
PRIOR APPLICATION NUMBER: KR10-2011-0063729
PRIOR FILING DATE: 2011-06-29
NUMBER OF SEQ ID NOS: 25
SEQ ID NO 5
LENGTH: 462
TYPE: PRT
ORGANISM: Neisseria gonorrhoeae
FEATURE:
NAME/KEY: PEPTIDE
LOCATION: (1)..(462)
OTHER INFORMATION: carbonic anhydrase (cell surface expression)
Query Match 99.6%; Score 1188; Length 462;
Best Local Similarity 100.0%;
Matches 228; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MALDKALVLRTCANNMADHCGLIWPASGTVESRYWQSTRRHENGLVGLLWGAGTSAFLSV 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MALDKALVLRTCANNMADHCGLIWPASGTVESRYWQSTRRHENGLVGLLWGAGTSAFLSV 60
Qy 61 HADARWIVCEVAVADIISLEEPGMVKFPRAEVVHVGDRISASHFISARQADPASTSTSTS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 HADARWIVCEVAVADIISLEEPGMVKFPRAEVVHVGDRISASHFISARQADPASTSTSTS 120
Qy 121 TSTLTPMPTAIPTPMPAVASVTLPVAEQARHEVFDVASVSAAAAPVNTLPVTTPQNLQTR 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 TSTLTPMPTAIPTPMPAVASVTLPVAEQARHEVFDVASVSAAAAPVNTLPVTTPQNLQTR 180
Qy 181 SRLWDGKRYRQLVARTGENGVEADIPYYVNEDDDIVDKPDEDDDWIEV 228
||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 SRLWDGKRYRQLVARTGENGVEADIPYYVNEDDDIVDKPDEDDDWIEV 228
Response to Applicant’s Remarks:
Regarding claims 8, 12, 16-17, Applicant argued that “growing E. coli at OD600 = 1” is “entirely incompatible with the instant invention's inert-scaffold concept”; and that the prior art does not teach or suggest “co-culture with an EET-capable electroactive microbe,
EET-based detection”, …... This argument has not been deemed persuasive. Applicant is reminded that the argued limitations are not in the claims.
Applicant further argued “unexpected results”. Applicant is reminded that the alleged unexpected results should be commensurate to the scope of the claims.
At least for these reasons, the rejections are maintained.
Conclusion
No claims are 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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to WEIHUA FAN whose telephone number is (571)270-0398. The examiner can normally be reached Monday-Friday, 9-5.
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WEIHUA . FAN
Primary Examiner
Art Unit 1663
/WEIHUA FAN/Primary Examiner, Art Unit 1663
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