DETAILED ACTION
Status of the Application
Claims 1-9 are pending.
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
A preliminary amendment of claim 6 and cancellation of claim 10 as submitted in a communication filed on 5/11/2026 is acknowledged.
Applicant’s election without traverse of Group I, claims 1-5, drawn to a microorganism in which the activity of a protein comprising SEQ ID NO: 1 is weakened, as submitted in a communication filed on 5/11/2026 is acknowledged.
Claims 6-9 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 5/11/2026.
Claims 1-5 are at issue and are being examined herein.
Priority
Acknowledgment is made of a claim for foreign priority under 35 U.S.C. 119(a)-(d) to REPUBLIC OF KOREA 10-2021-0137890 filed on 10/15/2021. Receipt is acknowledged of papers submitted under 35 U.S.C. 119(a)-(d), which papers have been placed of record in the file.
This is the US national application which entered the national stage from PCT/KR2022/015551 filed on 10/14/2022.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 4/2/2024, 6/10/2025, and 11/18/2025 are acknowledged. The submissions are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA )
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 1-5 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 pre-AIA the applicant regards as the invention.
Claim 1 (claims 2-5 dependent thereon) is indefinite in the recitation of “…microorganism of the genus Corynebacterium producing L-arginine, in which the activity of a protein including the amino acid sequence of SEQ ID NO: 1 is weakened” for the following reasons. It is unclear if the term “producing L-arginine” intends to limit the microorganism to one that is able to produce L-arginine. Moreover, the term “the activity of a protein including the amino acid sequence of SEQ ID NO: 1” is unclear because one cannot determine how one could weaken the activity of the amino acid sequence of SEQ ID NO: 1. As known in the art, an amino acid sequence is a graphical representation of the order in which amino acids are arranged in a protein. Therefore, an amino acid sequence, which is not a molecule, does not have activity. Please note that as written, it appears that the term refers to the activity of an undefined protein and the activity of the amino acid sequence of SEQ ID NO: 1. If the intended limitation is a protein that comprises SEQ ID NO: 1, the claim should be amended accordingly. In addition, the term “activity” is unclear in the absence of the specific activity associated with the protein. As known in the art, a protein can have more than one activity, such as enzymatic activity, binding activity, antibody eliciting activity, etc. Furthermore, it is unclear as to what is encompassed by the term “weakened” as it relates to the activity of a protein. The term “weaken” can refer to lessen the strength or reduce the intensity or effectiveness of something. Does the term refer to simply reducing enzymatic activity? Does the term refer to reduce a particular action associated with an acetyltransferase? If the intended limitation is a recombinant microorganism that lacks acetyltransferase activity, the claim should be amended accordingly. Correction is required.
Claim 2 is indefinite in the recitation of “…increased L-arginine producing ability compared with a parent strain in which the activity of the protein including the amino acid sequence of SEQ ID NO: 1 is not weakened” for the following reasons. The term “a parent strain” is a generic term that encompasses a genus of strains which do not have to be of the same genus/species of the recombinant Corynebacterium. Therefore, the claim requires the comparison to be made with a genus of organisms. The basis for comparison is variable, thus making a determination as to what is encompassed and what is excluded impossible. For example, a recombinant Corynebacterium can be encompassed by the claim if the comparison is made with a B. subtilis strain and not encompassed by the claim if the comparison is made with a C. glutamicum strain. In addition, the term “the activity of a protein including the amino acid sequence of SEQ ID NO: 1” is unclear because one cannot determine how one could not weaken the activity of the amino acid sequence of SEQ ID NO: 1. As known in the art, an amino acid sequence is a graphical representation of the order in which amino acids are arranged in a protein. Therefore, an amino acid sequence, which is not a molecule, does not have activity. For examination purposes, claim 2 will be interpreted as a duplicate of claim 1. Correction is required.
Claim 4 is indefinite in the recitation of “wherein the activity of an arginine repressor is additionally weakened” for the following reasons. The term “activity” is unclear in the absence of the specific activity associated with the protein. As known in the art, a protein can have more than one activity, such as enzymatic activity, binding activity, antibody eliciting activity, etc. In addition, the term “arginine repressor” is unclear because one cannot determine what is being repressed by this repressor. Does it repress arginine production? Does it repress the activity of arginine in a particular process? Furthermore, it is unclear as to what is encompassed by the term “weakened” as it relates to the activity of a protein. The term “weaken” can refer to lessen the strength or reduce the intensity or effectiveness of something. Does the term refer to simply reducing activity? Does the term refer to reduce a particular action associated with an arginine repressor? If the intended limitation is a recombinant microorganism that lacks arginine repressor activity, the claim should be amended accordingly. For examination purposes, it will be assumed that the term “arginine repressor” refers to a protein that represses the production of arginine in a cell. Correction is required.
Claim 5 is indefinite in the recitation of “polynucleotide encoding the protein including the amino acid sequence of SEQ ID NO: 1” for the following reasons. It is unclear as to which is the protein being encoded by the polynucleotide. As written, it appears that the protein encodes a protein which can have any amino acid sequence and at the same time encodes the amino acid sequence of SEQ ID NO: 1. If the intended limitation is “polynucleotide encoding the protein that comprises SEQ ID NO: 1”, the claim should be amended accordingly. For examination purposes, it will be assumed that claim 5 is a duplicate of claim 1. Correction is required.
When amending the claims, applicant is advised to carefully review all examined claims and make the necessary changes to ensure proper antecedent basis and dependency.
Claim Rejections - 35 USC § 112(a) or First Paragraph (pre-AIA )
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 1-5 are 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
As stated in MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow. Claims 1-5 require a genus of unknown modifications made to a recombinant Corynebacterium cell to reduce the activity of a protein that comprises SEQ ID NO: 1 as well as a genus of unknown modifications made to a recombinant Corynebacterium cell to reduce the activity of a genus of proteins having any structure which can repress the production of arginine. See Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA ) for claim interpretation.
In University of California v. Eli Lilly & Co., 43 USPQ2d 1938, the Court of Appeals for the Federal Circuit has held that “A written description of an invention involving a chemical genus, like a description of a chemical species, ‘requires a precise definition, such as by structure, formula, [or] chemical name,’ of the claimed subject matter sufficient to distinguish it from other materials”. As indicated in MPEP § 2163, 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, reduction to drawings, 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 that Applicant was in possession of the claimed genus. In addition, MPEP § 2163 states that a representative number of species means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
There is no structural limitation with regard to the members of the genus of proteins that can repress the production of arginine in any Corynebacterium cell. While the specification in the instant application discloses the structure of an arginine repressor protein that comprises SEQ ID NO: 13, it provides no clue as to the structural elements required in any protein that can directly or indirectly repress the production of arginine in any Corynebacterium cell. No disclosure of a structure/function correlation has been provided which would allow one of skill in the art to recognize which variants of the polypeptide of SEQ ID NO: 13 can repress the synthesis of arginine in any Corynebacterium cell. In addition, there is no limit with regard to the genus of modifications that can be made to a recombinant Corynebacterium cell for such cell to have reduced expression/activity of the protein of SEQ ID NO: 1, or to reduce the activity/expression of any protein that can repress the production of arginine in a Corynebacterium cell.
The claims require a potentially large genus of unknown methods to reduce the activity/expression of a gene or protein encoded by said gene, such as (a) mutations in the regulatory region of a gene encoding the protein of interest, (b) mutations in the coding region of a gene encoding the protein of interest such that the desired activity is no longer displayed, (c) the expression of unknown genes which encode proteins that act as expression repressors, (d) the use of compounds that could decrease the expression of a gene, (e) the use of antisense nucleic acids of unknown structure that would block expression of the desired genes, and (f) the use of antisense nucleic acids of unknown structure that block the expression of unknown genes encoding inducers of the genes encoding the recited proteins. While the specification discloses the disruption of a gene as a genetic modification to decrease or eliminate the activity of a protein, the specification is silent with regard to other modifications to decrease the activity of a protein as required by the claims.
The claims encompass a large genus of proteins that can repress the production of arginine which are structurally unrelated A sufficient written description of a genus of polypeptides may be achieved by a recitation of a representative number of polypeptides defined by their amino acid sequence or a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. However, in the instant case, there is no recited structural feature which is representative of all the members of the genus of proteins recited in the claim. Furthermore, while one could argue that the one species disclosed is representative of the structure of all the members of the genus, it is noted that the art teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate (Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol. 183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98% amino acid sequence identity catalyze two different reactions: deamination and dehalogenation, therefore having different function. Therefore, since minor structural differences may result in changes affecting function, and no additional information correlating structure with the desired functional characteristics has been provided, one cannot reasonably conclude that the one species disclosed is representative of the structure of all the proteins that can repress production of arginine required by the claims.
Due to the fact that the specification only discloses one species of the genus of proteins required by the claimed microorganisms, and a limited number of methods to achieve the desired decrease in activity, one of skill in the art would not recognize from the disclosure that Applicant was in possession of the claimed invention.
Claims 1-5 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a recombinant C. glutamicum cell that comprises a disruption in an endogenous gene that encodes the protein of SEQ ID NO: 1, and the endogenous argR gene that encodes the protein of SEQ ID NO: 13, does not reasonably provide enablement for recombinant Corynebacterium microorganisms modified by any means to reduce the acetyltransferase activity of the polypeptide of SEQ ID NO: 1 and to reduce the activity of any arginine repressor. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2nd 1400 (Fed. Cir. 1988)) as follows: 1) quantity of experimentation necessary, 2) the amount of direction or guidance presented, 3) the presence and absence of working examples, 4) the nature of the invention, 5) the state of prior art, 6) the relative skill of those in the art, 7) the predictability or unpredictability of the art, and 8) the breadth of the claims. The factors which have led the Examiner to conclude that the specification fails to teach how to make and/or use the claimed invention without undue experimentation, are addressed in detail below.
The breadth of the claims. Claims 1-5 broadly encompass unknown modifications made to a recombinant Corynebacterium cell to reduce the activity of a protein that comprises SEQ ID NO: 1 as well as unknown modifications made to a recombinant Corynebacterium cell to reduce the activity of a genus of proteins having any structure which can repress the production of arginine. See Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA ) for claim interpretation.
The enablement provided is not commensurate in scope with the claims due to the lack of information regarding the structural elements required in any protein that can repress the production of arginine in a Corynebacterium cell, and the lack of information regarding those modifications required in any Corynebacterium to reduce the activity of a protein that comprises SEQ ID NO: 1 as well as that of proteins having any structure which can repress the production of arginine. In the instant case, the specification enables a recombinant C. glutamicum cell that comprises a disruption in an endogenous gene that encodes the protein of SEQ ID NO: 1, and the endogenous argR gene that encodes the protein of SEQ ID NO: 13.
The amount of direction or guidance presented and the existence of working examples. The specification the disruption of the gene encoding the protein of SEQ ID NO: 1 and the disruption of the gene encoding the protein of SEQ ID NO: 3 in C. glutamicum as a working example. However, the specification fails to provide any clue as to the structural elements required in any protein that is able to repress the production of arginine in any Corynebacterium cell, or the structural elements within the polypeptide of SEQ ID NO: 13 which are associated with the ability to repress the production of arginine.
No correlation between structure and function has been presented to determine which Corynebacterium proteins can act as repressors of arginine production. In addition, the specification fails to disclose other methods to decrease the expression/activity of a protein. The specification is completely silent with regard to the structural elements in the regulatory region of the genes encoding the recited proteins that need to be modified to obtain changes in expression, the modifications that can be made to a protein to reduce its activity, or the structure of antisense molecules that can block the expression of the recited proteins or the expression of proteins which are inducers of the expression of the desired proteins, or the structure/identity of compounds that could be used to inhibit expression of the protein of interest or the activity of the protein of interest.
The state of prior art, the relative skill of those in the art, and the predictability or unpredictability of the art. The amino acid sequence of a protein determines the structural and functional properties of said protein. While the art discloses the repressor of SEQ ID NO: 13, neither the specification nor the art provide a correlation between structure and function such that one of skill in the art can envision the structure of any variant of the protein of SEQ ID NO: 13 having the ability to repress the production of arginine in a Corynebacterium cell. Neither the specification nor the art provide additional information as to the structural elements in the regulatory regions of the recited genes which can be modified to decrease expression, or how these structural elements should be modified to obtain the desired level of expression. In addition, neither the specification nor the art provide any information as to the structure of transcription modulators of the recited genes, such as proteins, chemical compounds or nucleic acids that can modulate expression or the activity of the protein of interest.
While the argument can be made that the structure/identity of those proteins required by the claims can be obtained by structural homology, the art clearly teaches that (i) there is a high level of unpredictability associated with accurate functional annotation of proteins based solely on structural homology, and (ii) modification of a protein’s amino acid sequence to obtain the desired activity without any guidance/knowledge as to which amino acids in a protein are tolerant of modification and which ones are conserved is highly unpredictable. For example, Singh et al. (Current Protein and Peptide Science 19(1):5-15, 2018) disclose different protein engineering approaches and state that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility and conformational changes (page 11, left column, last paragraph). Sadowski et al. (Current Opinion in Structural Biology 19:357-362, 2009) teach that much of the problem in assigning function from structure comes from functional convergence, where although a stable structure is required to perform many functions it is not always necessary to adopt a particular structure to carry out a particular function (page 357, right column, first full paragraph). Sadowski et al. further explain that the unexpected and significant difficulties of predicting function from structure show that the potential of structural models for providing novel functional annotations has not yet fully realized. Sadowski et al. also states that while a few successes have been achieved which required manual intervention, the ability to vary the requirements for specificity in prediction means that it is difficult to determine how useful the end result may be for the user (page 361, left column, first full paragraph). The teachings of Singh et al. and Sadowski et al. are further supported by the teachings of Witkowski et al., Tang et al. and Seffernick et al. already discussed above, where it is shown that even small amino acid changes result in unpredictable enzymatic activity changes.
As taught in the art, prokaryotes achieve gene transcription and translation regulation by means of a series of complex mechanisms. Zhou et al. (Cell Mol Life Sci 63(19-20):2260-2290, 2006) teach that a gene in a cell may be regulated by different transcription factors and the contribution from different transcription factors may function under different conditions (page 2283, left column, lines 12-22). Zhou et al. also teach that the relationship between transcription factors and genes may be much more complex than we imagine and states that data from mRNA expression and transcription factor-DNA interactions give only limited information that does not include post-transcriptional events or protein-protein interactions. Kozak (Gene 234:187-208, 1999) while describing the principles of protein synthesis states that the details of translational regulation are unique to each mRNA, and thus too complicated to be included in a review of basic mechanisms (page 187, right column, last line-page 188, left column, line 4). Thus, the art appears to suggest the unpredictability of determining the factors which would lead to expression modulation for a specific gene without further experimentation.
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification. While methods of generating or isolating variants of a polypeptide as well as enzymatic/functional assays were known in the art at the time of the invention, it was not routine in the art to screen by a trial and error process for an essentially infinite number of proteins to find those having the desired activity. In the absence of (i) a rational and predictable scheme for selecting those proteins most likely to have the desired functional features, and/or (ii) a correlation between structure and the desired activity, one of skill in the art would have to test an essentially infinite number of proteins to determine which ones have the desired functional characteristics. Similarly, while methods of altering the structure of a nucleic acid and detecting changes in expression were known in the art at the time of the invention, it was not routine in the art to screen by a trial and error process for all possible proteins, chemical compounds or nucleic acids which can serve as transcription repressors of genes or inhibitors of activity, or all possible mutations in the regulatory or coding region of a gene to determine which ones result in decrease expression or activity of the desired protein. In the absence of a rational and predictable scheme for selecting those genetic modifications, proteins, chemical compounds or nucleic acids that would result in the decrease of expression/activity of the desired gene or protein encoded by said gene, one of skill in the art would have to test an essentially infinite number of genes, proteins, compounds and genetic modifications to enable the entire scope of the claimed invention.
Therefore, taking into consideration the extremely broad scope of the claim, the lack of guidance, the amount of information provided, the lack of knowledge about a correlation between structure and the desired function, the high degree of unpredictability of the prior art in regard to structural changes and their effect on function, and the high degree of unpredictability of the prior art in regard to gene expression regulation, one of ordinary skill in the art would have to go through the burden of undue experimentation in order to practice the claimed invention. Thus, Applicant has not provided sufficient guidance to enable one of ordinary skill in the art to make and use the invention in a manner reasonably correlated with the scope of the claims.
Claim Rejections - 35 USC § 102 (AIA )
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 1-3, 5 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Choi et al. (U.S. Publication No. 2015/0104838 published 4/16/2015).
Claims 1-3 and 5 as interpreted are directed in part to a C. glutamicum cell that has been modified to delete a gene encoding the protein of SEQ ID NO: 1, wherein said C. glutamicum produces L-arginine. See Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA ) for claim interpretation.
Choi et al. teach a Corynebacterium in which the activity of the acetyltransferase NCgl1469 that comprises SEQ ID NO: 20 is weakened (paragraphs [0011]-[0014]; page 24, claim 20). The protein of SEQ ID NO: 20 is identical to the protein of SEQ ID NO: 1 of the instant application. See alignment below. Choi et al. teach that weakening of the activity is obtained by deleting a part or all of a polynucleotide encoding the protein (paragraph [0018]). Choi et al. teach that the Corynebacterium is C. glutamicum (paragraph [0040]). Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of Choi et al. would also produce arginine. In addition, since the specification asserts that deleting a gene encoding the protein of SEQ ID NO: 1 in C. glutamicum, which is identical to the protein of SEQ ID NO: 20 of Choi et al., would result in an increase in the production of arginine, it follows that the C. glutamicum of Choi et al. would also produce more arginine than the same C. glutamicum cell lacking the deletion. Therefore, the teachings of Choi et al. anticipate the instant claims as written/interpreted.
SEQ ID NO: 1
RESULT 1
US-14-372-000A-20
Sequence 20, US/14372000A
Publication No. US20150104838A1
GENERAL INFORMATION
APPLICANT: CHOI, Su Jin
APPLICANT: CHOI, Hyang
APPLICANT: KANG, Min Sun
APPLICANT: JHON, Sung Hoo
APPLICANT: LEE, Kyoung Min
APPLICANT: UM, Hye Won
APPLICANT: YANG, Young Lyeol
TITLE OF INVENTION: Recombinant Microorganisms with an Improved Productivity of
TITLE OF INVENTION: Putrescine and Method for Producing Putrescine Using the Same
FILE REFERENCE: HANO-031/00US
CURRENT APPLICATION NUMBER: US/14/372,000A
CURRENT FILING DATE: 2014-07-11
PRIOR APPLICATION NUMBER: PCT/KR2013/000263
PRIOR FILING DATE: 2013-01-11
PRIOR APPLICATION NUMBER: KR 10-2012-0003634
PRIOR FILING DATE: 2012-01-11
NUMBER OF SEQ ID NOS: 27
SEQ ID NO 20
LENGTH: 203
TYPE: PRT
ORGANISM: Corynebacterium glutamicum
Query Match 100.0%; Score 1059; Length 203;
Best Local Similarity 100.0%;
Matches 203; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MSPTVLPATQADFPKIVDVLVEAFANDPAFLRWIPQPDPGSAKLRALFELQIEKQYAVAG 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MSPTVLPATQADFPKIVDVLVEAFANDPAFLRWIPQPDPGSAKLRALFELQIEKQYAVAG 60
Qy 61 NIDVARDSEGEIVGVALWDRPDGNHSAKDQAAILPRLVSIFGIKAAQVAWTDLSSARFHP 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 NIDVARDSEGEIVGVALWDRPDGNHSAKDQAAILPRLVSIFGIKAAQVAWTDLSSARFHP 120
Qy 121 KFPHWYLYTVATSSSARGTGVGSALLNHGIARAGDEAIYLEATSTRAAQLYNRLGFVPLG 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 KFPHWYLYTVATSSSARGTGVGSALLNHGIARAGDEAIYLEATSTRAAQLYNRLGFVPLG 180
Qy 181 YIPSDDDGTPELAMWKPPAMPTV 203
|||||||||||||||||||||||
Db 181 YIPSDDDGTPELAMWKPPAMPTV 203
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 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.
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 1-3 and 5 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over (i) claims 1-9 of U.S. Patent No. 9,677,099, (ii) claims 6-7 of U.S. Patent No. 10,221,433, (iii) claims 4-5 of U.S. Patent No. 9,657,264, (iv) claims 2-3 of U.S. Patent No. 10,633,679, (v) claims 2-3 of U.S. Patent No. 10,640,797, (vi) claims 11-12 of U.S. Patent No. 11,053,525, (vii) claims 12-13 of U.S. Patent No. 10,640,753, (viii) claims 2-3 of U.S. Patent No. 10,640,798, (ix) claim 3 of U.S. Patent No. 11,124,812, (x) claims 2-3 of U.S. Patent No. 10,626,425, and (xi) claims 6-7 of U.S. Patent No. 11,268,074. Although the conflicting claims are not identical, they are not patentably distinct from each other for the following reasons.
Claims 1-3 and 5 as interpreted are directed in part to C. glutamicum cell that has been modified to delete an endogenous gene encoding the protein of SEQ ID NO: 1, wherein said C. glutamicum produces L-arginine. See Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA ) for claim interpretation.
Claims 1-9 of U.S. Patent No. 9,677,099 are directed in part to a C. glutamicum cell that has been modified to delete an endogenous gene encoding the protein of SEQ ID NO: 20. The protein of SEQ ID NO: 20 is identical to the protein of SEQ ID NO: 1 of the instant application. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 1-9 of U.S. Patent No. 9,677,099 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are anticipated by the cell of claims 1-9 of U.S. Patent No. 9,677,099.
Claims 6-7 of U.S. Patent No. 10,221,433 are directed in part to a recombinant microorganism having a disruption (i.e., deletion) of an endogenous gene encoding an acetyltransferase that comprises SEQ ID NO: 32. The protein of SEQ ID NO: 32 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by claim 9 of U.S. Patent No. 10,221,433, the preferred recombinant microorganism is a C. glutamicum cell. Therefore, it follows that the recombinant microorganism of claim 7 of U.S. Patent No. 10,221,433 is a C. glutamicum cell. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 6-7 of U.S. Patent No. 10,221,433 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 6-7 of U.S. Patent No. 10,221,433.
Claims 4-5 of U.S. Patent No. 9,657,264 are directed in part to a Corynebacterium cell which has been modified to inactivate an endogenous putrescine acetyltransferase that comprises SEQ ID NO: 16. The polypeptide of SEQ ID NO: 16 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by claim 6 of U.S. Patent No. 9,657,264, the preferred recombinant microorganism is a C. glutamicum cell. Therefore, it follows that the recombinant microorganism of claim 5 of U.S. Patent No. 9,657,264 is a C. glutamicum cell. The specification of U.S. Patent No. 9,657,264 discloses deletion as a preferred mode for inactivating the putrescine acetyltransferase. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 4-5 of U.S. Patent No. 9,657,264 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 4-5 of U.S. Patent No. 9,657,264.
Claims 2-3 of U.S. Patent No. 10,633,679 are directed in part to a microorganism that has been modified to weaken the activity of a diamine acetyltransferase that comprises SEQ ID NO: 12. The protein of SEQ ID NO: 12 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by the specification of U.S. Patent No. 10,633,679, the preferred recombinant microorganism is a C. glutamicum cell. Therefore, it follows that the recombinant microorganism of claim 3 of U.S. Patent No. 10,633,679 is a C. glutamicum cell. The specification of U.S. Patent No. 10,633,679 discloses deletion as a preferred mode for weakening the diamine acetyltransferase. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 2-3 of U.S. Patent No. 10,633,679 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 2-3 of U.S. Patent No. 10,633,679.
Claims 2-3 of U.S. Patent No. 10,640,797 are directed in part to a recombinant microorganism which has been modified to weaken an endogenous diamine acetyltransferase that comprises SEQ ID NO: 13. The polypeptide of SEQ ID NO: 13 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by the specification of U.S. Patent No. 10,640,797, the preferred recombinant microorganism is a C. glutamicum cell. Therefore, it follows that the recombinant microorganism of claim 3 of U.S. Patent No. 10,640,797 is a C. glutamicum cell. The specification of U.S. Patent No. 10,640,797 discloses deletion as a preferred mode for weakening the diamine acetyltransferase. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 2-3 of U.S. Patent No. 10,640,797 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 2-3 of U.S. Patent No. 10,640,797.
Claims 11-12 of U.S. Patent No. 11,053,525 are directed in part to a recombinant Corynebacterium cell which has been modified to weaken an endogenous acetyltransferase that comprises SEQ ID NO: 37. The polypeptide of SEQ ID NO: 37 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by claim 3 of U.S. Patent No. 11,053,525, the preferred recombinant Corynebacterium cell is a C. glutamicum cell. Therefore, it follows that the recombinant Corynebacterium cell of claim 12 of U.S. Patent No. 11,053,525 is a C. glutamicum cell. The specification of U.S. Patent No. 11,053,525 discloses deletion as a preferred mode for weakening the acetyltransferase. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 11-12 of U.S. Patent No. 11,053,525 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 11-12 of U.S. Patent No. 11,053,525.
Claims 12-13 of U.S. Patent No. 10,640,753 are directed in part to a recombinant Corynebacterium cell which has been modified to weaken an endogenous acetyltransferase that comprises SEQ ID NO: 31. The polypeptide of SEQ ID NO: 31 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by claim 4 of U.S. Patent No. 10,640,753, the preferred recombinant Corynebacterium cell is a C. glutamicum cell. Therefore, it follows that the recombinant Corynebacterium cell of claim 13 of U.S. Patent No. 10,640,753 is a C. glutamicum cell. The specification of U.S. Patent No. 10,640,753 discloses deletion as a preferred mode for weakening the acetyltransferase. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 12-13 of U.S. Patent No. 10,640,753 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 12-13 of U.S. Patent No. 10,640,753.
Claims 2-3 of U.S. Patent No. 10,640,798 are directed in part to a recombinant microorganism which has been modified to weaken an endogenous diamine acetyltransferase that comprises SEQ ID NO: 13. The polypeptide of SEQ ID NO: 13 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by the specification of U.S. Patent No. 10,640,798, the preferred recombinant microorganism is a C. glutamicum cell. Therefore, it follows that the recombinant microorganism of claim 3 of U.S. Patent No. 10,640,798 is a C. glutamicum cell. The specification of U.S. Patent No. 10,640,798 discloses deletion as a preferred mode for weakening the diamine acetyltransferase. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 2-3 of U.S. Patent No. 10,640,798 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 2-3 of U.S. Patent No. 10,640,798.
Claim 3 of U.S. Patent No. 11,124,812 is directed in part to a recombinant C. glutamicum cell that has been modified to inactivate an endogenous gene encoding a putrescine acetyltransferase. The specification of U.S. Patent No. 11,124,812 disclose the protein of SEQ ID NO: 19 as a preferred embodiment of the genus of putrescine acetyltransferases encoded by the gene to be inactivated. The protein of SEQ ID NO: 19 is identical to the polypeptide of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Therefore, claim 3 encompasses a recombinant C. glutamicum cell that has been modified to inactivate a gene encoding the putrescine acetyltransferase of SEQ ID NO: 19. In addition, the specification of U.S. Patent No. 11,124,812 discloses gene deletion as a preferred mode to inactivate the gene. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claim 3 of U.S. Patent No. 11,124,812 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the C. glutamicum cell of claim 3 of U.S. Patent No. 11,124,812.
Claims 2-3 of U.S. Patent No. 10,626,425 are directed in part to a recombinant microorganism which has been modified to weaken an endogenous diamine acetyltransferase that comprises SEQ ID NO: 12. The polypeptide of SEQ ID NO: 12 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by the specification of U.S. Patent No. 10,626,425, the preferred recombinant microorganism is a C. glutamicum cell. Therefore, it follows that the recombinant microorganism of claim 3 of U.S. Patent No. 10,626,425 is a C. glutamicum cell. The specification of U.S. Patent No. 10,626,425 discloses deletion as a preferred mode for weakening the diamine acetyltransferase. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 2-3 of U.S. Patent No. 10,626,425 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 2-3 of U.S. Patent No. 10,626,425.
Claims 6-7 of U.S. Patent No. 11,268,074 are directed in part to a recombinant Corynebacterium cell which has been modified to weaken an endogenous acetyltransferase that comprises SEQ ID NO: 31. The polypeptide of SEQ ID NO: 31 is identical to the protein of SEQ ID NO: 1 of the instant application. As evidenced by the instant application, the protein of SEQ ID NO: 1 is found endogenously in C. glutamicum. Moreover, as evidenced by claim 3 of U.S. Patent No. 11,268,074, the preferred recombinant Corynebacterium cell is a C. glutamicum cell. Therefore, it follows that the recombinant Corynebacterium cell of claim 7 of U.S. Patent No. 11,268,074 is a C. glutamicum cell. The specification of U.S. Patent No. 11,268,074 discloses deletion as a preferred mode for weakening the acetyltransferase. Since C. glutamicum produces all 20 amino acids, it follows that the C. glutamicum of claims 6-7 of U.S. Patent No. 11,268,074 would also produce arginine. Therefore, the C. glutamicum cell of claims 1-3 and 5 of the instant application are either anticipated or render obvious by the cell of claims 6-7 of U.S. Patent No. 11,268,074.
Conclusion
No claim is in condition for allowance.
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Any inquiry concerning this communication or earlier communications from the examiner should be directed to DELIA M RAMIREZ, Ph.D., whose telephone number is (571) 272-0938. The examiner can normally be reached on Monday-Friday from 8:30 AM to 5:00 PM. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert B. Mondesi, can be reached at (408) 918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
/DELIA M RAMIREZ/Primary Examiner, Art Unit 1652
DR
May 23, 2026
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