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 .
Claim Status
The amended claim set filed 2 March 2026 is acknowledged. Claims 1 and 3-16 are currently pending. Of those, claims 1, 3-4, and 7-8 are currently amended, and claims 11-16 are new. Claim 2 is cancelled. Claims 1 and 3-16 will be examined on the merits herein.
Response to Arguments
The Applicants’ arguments filed 2 March 2026 are acknowledged. For clarity, in this action, said arguments will be referred to as “Remarks” and the Non-Final Office Action mailed 28 Nov 2025 will be referred to as “NFOA.”
Priority
This case claims priority to the foreign patent application JP2021-046808 (filed 22 March 2021) and is a continuation of PCT/JP2022/004680 (filed 7 Feb 2022). Receipt is acknowledged of the translation of the foreign patent application JP2021-046808. Applicant has perfected foreign priority. Therefore, the filing date that was used to search the art is 22 March 2021.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 9 Jan 2026 was filed in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered by the examiner. A signed copy of the statement is attached with this action.
Objection(s) and Rejection(s) Withdrawn
The rejection of claim 8 under 35 U.S.C. 112(b) (NFOA par. 5-6) is withdrawn in view of the claim amendment and applicant’s arguments.
The rejections of claims 1-10 under 35 U.S.C. 112(a) (NFOA enablement par. 7-17 and written description par. 18-25) are both withdrawn in view of the claim amendments and arguments. Specifically, the amendments reduced the breadth of the claims and the applicant’s arguments point out support for specific contemplated signal sequences and reduction to practice of a mutation in a signal sequence Example 1. Collectively, the arguments and amendments overcome the rejection of record.
The rejection of claims 1-3, 5-6, 9-10 under 35 U.S.C. 102(a)(1) as being anticipated by Caparon et al. (NFOA par. 26-27) is withdrawn in view of the claim amendments and arguments.
The rejection of claims 1-2, 4-5, 9-10 under 35 U.S.C. 102(a)(1) as being anticipated by Shin and Chen (NFOA par. 28-29) is withdrawn in view of the claim amendments and arguments.
The provisional double patenting rejection of claims 1-10 over copending Application No. 18/413,543 in view of Shin and Chen is withdrawn in view of the claim amendments and arguments.
Rejection(s) Maintained
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 § 102
Claims 1, 4-6, 8, and 10 remain rejected under 35 U.S.C. 102(a)(1) as being anticipated by Hak et al. (KR-20040036176-A; hereafter Hak; PTO-892 mailed 28 Nov 2025).
Hak teaches E. coli where the tolA gene (i.e. a gene associated with maintenance of the outer membrane structure) is removed from the genome (Example 3), and substituted with a TolA variant where the C-terminal region of TolA protein gene is substituted with a gene encoding a target protein (i. e. a target foreign protein, Abstract). This results in the cell having a modified tolA gene (see instant claim 1, 4), and where the modification is complete deletion of the genomic copy of the gene (see instant claim 5) and partial mutation of the gene (see instant claims 6, 8, the cell only encodes the N-terminal region of TolA).
Hak shows a specific example method (Example 6 part (2)) where the foreign protein used is a 6x His peptide fused to the TolA fragment (pg. 15). (a) “E. coli SOLR cells were transfected with ptEAST / TolAΔC-GST-6xHis vector” (pg. 15 par. 6), the cells were also infected with a mutant phage comprising a short-chain antibody phage library, which can also be considered genes encoding foreign proteins; (b) “E. coli colonies formed were seeded in 10 ml LB medium and further incubated at 37 ° C. for 12 hours” (pg. 16 par. 3); and (c) “The culture solution was centrifuged to obtain E. coli cells, dissolved in cell disruption buffer (50 mM Tris, pH7.5, 150 mM NaCl, 1% NP-40, 5 mM EDTA, 1 mM PMSF), and then disrupted by ultrasonication” (pg. 16 par. 3). The instant specification provides evidence that use of a Tris/EDTA buffer is an example of a method involving the use of a chelate agent [0088] (see claim 10).
Response to Arguments
Applicant argues (Remarks pg. 13) that “As noted above, amended independent claim 1 recites "a step of recovering a target foreign protein from the periplasmic fraction" of the E. coli after culture. Hak discloses expressing a target foreign protein on the surface of E. coli.”
This argument has been carefully considered but is not persuasive. Respectfully, applicant appears to be incorrect that the foreign protein of a 6x His peptide fused to the TolA fragment is expressed on the surface of E. coli. Hak teaches “E. coli's TolA protein used in the present invention is a protein that is attached to the inner membrane of one side and extends toward the outer membrane of one side and is present in a part of the periplasm.” (par. bridging pg. 4-5, emphasis added). The fusion protein is present in the periplasm and would be purified because the method is the same as the claimed purification method. Of note, the claims do not require that the periplasmic fraction be separated from other cell fractions. The claims only require that a target protein be recovered, and that the protein have been present in the periplasm so that the protein can be recovered from the periplasm.
Applicant argues (Remarks pg. 13) that “Additionally while deletion of the C-terminal region of TolA as disclosed in Hak may overlap with general mutation of TolA as disclosed in the instant application, the C-terminal region of TolA is distinct from the TolA signal peptide, which is located at the N-terminus of the protein.”
This argument has been carefully considered but is not persuasive. The relevance of this argument is unclear because the rejection does not discuss the TolA signal peptide and claim 7, which recites a signal peptide, was not previously rejected. If applicant is arguing that claim 7 and new claim 16 should not be rejected over Hak, the examiner agrees.
New Rejection(s)
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, 3-4, and 6-16 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.
Regarding claim 1, the term “quenches” is a relative term which renders the claim indefinite. The term “quenches” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. While it is clear that “quenches” refers to a decrease, the level of decrease is not defined by the claim or specification. Therefore, one of ordinary skill in the art at the time of filing would not be able to determine the bounds of the claim. Claims 3-4 and 6-16 are also rejected because they depend from claim 1 and do not obviate this grounds of rejection. Claim 5 is not rejected because complete deletion is a specific mutation that must necessarily reduce the level of protein activity.
Regarding claims 6 and 8, the antecedent basis of these claims is insufficient. Claim 6 recites “the modification is partial mutation”, which appears to have antecedent basis in “a modification in at least one gene associated with maintenance of outer membrane structure” from claim 1. However, claim 8 recites the limitation "the modification is partial mutation of a gene associated with outer membrane formation". There is insufficient antecedent basis for the limitations “the modification” and “a gene associated with outer membrane formation” in claim 8.
The specification defines “The term “gene associated with outer membrane formation” used herein refers to a gene of E. coli associated with maintenance of the outer membrane structure” [0017]. The specification also states “A gene associated with outer membrane formation is not particularly limited, provided that such gene is associated with maintenance of the outer membrane structure” [0017], but it does not define what “associations” fall within the scope of the definition. Due to this definition, the claim is indefinite because one of ordinary skill in the art would not be able to determine whether:
The “gene associated with outer membrane formation” in claim 8 is the same as the “at least one gene associated with maintenance of outer membrane structure” from claim 1 and is limited to being “selected from the group consisting of pal, ompA, tolA, mepS, nlpI, bamD, cyoA, ecnB, and slyB” as in claim 1, which would result in claim 8 not limiting claim 6.
The “gene associated with outer membrane formation” includes the full scope of the definition, which would result in claim 8 being broader than the scope of claims 1 and 6.
The “partial mutation” in claims 6 and 8 have improper antecedent basis and reference two different mutations despite using the same term.
The claim is indefinite because the insufficient antecedent basis for “the modification” and “a gene associated with outer membrane formation” prevents one of ordinary skill in the art from determining the claim scope.
Regarding claim 7, the claim recites “a signal sequence comprising an expression control sequence.” However, the specification defines “expression control sequence” as “The term "expression control sequence" used herein is not particularly limited, provided that such nucleotide sequence can be associated with expression of the coding region, and the expression control sequence may be a signal sequence and/or an SD sequence” [0038]. Due to the recursive definition (signal sequences comprises expression controls sequences which may be signal sequences), one of ordinary skill in the art would not be able to determine whether the signals from the sequence must be related to protein expression, or whether the specification is creating a special definition “expression control sequences” that is broader and includes any type of signaling. Where applicant acts as his or her own lexicographer to specifically define a term of a claim contrary to its ordinary meaning, the written description must clearly redefine the claim term and set forth the uncommon definition so as to put one reasonably skilled in the art on notice that the applicant intended to so redefine that claim term. Process Control Corp. v. HydReclaim Corp., 190 F.3d 1350, 1357, 52 USPQ2d 1029, 1033 (Fed. Cir. 1999). The claim is indefinite due to the lack of a clarity in the specification’s definition. In the interest of compact prosecution, the claim is interpreted as requiring the signal to be related to protein expression due to the presumption that claim terms are given their plain meaning, see MPEP 2173.01. Claim 16 is not rejected because the scope is limited to specific sequences.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 8 and 16 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. These rejections are related to the claim interpretations laid out in the 35 U.S.C. 112(b) rejection above. 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.
Regarding claim 8, depending on the interpretation, claim 8 is broader than or does not limit claim 6, as discussed in interpretations (a) and (b) above.
Regarding claim 16, the claim recites “the signal sequence comprises an expression control sequence selected from any one of SEQ ID NOs: 7, 9, 13, 17, 23, 25, 29, and 31”, which is interpreted as requiring a protein expression-related signal. Martin and Hine (2008, A Dictionary of Biology “gene expression”; PTO-892) teaches that gene expression defined by one of ordinary skill in the art at the time of filing as “The manifestation of the effects of a gene by the production of the particular protein, polypeptide, or type of RNA whose synthesis it controls. The transcription of individual genes can be ‘switched on’ or ‘switched off’ according to the needs and circumstances of the cell at a particular time.” Ostendorp et al. (US-20100168392-A1; PTO-892) teaches that SEQ ID NO: 25 is a “signal sequence” from OmpA from E. coli [0061]. However, Ostendorp teaches that this signal is not related to protein expression/production, it is related to protein localization after the protein expression has occurred: “A “signal sequence”, “signal peptide” or “secretion signal sequence” as used herein refers to a stretch of amino acids within a polypeptide or protein which directs said polypeptide or protein, typically a newly synthesized polypeptide or protein, through a cellular membrane of a host cell. In prokaryotic cells, signal sequences typically direct polypeptides or proteins through the cytoplasmic membrane into the periplasmic space. Usually, the signal sequence is present at the N-terminus of a protein or polypeptide and facilitates its transport to the periplasm or into the culture medium of the host cell.” [0025]. Therefore, claim 16 is broader than its parent claim 7 because it requires “expression control sequences” that are not related to controlling expression.
Claim Rejections - 35 USC § 112(a)
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 1, 3-4, and 6-16 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.
When evaluating the specification in the context of the prior art at the time of filing, one having ordinary skill in the art at the time of filing would have concluded that the specification demonstrated possession of methods of using E. coli having a modification in at least one gene associated with maintenance of outer membrane structure, wherein the at least one gene associated with maintenance of the outer membrane structure is selected from the group consisting of pal, ompA, tolA, mepS, nlpI, bamD, cyoA, ecnB, and slyB, and the modification quenches activity of a protein encoded by the at least one gene associated with maintenance of the outer membrane structure and wherein the modification is complete deletion, but have not demonstrated possession of a representative number of other types of modifications to the gene(s) that quench activity of the encoded protein(s). The rationale for this conclusion follows.
MPEP 2163 states:
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice (see i)(A) above), reduction to drawings (see i)(B) above), or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the inventor was in possession of the claimed genus (see i)(C) above).”
An original claim may lack written description support when (1) the claim defines the invention in functional language specifying a desired result but the disclosure fails to sufficiently identify how the function is performed or the result is achieved or (2) a broad genus claim is presented but the disclosure only describes a narrow species with no evidence that the genus is contemplated. See Ariad Pharms., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1349-50 (Fed. Cir. 2010) (en banc). The written description requirement is not necessarily met when the claim language appears in ipsis verbis in the specification. "Even if a claim is supported by the specification, the language of the specification, to the extent possible, must describe the claimed invention so that one skilled in the art can recognize what is claimed. The appearance of mere indistinct words in a specification or a claim, even an original claim, does not necessarily satisfy that requirement." Enzo Biochem, Inc. v. Gen-Probe, Inc., 323 F.3d 956, 968, 63 USPQ2d 1609, 1616 (Fed. Cir. 2002).
Thus, the written description requirement may be satisfied through disclosure of function and minimal structure when there is a well-established correlation between structure and function. In contrast, without such a correlation, the capability to recognize or understand the structure from the mere recitation of function and minimal structure is highly unlikely. In this latter case, disclosure of function alone is little more than a wish for possession; it does not satisfy the written description requirement. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406 (written description requirement not satisfied by merely providing "a result that one might achieve if one made that invention"); In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming a rejection for lack of written description because the specification does "little more than outline goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate").
The claims are methods of producing a target foreign protein, comprising: (a) a step of step of introducing a gene encoding the target foreign protein into E. coli, (b) b) a step of culturing the E. coli of (a); and (c) a step of recovering a target foreign protein from the periplasmic fraction of the E. coli after culture. The E. coli as claimed has been amended to claim a modification in at least one gene associated with maintenance of outer membrane structure, wherein the at least one gene associated with maintenance of the outer membrane structure is selected from the group consisting of pal, ompA, tolA, mepS, nlpI, bamD, cyoA, ecnB, and slyB, and the modification quenches activity of a protein encoded by the at least one gene associated with maintenance of the outer membrane structure.
The “modification” is broad and not limited by the claims. Claim 5 teaches the modification can be a complete deletion of the gene. Claim 6 teaches the modification can be a partial modification of the gene; the broadest reasonable interpretation includes amino acid insertions, partial deletions, amino acid substitutions, fusions with other proteins, etc. The specification defines that the modifications can be deletions, insertions, or substitutions at [0036]. Claim 7 teaches the modification can be to a protein-expression-related signal sequence; the broadest reasonable interpretation includes modifications to the promoter and other non-coding parts of the gene. Claim 16 teaches the modification can be a partial modification of some specific signal sequences with defined SEQ ID NOs, but does not teach what the sequence is modified to. The scope of modifications is broader than the modifications described to quench activity.
The art at the time of filing confirms the breadth of modifications that are claimed. Hak et al. (KR-20040036176-A; hereafter Hak; PTO-892 mailed 28 Nov 2025) teaches E. coli where the tolA gene is removed from the genome (Example 3, i.e. a complete deletion), and substituted with a TolA variant where the C-terminal region of TolA protein gene is substituted with a gene encoding a target protein (Abstract, i.e. the target foreign protein is a TolA protein with a partial deletion of the gene that is also fused to another protein). As a second example, Ellis et al. (US-20120295309-A1; hereafter Ellis; PTO-892) teaches a recombinant gram-negative bacterial cell comprising a mutant spr gene encoding a spr protein having a mutation at one or more amino acids selected from D133, H145, H157, N31, R62, I70, Q73, C94, S95, V98, Q99, R100, L108, Y115, V135, L136, G140, R144 and G147 [Abstract], particularly in E. coli [0001]. Ellis specifically teaches that the E. coli may have combinations of multiple point mutations [0122, 0093], and teaches that the mutations may replace the amino acid with “any suitable amino acid” [0091]. Lee et al. (2021; hereafter Lee; PTO-892) provides evidence that the protein mepS was formerly annotated as Spr (Abstract, pg. 178 col. 2 par. 2); this evidentiary reference is cited “to understand "the meaning of a term in the relevant art during the relevant time period". Actelion, 85 F.4th at 1174 (quoting Teva Pharmaceuticals USA, Inc v. Sandoz, Inc., 574 U.S. 318, 331,135 S. Ct. 831, 841, 113 USPQ2d 1269, 1276 (2015))”, see MPEP 2131.01, and to show that the characteristics and properties of the protein mepS are the same as the characteristics and properties of the protein Spr at the application’s filing date, see MPEP 2124. Therefore, Ellis teaches E. coli having a modification in at least one gene associated with maintenance of outer membrane structure, wherein the at least one gene associated with maintenance of the outer membrane structure is mepS/spr.
Applicant points to cancelled claim 2 and paragraphs [0017], [0035], [0036], and [0038] as support for the amendment to claim 1. There is support for limiting the “gene associated with maintenance of the outer membrane structure” to the specific list of genes now claimed in cancelled claim 2 and [0017].
For support for “the modification quenches activity of a protein encoded by the at least one gene associated with maintenance of the outer membrane structure”, [0035] states “In particular, genetic modification that attenuates activity of a protein encoded by the gene, compared with activity of the parent strain, and such modification encompasses genetic modification that would completely quench the activity.” This is the only use of the word “quench” in the specification. The specification does not give any examples of specific mutations that would quench the protein activity at [0035], [0036], or [0038]. The specification reduces to practice mutant E. coli with full gene deletion of pal, a partial deletion of positions 39-63 of pal and a point mutation to substitute position 14 of lpp with a glycine (Example 1) and also reduces to practice mutant E. coli with single-gene deletions of ompA, tolA, mepS, nlpI, arcA, cyoA, dppA, ecnB, mrcA, mnrcB, oppA, and slyB (Example 3). The specification measures the recovery of a target protein of interest (specifically, a VHH antibody) from the periplasmic fraction in these modified strains (Examples 2-3). The specification does not measure the activity of any of the modified proteins. A deleted gene necessarily causes the protein to not be present, so the full gene deletions must quench the protein activity. However, the specification does not provide any evidence or rationale supporting that a partial deletion of positions 39-63 of pal and a point mutation to substitute position 14 of lpp with a glycine have a “quenching” effect on the protein activity.
The specification is not required to teach features that were well known in the art at the time of filing. From MPEP 2163: “What is conventional or well known to one of ordinary skill in the art need not be disclosed in detail. See Hybritech Inc. v. Monoclonal Antibodies, Inc., 802 F.2d at 1384, 231 USPQ at 94. See also Capon v. Eshhar, 418 F.3d 1349, 1357, 76 USPQ2d 1078, 1085 (Fed. Cir. 2005).” However, in this situation, the art does not fill the gap by disclosing a conventional and well known correlation between which potential gene modifications have the function of quenching activity of the encoded protein. Ellis teaches spr/mepS mutations that are “capable of suppressing the phenotype of a cell comprising a mutated Tsp gene” [0089], and teaches that the mutations may be in the catalytically active site [0093], but does not teach the correlation of whether the disclosed mutations affect the spr/mepS activity by increasing activity, decreasing activity, or changing the protein’s activity or function in some other way.
MPEP 2163 states: “The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice (see i)(A) above), reduction to drawings (see i)(B) above), or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the inventor was in possession of the claimed genus (see i)(C) above).”
In this case, the specification has actually reduced to practice E. coli with whole gene deletions that have the function of quenching the protein’s activity. The reduction to practice of a partial gene deletion and a point mutation fall outside the scope of what is claimed because the specification does not describe that the mutants have quenched protein activity. There are no additional mutations that are disclosed by reduction to drawings. Finally, while the specification contemplates mutations that could be made in general terms, the specification does not describe any additional modifications with the function of quenching the protein’s activity by a specific disclosure of specific identifying characteristics such as describing the structure of the mutation that should be made. There is no disclosed correlation between the claimed function and the gene modification(s), and such a correlation is also not conventional in the art at the time of filing. Therefore, what is described amounts to methods of using E. coli with whole gene deletions that have the function of quenching the protein’s activity. This one type of mutation is not representative of the breadth of mutations that are claimed because it removes a protein completely rather than changing any of the protein’s properties like the partial deletions, insertions, and substitution mutations. Therefore, one of ordinary skill in the art at the time of filing would have concluded that the specification does not disclose a representative number of species within the clamed genera of methods, E. coli strains, and gene modifications.
When evaluating the specification in the context of the prior art at the time of filing, one having ordinary skill in the art at the time of filing would have concluded that the specification demonstrated possession of methods of using E. coli having a modification in at least one gene associated with maintenance of outer membrane structure, wherein the at least one gene associated with maintenance of the outer membrane structure is selected from the group consisting of pal, ompA, tolA, mepS, nlpI, bamD, cyoA, ecnB, and slyB, and the modification quenches activity of a protein encoded by the at least one gene associated with maintenance of the outer membrane structure and wherein the modification is complete deletion, but have not demonstrated possession of a representative number of other types of modifications to the gene(s) that quench activity of the encoded protein(s). Therefore, claims 1, 3-4, 6-16 are rejected for failing to describe the scope of the claimed invention. In the interest of compact prosecution, it is noted that there were at least two additional mutations described by the specification that would fall within the bounds of the claims if the functional limitation (“quenches activity”) was removed, but this non-claimed subject matter was not examined and no opinion is provided about what scope may or may not be described by the specification.
Pertinent Prior Art
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure. Tokunaga et al. (WO-2021200784-A1, priority to 31 March 2020, published 7 Oct 2021; hereafter Tokunaga; PTO-892) teaches Escherichia coli including a gene encoding a peptidoglycan-binding lipoprotein (Pal) having a partial mutation and a gene encoding an exogenous protein and the bacteria’s use to produce the exogenous protein [Abstract]. This reference is 102(a)(2) art only, and both the instant application and the reference have the applicant “Kaneka Corporation” and appear to have shared inventors. If possible, it is requested that applicant clarify whether the reference qualifies for a 102(b)(2)(A) and/or 102(b)(2)(C) exception.
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 AMELIA N DICKENS whose telephone number is (571)272-0381. The examiner can normally be reached M-F 8:30-4:30 (EDT/EST).
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/AMELIA NICOLE DICKENS/Examiner, Art Unit 1645
/SAMIRA J JEAN-LOUIS/Supervisory Patent Examiner, Art Unit 1642
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