DETAILED OFFICE ACTION
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s preliminary amendment to the claims, filed on November 21, 2023, is
acknowledged. This listing of the claims replaces all prior versions and listings of the
claims.
Claims 1-2, 4-7, 9, 11, 13, 15-24, and 29 are pending and are being examined on the merits.
Claims 3, 8, 10, 12, 14, and 25-28 are cancelled.
Priority
This application is filed under 35 U.S.C. 371 as a national stage of international
application PCT/EP2022/065066, filed on June 2, 2022, which claims foreign priority under 35 U.S.C. 119(a)-(d) to a foreign patent application EP21177466.6 filed on June 2, 2021. A certified copy of the foreign priority application has been filed in this application on November 21, 2023.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on February 22, 2024 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDS has been considered by the examiner.
The listing of references in the specification (i.e., p. 41-42) is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Claim Objections
Claims are 1, 4-6, 9, 11, 16, 18, 21, and 23-24 objected to because of the following informalities:
Claims 1, 5-6, 9, 11, 16, 23-24 are objected to for reciting “SEQ ID NO.” Claims 1 and 16 are objected to for reciting “A.”, “B.”, and “C.”. Claim 18 is objected to for reciting “D.” and “E.”. Claim 23 is objected to for reciting “A.” and “B.”. According to MPEP 608.01(m), “Each claim begins with a capital letter and ends with a period. Periods may not be used elsewhere in the claims except for abbreviations. See Fressola v. Manbeck, 36 USPQ2d 1211 (D.D.C. 1995)”. In the interest of improving claim form, the Office suggests amending “SEQ ID NO.” to ““SEQ ID NO:”. In the interest of improving claim form, the Office suggests amending “A.”, “B.”, “C.”, “D.”, and “E.” to “A)”, “B)”, “C)”, “D)”, and “E)”, respectively.
Claim 1 is objected to for reciting “gene is on the genome of said cell.” Claims 4-5 are objected to for reciting “encoded by the gene on the genome.” In the interest of improving claim form, the Office suggests amending “gene is on the genome of said cell” to “gene is encoded by the host cell genome.” In the interest of improving claim form, the Office suggests amending “encoded by the gene on the genome” to “encoded by the host genome.”
Claim 4 is objected to because of the recitation of “according claim 1.” In the interest of improving claim form, the Office suggests amending the recited phrase to “according to claim 1.”
Claim 21 is objected to because of the recitation of “E. coli” without first writing out the full phrase for which the abbreviation “Escherichia coli” is used. In the interest of improving claim form, the Office suggests amending “E. coli” to “Escherichia coli.”
Claims 1, 16, and 21 are objected to because of the recitation of “enhanced.” In the interest of improving claim form, the Office suggests amending “enhanced” to “increased.”
Claim 23 is objected to for not ending with a period. In the interest of improving claim form, the Office suggests amending the claim to end with a period.
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.
Claims 1-2, 4-7, 9, 11, 13, 15-24, and 29 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
Claim 1 (claims 2, 4-7, 9, 11, 13, 15-22, and 29 dependent therefrom) and claim 23 (claim 24 dependent therefrom) are indefinite because the recitation of the phrase “decreased activity” is unclear. It is unclear what activity is decreased in the mutant RNAse E as compared to the RNAse E of SEQ ID NO: 2. The Offices suggests that the applicant clarify the meaning by amending the claims to recite the activity that is decreased in the mutant. For the purpose of compact prosecution, the limitation of “decreased activity” in the claims is construed to refer to any “activity” comprised by RNAse E.
Claims 2, 7, 9, 11, 13, and 24 are indefinite because of the use of exemplary claim language in the phrase “such as”. The phrase “such as” renders the claims indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. Description of examples or preferences is properly set forth in the specification rather than the claims. If stated in the claims, examples and preferences may lead to confusion over the intended scope of a claim. See MPEP § 2173.05(d). For the purpose of compact prosecution, the limitations following “such as” are interpreted as optional limitations.
Claims 7, 11, 13, and 15 are indefinite for being unclear in the recitation of position(s) of amino acid substitution(s) without providing a relative sequence to which the substitution(s) occur. The Offices suggests that the applicant clarify the meaning by amending the claims to recite that the substitutions occur “relative to SEQ ID NO: 2” – like in line 4 of claim 6. For the purpose of compact prosecution, the substitutions listed in claims are interpreted as occurring “relative to SEQ ID NO: 2” or at the respective position of any RNAse E polypeptide.
Claim is 15 is indefinite because the phrase “the amino acid substitution is A441” is unclear. It is unclear to whether the recited phrase means the amino acid substitution is a substitution of alanine at position 441 with another amino acid or the amino acid substitution is a substitution for the amino acid at position 441 with alanine. The Offices suggests that the applicant clarify the meaning by amending the recited phrase to “the amino acid substitution is at A441 relative to SEQ ID NO: 2.” For the purpose of compact prosecution, the recited phrase is interpreted as a substitution of alanine at position 441 with another amino acid or the amino acid substitution is a substitution for the amino acid at position 441 with alanine.
Claim 19 is indefinite because the claim recites the phrase "the first prokaryotic vector" which lacks antecedence. Claim 1 and claim 18 do not recite the phrase “the first prokaryotic vector.” Since claim 19 depends up claim 18 which further depends upon claim 1, there is insufficient antecedent basis for this limitation and therefore “the first prokaryotic vector” lacks antecedence. The Offices suggests that the applicant clarify the meaning by amending the recited phrase to phrase "a first prokaryotic vector." For the purpose of compact prosecution, the recited phrase is interpreted as "a first prokaryotic vector."
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 1-2, 4, 6-7, 9, 11, 13, 16, 21-22, and 29 are rejected under 35 U.S.C. 103 as being unpatentable over Gialama (J Mol Biol, published 2017, Vol. 429, p. 1800-1816; cited on the attached Form PTO-892; hereafter “Gialama”) in view of Callaghan et al. (Nature, published 2005, Vol 437, p. 1187-1191; cited on the IDS filed February 22, 2024; hereafter “Callaghan”) and Garrey et al. (The Journal of Biochemistry, published 2009, Vol. 284, No. 46, p. 31843-31850; cited on the IDS filed February 22, 2024; hereafter “Garrey”) as evidenced by Richards et al. (The Journal of Biological Chemistry, published 2015, Vol. 291, No. 10, p. 5038-5048; cited on the attached Form PTO-892; hereafter “Richards”) and Uniprot Accession Number A0A1V3W0R1 (entry version 22, published February 26, 2020; cited on the attached Form PTO-892; hereafter “A0A1V3W0R1”)
Regarding claims 1-2, 4, and 22, Gialama teaches an Escherichia coli strain engineered to express a toxic membrane protein of interest, and wherein the strain expresses a RNAse E mutant ENS134-22 with reduced activity which increases the accumulation of the toxic membrane protein (Abstract; p. 1809, col 2, para 2; Supplemental p. 4, para 2; Figure 4). Gialama teaches the RNAse E mutant ENS134-22 comprises a deletion of amino acid residues 603-693 of wild-type RNAse E from Escherichia coli (Figure 4). Gialama teaches RNAse E is an endonuclease known to degrade mRNA in Escherichia coli and is an essential gene for cell viability (p. 1809, col 1, para 3). Gialama teaches Escherichia coli comprises the ribonuclease RNAse G (Abstract; p. 1813, col 1, para 1).
Richards is cited in accordance with MPEP 2131.01.III to show Escherichia coli RNAse G is an endonuclease (Abstract; p. 5038, col 1, para 1). Therefore, the Escherichia coli strain comprises an endonuclease RNAse G encoded by the native genome.
A0A1V3W0R1 is cited as an evidentiary reference to show the amino acid sequence of Escherichia coli RNAse E is identical to instant SEQ ID NO: 2 (p. 1, see alignment below).
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750
315
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Therefore, the Escherichia coli RNAse E mutant comprising a deletion of amino acid residues 603-693 of wild-type RNAse E from Escherichia coli taught by Gialama has 91.4% sequence identity with instant SEQ ID NO: 2 (see alignment below).
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1005
407
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Regarding claim 21, Gialama teaches the Escherichia coli strain expressing the RNAse E mutant ENS134-22 produces the toxic protein approximately 2.5-9 times and 1.5-2.5 times greater than a control cell expressing the control RNAse E when effector protein RraA is not co-expressed or is co-expressed, respectively (Figure 4).
Regarding claim 29, Gialama teaches the Escherichia coli strain engineered to express a toxic membrane protein of interest is cultured in LB media (Abstract; p. 1809, col 2, para 2; Supplemental p. 4, para 2; Figure 4).
Regarding claims 1-2, 4, 21-22, and 29, Gialama does not teach a mutant RNAse E with a at least 75% sequence identity with SEQ ID NO: 2 and wherein the amino acid sequence has one or more substitutions which results in the decreased activity compared to SEQ ID NO: 2. Regarding claims 6-7, 9, 11, and 13, Gialama also does not teach mutant RNAse E with a mutation selected from D346, E297, D303, N305, E325, R337, D349, V128, R169, T170, F57, F67, K112, G124, R141, R142, or R373 relative to SEQ ID NO: 2.
Callaghan teaches D303R and D346N substitutions reduces RNAse E catalytic activity 25-fold (p. 1188, col 1, para 2 – p. 1188, col 2, para 1). Callaghan teaches the DNase I-like domain of RNAse E comprises amino acids 279-400 (Figure 2). Callaghan teaches D303 and D346 is coordinates Mg ion in RNAse E (p. 1188, col 1, para 2; Figure 2). Callaghan teaches N305D and N305L substitutions reduces RNAse E catalytic (p. 1188, col 1, para 2 – p. 1188, col 2, para 1).Callaghan teaches F57A, F67A, or K112A substitutions reduces RNAse E catalytic activity by 50-fold (p. 1188, col 2, para 2). Callaghan teaches R373A or R373D substitutions reduces RNAse E catalytic activity tenfold (p. 1188, col 1, para 1). Callaghan teaches replacing R169 or V128 in RNAse E reduces its catalytic activity for substrate with 5’ monophosphate (p. 1187, col 2, para 4 – p. 1188, col 1, para 1). Callaghan teaches the 5’ sensing pocking of RNAse E comprises V128, G124, R169, and T170 (Figure 3). Callaghan teaches a T170V substitution inactivates RNAse E (p. 1188, col 1, para 1).
Garrey also teaches single-point mutation variants of the Escherichia coli RNAse E catalytic domain that exhibit reduced catalytic activity compared with wild-type RNAse E: F57A, F67A, R169Q, D303A, and D346A (Abstract; p. 31847, col 2, para 1; Table 2). Garrey teaches F67 of RNAse E interacts with the RNA substrate in the S1 domain close to the catalytic site (p. 31847, col 2, para 2). Garrey teaches amino acid residues Q297, D303, Q325, and D346, and D349 of RNAse E are acidic residues that could play a role in metal ion chelation and also that D303 and D346 believed to chelate a Mg+2 ion (p. 31845, col 1, para 1; p. 31847, col 2, para 2). Garrey teaches the amino acid R169 is in the RNAse E 5’-sensor as well as that 5’-sensor domain interacts with a 5’-mono-phosphorylated substrate via contact with G124, V128, R169, and T170 (Abstract; p. 31843, col 2, para 1-2; p. 31847, col 2, para 1).
In view of the combined teachings of Gialama, Callaghan, and Garrey, it would have been obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention to substitute the mutant RNAse E with reduced activity in the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by Gialama with a full-length RNAse E modified to have reduced catalytic activity as a result of a substitution from the group taught by Callaghan comprising F57A, F67A, K112A, D303R, N305D, N305L, D346N, R373A, and R373D or the R169Q taught by Garrey, thereby arriving at the invention of claims 1-2, 4, 6-7, 9, 11, 13, 21-22, and 29.
An ordinary artisan would have been motivated to and would have had a reasonable expectation of success of substituting the mutant RNAse E with reduced activity in the Escherichia coli strain engineered to express a toxic membrane protein of interest when cultured in LB media taught by Gialama with a full-length RNAse E modified to have reduced catalytic activity as a result of a substitution from the group taught by Callaghan comprising F57A, F67A, K112A, D303R, N305D, N305L, D346N, R373A, and R373D or the R169Q taught by Garrey because it is obvious to substitute one known RNAse E with reduced catalytic activity for another and achieve a predictable result because they have the same function and impairment at cleaving RNA molecules.
Regarding claim 16, the relevant teachings of Gialama, Callaghan, and Garrey, and evidentiary references Richards and A0A1V3W0R1 as applied to claims 1-2, 4, 6-7, 9, 11, 13, 21-22, and 29, are discussed above and incorporated herein.
It is the Examiner’s position that claim 16 constitutes a product-by-process and because claim 16 does not recite a particular “parent cell,” claim 16 does not structurally and/or functionally further limit the prokaryotic microbial host cell of claim 1. Since the patentability of a product-by-process claim is determined by the product claimed and not the recited process steps (see MPEP 2113), instant claim 16 is obvious over the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination Gialama, Callaghan, and Garrey, and evidentiary references Richards and A0A1V3W0R1, as applied to claim 1.
Consequently, the invention of claims 1-2, 4, 6-7, 9, 11, 13, 16, 21-22, and 29 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claims 5, 17, and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Gialama in view of Callaghan and Garrey, as applied to claims 1-2, 4, 6-7, 9, 11, 13, 16, 21-22, and 29 above, and further in view of Briegel et al. (Genetics, published 2006, Vol. 172, p. 7-15; cited on the IDS filed February 22, 2024; hereafter “Briegel”), Woo et al. (The Journal of Biological Chemistry, published 1997, Vol. 272, No. 24, p. 15516-15520; cited on the attached Form PTO-892; hereafter “Woo”), and McDowall et al. (Journal of Bacteriology, published 1993, Vol. 175, No. 13, p. 4245-4249; cited on the attached Form PTO-892; hereafter “McDowall”) as evidenced by Richards and A0A1V3W0R1.
The relevant teachings of Gialama, Callaghan, and Garrey, and evidentiary references Richards and A0A1V3W0R1 as applied to claims 1-2, 4, 6-7, 9, 11, 13, 16, 21-22, and 29, are discussed above and incorporated herein.
Regarding claims 5, 17, and 24, Gialama further teaches wherein the toxic membrane protein is encoded by and expressed from a plasmid (Figures 2 and 4).
The combination of Gialama, Callaghan, and Garrey does not explicitly teach wherein the mutant RNAse E is expressed on a plasmid.
Briegel teaches expressing mutant Escherichia coli RNAse E encoded by a plasmid without a rne promoter that instead uses a Lac promoter to avoid autoregulation (p. 8, col 2, para 3 - p. 9, col 1, para 2).
Woo teaches culturing Escherichia coli comprising temperature sensitive RNAse E variant rne-3071 at a non-permissive temperature to inactivate the temperature sensitive enzyme (p. 15516, col 1, para 1 – p. 15516, col 2, para 3; p. 15517, col 1, para 1 – p. 15517, col 2, para 1).
McDowall teaches the temperature sensitive variant of Escherichia coli RNase E called rne-3071 consists of the substitution F68L (p. 4245, col 1, para 1 – p. 4245, col 2, para 3).
In view of the combined teachings of Gialama, Callaghan, Garrey, Briegel, Woo, and McDowall, it would have been obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention modify the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination of Gialama, Callaghan, and Garrey such that the mutant RNAse E is encoded on and expressed from a plasmid with Lac promoter as taught by Briegel and wherein the genomic rne gene is modified to comprise the temperature-sensitive RNase E variant encoded by rne-3071 taught by Woo and McDowall, thereby arriving at the invention of claims 5, 17, and 24.
An ordinary artisan would have been motivated to and would have had a reasonable expectation of success of modifying the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination of Gialama, Callaghan, and Garrey such that the mutant RNAse E is encoded on and expressed from a plasmid with Lac promoter to prevent autoregulation from the genomic rne. An ordinary artisan would further have been motivated to and would have had a reasonable expectation of success of modifying the genomic rne gene is modified to comprise the temperature-sensitive RNAse E variant encoded by rne-3071 taught by Woo and McDowall in order to inactivate the temperature-sensitive RNAse E when the cell is cultured at a non-permissive temperature so that the RNAse E mutant with reduced activity increases the production of the toxic membrane protein.
Consequently, the invention of claims 5, 17, and 24 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claims 18-20 and 23 are rejected under 35 U.S.C. 103 as being unpatentable over Gialama in view of Callaghan, Garrey, Briegel, Woo, and McDowall, as applied to claims 1-2, 4-7, 9, 11, 13, 16-17, 21-22, 24, and 29, and further in view of Studier et al. (J. Mol. Biol., published 1991, Vol. 219, p. 37-44; cited on the IDS filed February 22, 2024; hereafter “Studier”) as evidenced by Richards and A0A1V3W0R1.
The relevant teachings of Gialama, Callaghan, Garrey, Briegel, Woo, McDowall, and evidentiary references Richards and A0A1V3W0R1 as applied to claims 1-2, 4-7, 9, 11, 13, 16-17, 21-22, 24, and 29, are discussed above and incorporated herein.
Regarding claims 18 and 23, the combination of Gialama, Callaghan, Garrey, Briegel, Woo, and McDowall does not explicitly teach wherein the Escherichia coli further comprises a gene encoding a T7 polymerase and wherein the expression of the target protein is regulated by an inducible T7 promoter.
Studier teaches the presence of T7 lysozyme improves an inducible T7 expression system comprising plasmid expressing a T7 RNA polymerase under a T7 inducible promoter to express a toxic gene in Escherichia coli (Abstract; p. 38, col 1, para 1). Studier teaches the T7 lysozyme is a natural inhibitor of T7 RNA polymerase and can reduce the activity from an inducible gene for T7 RNA polymerase and stabilizes target plasmids and allow high level production of a target protein (Abstract). Studier further teaches the presence of T7 lysozyme has the additional advantage of facilitating the lysis of the host cells in the preparation of extracts for purification of the target gene product (Abstract).
In view of the combined teachings of Gialama, Callaghan, Garrey, Briegel, Woo, McDowall, and Studier, it would have been obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention to modify the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination of Gialama, Callaghan, Garrey, Briegel, Woo, and McDowall such that the plasmid encoding the target toxic protein is modified such that it under the control of a T7 inducible promoter and that the cell is modified to express T7 lysozyme, thereby arriving at the invention of claim 18 and 23.
An ordinary artisan would have been motivated to and would have had a reasonable expectation of success of modifying the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination of Gialama, Callaghan, Garrey, Briegel, Woo, and McDowall such that the plasmid encoding the target toxic protein is modified such that it under the control of a T7 inducible promoter and that the cell is modified to express T7 lysozyme Studier teaches the presence of T7 lysozyme improves an inducible T7 expression system comprising plasmid expressing a T7 RNA polymerase under a T7 inducible promoter to express a toxic gene in Escherichia coli. This is because Studier teaches the presence of T7 lysozyme improves an inducible T7 expression system comprising plasmid expressing a T7 RNA polymerase under a T7 inducible promoter to express high amounts of a toxic gene in Escherichia coli.
Regarding claim 19, the relevant teachings of Gialama, Callaghan, Garrey, Briegel, Woo, McDowall, and Studier, and evidentiary references Richards and A0A1V3W0R1 as applied to claims 1-2, 4-7, 9, 11, 13, 16-18, 21-24, and 29, are discussed above and incorporated herein.
The combination of Gialama, Callaghan, Garrey, Briegel, Woo, McDowall, and Studier does not explicitly teach wherein the Escherichia coli further comprises a gene encoding a T7 lysozyme located on the plasmid encoding the mutant RNAse E with reduced activity.
An ordinary artisan would have immediately recognized the expression of T7 lysozyme from either the plasmid encoding the mutant RNAse E or the plasmid encoding the target toxic protein and expressed by a T7 RNA polymerase would lead to the inhibition of the polymerase and improve the expression of the target toxic protein.
In view of the combined teachings of Gialama, Callaghan, Garrey, Briegel, Woo, McDowall, and Studier, it would have been obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention to modify the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination of Gialama, Callaghan, Garrey, Briegel, Woo, McDowall, and Studier such that the T7 lysozyme is encoded by the plasmid encoding the mutant RNAse polymerase with reduced activity, thereby arriving at the invention of claim 19.
An ordinary artisan would have been motivated to and would have had a reasonable expectation of success of modifying the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination of Gialama, Callaghan, Garrey, Briegel, Woo, McDowall, and Studier such that the T7 lysozyme is encoded by the plasmid encoding the mutant RNAse polymerase with reduced activity in order to lead to the inhibition of the T7 RNA polymerase and improve the expression of the target toxic protein.
Regarding claim 20, the combination of Gialama, Callaghan, Garrey, Briegel, Woo, and McDowall does not explicitly teach wherein the target toxic protein is expressed by a promoter selected from rhaBad promoter, araBad promoter, Ptrc promoter, Ptact promoter, and PL promoter.
Studier teaches the use of a tet promoter to express a recombinant gene encoded by a plasmid in Escherichia coli (p. 37, col 2, para 2; p. 38, col 1, para 2).
In view of the combined teachings of Gialama, Callaghan, Garrey, Briegel, Woo, McDowall, and Studier, it would have been obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention to modify the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination of Gialama, Callaghan, Garrey, Briegel, Woo, and McDowall such that the plasmid encoding the target toxic protein is modified such that it under the control of a tet inducible promoter, thereby arriving at the invention of claim 20.
An ordinary artisan would have been motivated to and would have had a reasonable expectation of success of modifying the Escherichia coli strain engineered to express a toxic membrane protein of interest taught by the combination of Gialama, Callaghan, Garrey, Briegel, Woo, and McDowall such that it under the control of a tet inducible promoter because Studier taught the use of a tet promoter to express a recombinant gene encoded by a plasmid in Escherichia coli.
Consequently, the invention of claims 18-20 and 23 would have been obvious to one of ordinary skill in the art before the effective filing date.
Allowable Subject Matter
The closest prior art of record is Gialama. Gialama teaches an Escherichia coli strain engineered media to express a toxic membrane protein of interest, and wherein the strain expresses a RNAse E mutant ENS134-22 with reduced activity which increases the accumulation of the toxic membrane protein. Regarding claim 15, Gialama either alone or in combination with the other prior art of record, does not teach or suggest an RNAse E with a substitution at A441 relative to SEQ ID NO: 2.
Conclusion
No claims are currently allowed for the reasons as stated above. Applicants must
respond to the objections/rejections in this Office action to be fully responsive in
prosecution.
The instant Office Action is non-final.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SCOTT E. MULDER whose telephone number is (571)272-2372. The examiner can normally be reached Monday - Friday 7:30 AM - 3:30 PM.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath Rao can be reached on (571) 272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/SCOTT E. MULDER/Examiner, Art Unit 1656
/David Steadman/Primary Examiner, Art Unit 1656
Prosecution Insights