DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Priority
The present application is a § 371 National Stage Entry of PCT/KR2022/007225 (filed on 05/20/2022) and claims priority to Korean application KR10-2021-0065740 (filed on 05/21/2021).
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 02/24/2026 is in compliance with the provisions of 37 C.F.R. 1.97. All references cited in this IDS have been fully considered.
Amendments
Claims 2-3 are canceled.
Claims 4-5 and 12 now depend from claim 1.
Claims 13-23 are newly added.
Claim Objections
Claims 1, 4-5, 12, 16, 18-20, and 22-23 are objected to because the gene pitA should be italicized.
Claim 4 is objected to because the taxonomic name Escherichia coli should be fully established when first used in the claims and the full name should be italicized.
Claim 10 is objected to because the semicolons delineating each element should be replaced with commas.
Claim 16 is objected to because the taxonomic name E. coli should be italicized and a period should be added before “E”.
Appropriate correction is required.
Duplicate Claim Warning
Applicant is advised that should claim 9 be found allowable, claim 17 will be objected to under 37 CFR 1.75 as being a substantial duplicate thereof. When two claims in an application are duplicates or else are so close in content that they both cover the same thing, despite a slight difference in wording, it is proper after allowing one claim to object to the other as being a substantial duplicate of the allowed claim. See MPEP § 608.01(m). Specifically, claims 9 and 17 are identical.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
RE: Applicant’s Arguments
Applicant has not argued the merits of the rejections of record but instead argues that the claims, as amended, are nonobvious over Hirano (or Hirano in view of Lee) because the claims have been amended to “better capture commercial embodiments” (Remarks, p. 5, par. 2).
Specifically, applicant asserts that (i) the claimed invention exhibits unexpected results and (ii) the cited references do not teach or suggest the claimed purine nucleotide production.
Applicant’s arguments have been fully considered but are not sufficient to overcome the teachings of Hirano (or Hirano in view of Lee) for the following reasons.
With respect to the first argument, applicant has asserted that the Corynebacterium stationis microorganism exhibits an unexpectedly superior increase in purine nucleotide production. Namely, applicant provides a table which allegedly demonstrates that introduction of E. coli-derived pitA into strain #971 increases XMP yield 1.5% whereas introducing pitB only increased yield by 0.01%. These data were provided in the Lee declaration filed concurrent with applicant’s response.
On its face, this declaration merely seeks to demonstrate that enhanced 5’-xanthosine monophosphate (XMP) production is derived from the pitA rather than pitB gene. However, neither this declaration nor applicant’s arguments filed therewith are sufficient to establish an unexpected or remarkable result. As discussed in the rejection of record, applicant’s specification admits that “[t]he purine nucleotide production ability may be a trait of the wild-type strain of the Corynebacterium stationis microorganism” (p. 21, par. 1). Any differences between the claimed invention and the prior art may be expected to result in some differences in properties (MPEP § 716.02). The issue is whether the properties differ to such an extent that the difference is really unexpected (Id.).
Hirano teaches improving the activity of the Pit system such as by increasing the activity of the PitA protein which is the pitA gene product (col. 20, lines 45-48), teaches that the modified Corynebacterium bacterium can be Corynebacterium stationis (col. 5, lines 21-29), and teaches that the pitA gene can be from Escherichia coli (col. 20, lines 49-61). Thus, although Hirano is directed to improving L-amino acid production by improving the phosphate transporter system, it nonetheless renders obvious arriving at a Corynebacterium stationis microorganism in which the activity of a polypeptide encoded by pitA gene is enhanced as compared with endogenous activity, and wherein the pitA gene is a foreign pitA gene.
In light of this teaching, the relevant analysis is whether it is unexpected or remarkable that Hirano’s proposed modification to C. stationis improved purine nucleotide production ability. But before this analysis can be performed, it has to be determined whether the strain “having increased purine nucleotide production ability” inherently possesses this characteristic.
"[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer." Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Therefore, because Hirano renders obvious the same composition (a Corynebacterium stationis microorganism in which the activity of a polypeptide encoded by pitA gene is enhanced as compared with endogenous activity, and wherein the pitA gene is a foreign pitA gene) and the claim differs only in that it states that the bacterium has “increased purine nucleotide production ability”, the amended “microorganism” claim is obvious over Hirano as being inherent to its teachings.
In the interest of prosecution, applicant’s allegation of remarkable or unexpected results has been fully considered. Assuming arguendo that the art of record does not teach or render obvious the claimed inventions, the evidence relied upon should establish "that the differences in results are in fact unexpected and unobvious and of both statistical and practical significance." (MPEP § 716.02(b)(I)). Applicant has the burden of explaining how their data provides evidence of non-obviousness (MPEP § 716.02(b)(II)). Applicant’s response is not sufficient to establish an unexpected or remarkable result because (1) they have not demonstrated how a 1.5% increase in XMP yield is unexpected based upon the art of record, (2) even if this burden has been met, they have not demonstrated statistical significance, (3) even if statistical significance has been met, they have not demonstrated how improving XMP yield by 1.5% is practically significant, and (4) even if each of the above burdens have been met, the claim is not commensurate because applicant’s evidence only supports an increase in XMP not a generic increase in “purine nucleotide production”. Finally, even if the above demonstrations of a remarkable result have been met, the next appropriate analysis would be if the evidence is unexpected. The result cannot be considered to be unexpected because it was known, before the effective filing date, that improving Corynebacterium phosphate importer activity increases the production of purine nucleotides (Lee et al., KR102185850 B1; See attached English Machine Translation; p. 5, par. 4). In the context of Lee, “phosphate importer” means a protein having a function of absorbing phosphoric acid into cells, which is mainly absorbed in the form of inorganic orthophosphate” (p. 2, par. 8). Thus, the observed improvement in purine nucleotide production would have been expected because (1) Hirano teaches enhancing the activity of PitA encoded by pitA and (2) Lee teaches that improving phosphate importer activity increases the production of purine nucleotides.
With respect to applicant’s second argument, applicant asserts that Hirano is directed to methods for producing L-amino acids and neither teaches nor suggests increasing purine nucleotide production through enhancement of pitA activity or introduction of a foreign pitA gene. Applicant asserts that Lee does not cure this deficiency.
As discussed above, Hirano renders obvious the same bacterium (a Corynebacterium stationis microorganism in which the activity of a polypeptide encoded by pitA gene is enhanced as compared with endogenous activity, and wherein the pitA gene is a foreign pitA gene) and differs only in that it did not recognize an inherent improvement in purine production. Therefore, there is no requirement that Hirano teach or suggest purine nucleotide production because the claims are merely descriptive of an unappreciated property of Hirano’s composition. And even if the prior art was required to make such a finding, the increased purine production is obvious over Hirano in view of Lee for the reasons discussed above.
For at least these reasons, the amended claims are unpatentable over Hirano or Hirano in view of Lee. In order to address applicant’s amendments to the claims and the newly added claims, the rejections of record have been withdrawn and new grounds of rejection are made below.
Claims 1, 4-6, 10, and 12-15 are rejected under 35 U.S.C. 103 as being unpatentable over Hirano et al. (US 9,506,094 B2).
Hirano teaches a method for producing an L-amino acid by culturing a coryneform bacterium having an L-amino acid-producing ability, which is modified so that the activity of a phosphate transporter is increased (abstract). Specifically, Hirano teaches increasing the activity by increasing expression of a gene coding for the phosphate transporter (col. 2, lines 15-18) and more specifically teaches the modification of the pitA gene.
Regarding claim 1, among the list of useful bacteria taught by Hirano is Corynebacterium stationis (col. 5, lines 16-17 and lines 21-29). Hirano additionally teaches that the bacterium can be modified so that the phosphate transporter activity is increased (col. 20, lines 15-16) and it is exemplary to increase the activity of the Pit system, specifically the activity of the PitA protein which is the pitA gene product (col. 20, lines 45-48). Hirano teaches specific pitA genes which can be used from a litany of microorganisms including Escherichia coli, Panteoea ananatis, and Corynebacterium glutamicum (col. 20, line 49 through col. 21, line 25).
Accordingly, Hirano renders obvious a Corynebacterium stationis microorganism in which the activity of a polypeptide encoded by pitA gene is enhanced as compared with endogenous activity, and wherein the pitA gene is a foreign pitA gene.
Hirano differs only in that it does not suggest that this modification results in a microorganism “having increased purine nucleotide production ability”.
Nonetheless, because Hirano renders obvious the same composition, the trait of “having increased purine nucleotide production ability” is inherent to Hirano’s obvious composition. "[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer." (MPEP § 2112(I)) and “[t]here is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the relevant time, but only that the subject matter is in fact inherent in the prior art reference” (MPEP § 2112(II)).
Thus, despite Hirano’s silence as to the effects on purine production associated with pitA upregulation, the microorganism is obvious over Hirano.
Regarding claim 4, as discussed above, Hirano renders obvious the use of a pitA gene derived from E. coli.
Regarding claims 5 and 12, as discussed above, Hirano renders obvious the use of a pitA gene derived from E. coli. As shown below, SEQ ID NO: 1 has 100% identity to Hirano’s SEQ ID NO: 2 (Amino acid sequence of PitA protein of E. coli MG1655; col. 40, lines 41-42; col 43-48).
Alignment 1
Identities 499 / 499 (100%)
Positives 499 / 499 (100%)
Query
1
MLHLFAGLDL HTGLLLLLAL AFVLFYEAIN GFHDTANAVA TVIYTRAMRS
50
MLHLFAGLDL HTGLLLLLAL AFVLFYEAIN GFHDTANAVA TVIYTRAMRS
Hit
1
MLHLFAGLDL HTGLLLLLAL AFVLFYEAIN GFHDTANAVA TVIYTRAMRS
50
Query
51
QLAVVMAAVF NFLGVLLGGL SVAYAIVHML PTDLLLNMGS SHGLAMVFSM
100
QLAVVMAAVF NFLGVLLGGL SVAYAIVHML PTDLLLNMGS SHGLAMVFSM
Hit
51
QLAVVMAAVF NFLGVLLGGL SVAYAIVHML PTDLLLNMGS SHGLAMVFSM
100
Query
101
LLAAIIWNLG TWYFGLPASS SHTLIGAIIG IGLTNALMTG TSVVDALNIP
150
LLAAIIWNLG TWYFGLPASS SHTLIGAIIG IGLTNALMTG TSVVDALNIP
Hit
101
LLAAIIWNLG TWYFGLPASS SHTLIGAIIG IGLTNALMTG TSVVDALNIP
150
Query
151
KVLSIFGSLI VSPIVGLVFA GGLIFLLRRY WSGTKKRARI HLTPAEREKK
200
KVLSIFGSLI VSPIVGLVFA GGLIFLLRRY WSGTKKRARI HLTPAEREKK
Hit
151
KVLSIFGSLI VSPIVGLVFA GGLIFLLRRY WSGTKKRARI HLTPAEREKK
200
Query
201
DGKKKPPFWT RIALILSAIG VAFSHGANDG QKGIGLVMLV LIGVAPAGFV
250
DGKKKPPFWT RIALILSAIG VAFSHGANDG QKGIGLVMLV LIGVAPAGFV
Hit
201
DGKKKPPFWT RIALILSAIG VAFSHGANDG QKGIGLVMLV LIGVAPAGFV
250
Query
251
VNMNATGYEI TRTRDAINNV EAYFEQHPAL LKQATGADQL VPAPEAGATQ
300
VNMNATGYEI TRTRDAINNV EAYFEQHPAL LKQATGADQL VPAPEAGATQ
Hit
251
VNMNATGYEI TRTRDAINNV EAYFEQHPAL LKQATGADQL VPAPEAGATQ
300
Query
301
PAEFHCHPSN TINALNRLKG MLTTDVESYD KLSLDQRSQM RRIMLCVSDT
350
PAEFHCHPSN TINALNRLKG MLTTDVESYD KLSLDQRSQM RRIMLCVSDT
Hit
301
PAEFHCHPSN TINALNRLKG MLTTDVESYD KLSLDQRSQM RRIMLCVSDT
350
Query
351
IDKVVKMPGV SADDQRLLKK LKSDMLSTIE YAPVWIIMAV ALALGIGTMI
400
IDKVVKMPGV SADDQRLLKK LKSDMLSTIE YAPVWIIMAV ALALGIGTMI
Hit
351
IDKVVKMPGV SADDQRLLKK LKSDMLSTIE YAPVWIIMAV ALALGIGTMI
400
Query
401
GWRRVATTIG EKIGKKGMTY AQGMSAQMTA AVSIGLASYT GMPVSTTHVL
450
GWRRVATTIG EKIGKKGMTY AQGMSAQMTA AVSIGLASYT GMPVSTTHVL
Hit
401
GWRRVATTIG EKIGKKGMTY AQGMSAQMTA AVSIGLASYT GMPVSTTHVL
450
Query
451
SSSVAGTMVV DGGGLQRKTV TSILMAWVFT LPAAVLLSGG LYWLSLQFL
499
SSSVAGTMVV DGGGLQRKTV TSILMAWVFT LPAAVLLSGG LYWLSLQFL
Hit
451
SSSVAGTMVV DGGGLQRKTV TSILMAWVFT LPAAVLLSGG LYWLSLQFL
499
Regarding claims 6 and 13-15, as discussed above, the composition suggested in Hirano inherently possesses increased purine nucleotide production ability. Similarly, the increased purine nucleotides recited in this claim are also inherent to Hirano’s composition.
Regarding claim 10, as discussed above, Hirano teaches a method for producing an L-amino acid comprising a) culturing a coryneform bacterium having an L-amino acid-producing ability in a medium and B) collecting the L-amino acid from the medium, wherein the bacterium has been modified so that the activity of a phosphate transporter is increased (col. 2, lines 4-14).
As Hirano renders obvious the composition of claim 1, it also renders obvious a composition comprising C. stationis microorganism of claim 1. And although the claim recites that the composition is “for producing purine nucleotides”, this is the intended use of the composition and does not impart patentable weight on the composition.
Claims 1, 4-10, and 12-23 are rejected under 35 U.S.C. 103 as being unpatentable over Hirano et al. (US 9,506,094 B2) in view of Lee et al. (KR 102185850 B1; English Machine Translation).
The teachings of Hirano are set forth above and applied herein. Hirano is found to render obvious claims 1, 4-6, 10, and 12-15.
Regarding claims 7 and 20, as discussed above, Hirano teaches a method for producing an L-amino acid comprising a) culturing a coryneform bacterium having an L-amino acid-producing ability in a medium and B) collecting the L-amino acid from the medium, wherein the bacterium has been modified so that the activity of a phosphate transporter is increased (col. 2, lines 4-14).
Among the list of useful bacteria taught by Hirano is Corynebacterium stationis (col. 5, lines 16-17 and lines 21-29). Hirano additionally teaches that the bacterium can be modified so that the phosphate transporter activity is increased (col. 20, lines 15-16) and it is exemplary to increase the activity of the Pit system, specifically the activity of the PitA protein which is the pitA gene product (col. 20, lines 45-48). Hirano teaches specific pitA genes which can be used from a litany of microorganisms including Escherichia coli, Panteoea ananatis, and Corynebacterium glutamicum (col. 20, line 49 through col. 21, line 25).
Accordingly, Hirano renders obvious a method comprising culturing the microorganism of claim 1 in a medium.
Hirano differs only in that it does not teach that the method is for producing purine nucleotides (claim 7) or increasing purine nucleotides production (claim 20).
Lee teaches a Corynebacterium stationis strain which produces purine nucleotides (claims) and a method for producing purine nucleotides comprising culturing a microorganism of the genus Corynebacterium that produces nucleotides in a medium (claims). Specifically, Lee seeks to provide a Corynebacterium for producing a purine nucleotide wherein the activity of a phosphate importer is enhanced (p. 2, par. 4). Lee teaches that increasing activity means that it is increased compared to the intrinsic activity and the improvement can be through transformation (p. 3, par. 16). According to Lee, “phosphate importer” means a protein having a function of absorbing phosphoric acid into cells, which is mainly absorbed in the form of inorganic orthophosphate” p. 2, par. 8) and although wild-type microorganisms cannot produce purine nucleotides or can produce very trace amounts, introduction of polypeptides exhibiting the phosphate importer activity and enhancing its activity increases the production of purine nucleotides in microorganisms and it may be meaningful to be able to do it (p. 5, par. 4).
Therefore, because Hirano renders obvious a method of culturing C. stationis having an increased activity of a phosphate importer (PitA through pitA) and because Lee teaches that enhancing phosphate importer activity increases the production of purine nucleotides, it would have been obvious to have modified Hirano’s method such that it is instead directed to a method for producing purine nucleotides. There would have been a reasonable expectation of success because (1) pitA was previously known to be a phosphate importer gene and (2) Lee teaches that improving phosphate importer genes in C. stationis yields increased purine nucleotides when the modified bacterium is cultured in a medium. There would have been particular motivation to make this modification because Lee teaches that the efficient production of purine nucleotides can greatly contribute to cost reduction on industrial scales (p. 6, par. 9). This obviousness is based upon the “Some Teachings, Suggestion, or Motivation in the Prior Art That Would Have Led One of Ordinary Skill To Modify the Prior Art Reference or To Combine Prior Art Reference Teachings To Arrive at the Claimed Invention” rationale set forth in KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395-97 (2007). See MPEP 2143(I)(G).
Thus, claims 7 and 20 are obvious over Hirano in view of Lee.
Regarding claim 8, Lee teaches that the method may include the step of recovering purine nucleotides from the culture medium or microorganism (p. 6, par. 6).
Regarding claims 9, 17, and 21, Lee teaches that the purine nucleotides are 5’inosine monophosphate, 5’ xanthosine monophosphate, and 5’guanosine monophosphate (p. 5, par. 7).
Regarding claim 16, as discussed above, Hirano renders obvious the use of a pitA gene derived from E. coli.
Regarding claims 18-19 and 22-23, as discussed above, Hirano renders obvious the use of a pitA gene derived from E. coli in the method of claim 7. As shown below, SEQ ID NO: 1 has 100% identity to Hirano’s SEQ ID NO: 2 (Amino acid sequence of PitA protein of E. coli MG1655; col. 40, lines 41-42; col 43-48).
Alignment 1
Identities 499 / 499 (100%)
Positives 499 / 499 (100%)
Query
1
MLHLFAGLDL HTGLLLLLAL AFVLFYEAIN GFHDTANAVA TVIYTRAMRS
50
MLHLFAGLDL HTGLLLLLAL AFVLFYEAIN GFHDTANAVA TVIYTRAMRS
Hit
1
MLHLFAGLDL HTGLLLLLAL AFVLFYEAIN GFHDTANAVA TVIYTRAMRS
50
Query
51
QLAVVMAAVF NFLGVLLGGL SVAYAIVHML PTDLLLNMGS SHGLAMVFSM
100
QLAVVMAAVF NFLGVLLGGL SVAYAIVHML PTDLLLNMGS SHGLAMVFSM
Hit
51
QLAVVMAAVF NFLGVLLGGL SVAYAIVHML PTDLLLNMGS SHGLAMVFSM
100
Query
101
LLAAIIWNLG TWYFGLPASS SHTLIGAIIG IGLTNALMTG TSVVDALNIP
150
LLAAIIWNLG TWYFGLPASS SHTLIGAIIG IGLTNALMTG TSVVDALNIP
Hit
101
LLAAIIWNLG TWYFGLPASS SHTLIGAIIG IGLTNALMTG TSVVDALNIP
150
Query
151
KVLSIFGSLI VSPIVGLVFA GGLIFLLRRY WSGTKKRARI HLTPAEREKK
200
KVLSIFGSLI VSPIVGLVFA GGLIFLLRRY WSGTKKRARI HLTPAEREKK
Hit
151
KVLSIFGSLI VSPIVGLVFA GGLIFLLRRY WSGTKKRARI HLTPAEREKK
200
Query
201
DGKKKPPFWT RIALILSAIG VAFSHGANDG QKGIGLVMLV LIGVAPAGFV
250
DGKKKPPFWT RIALILSAIG VAFSHGANDG QKGIGLVMLV LIGVAPAGFV
Hit
201
DGKKKPPFWT RIALILSAIG VAFSHGANDG QKGIGLVMLV LIGVAPAGFV
250
Query
251
VNMNATGYEI TRTRDAINNV EAYFEQHPAL LKQATGADQL VPAPEAGATQ
300
VNMNATGYEI TRTRDAINNV EAYFEQHPAL LKQATGADQL VPAPEAGATQ
Hit
251
VNMNATGYEI TRTRDAINNV EAYFEQHPAL LKQATGADQL VPAPEAGATQ
300
Query
301
PAEFHCHPSN TINALNRLKG MLTTDVESYD KLSLDQRSQM RRIMLCVSDT
350
PAEFHCHPSN TINALNRLKG MLTTDVESYD KLSLDQRSQM RRIMLCVSDT
Hit
301
PAEFHCHPSN TINALNRLKG MLTTDVESYD KLSLDQRSQM RRIMLCVSDT
350
Query
351
IDKVVKMPGV SADDQRLLKK LKSDMLSTIE YAPVWIIMAV ALALGIGTMI
400
IDKVVKMPGV SADDQRLLKK LKSDMLSTIE YAPVWIIMAV ALALGIGTMI
Hit
351
IDKVVKMPGV SADDQRLLKK LKSDMLSTIE YAPVWIIMAV ALALGIGTMI
400
Query
401
GWRRVATTIG EKIGKKGMTY AQGMSAQMTA AVSIGLASYT GMPVSTTHVL
450
GWRRVATTIG EKIGKKGMTY AQGMSAQMTA AVSIGLASYT GMPVSTTHVL
Hit
401
GWRRVATTIG EKIGKKGMTY AQGMSAQMTA AVSIGLASYT GMPVSTTHVL
450
Query
451
SSSVAGTMVV DGGGLQRKTV TSILMAWVFT LPAAVLLSGG LYWLSLQFL
499
SSSVAGTMVV DGGGLQRKTV TSILMAWVFT LPAAVLLSGG LYWLSLQFL
Hit
451
SSSVAGTMVV DGGGLQRKTV TSILMAWVFT LPAAVLLSGG LYWLSLQFL
499
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.
Previous double patenting rejections
RE: Rejection of claims 1-9 and 12 over claims 1, 4, 10-11, and 13 of U.S. Patent Application No. 17/911,876 in view of Hirano.
Applicant asserts that the copending claims are directed to a microorganism having modified GMP synthesis and do not disclose or suggest a microorganism having increase purine nucleotide production resulting from introduction of a foreign pitA gene.
Applicant’s arguments have been fully considered and are sufficient to overcome the rejection of record.
The amended claims require a Corynebacterium stationis having increased purine nucleotide production and a foreign pitA gene. There is no teaching or suggestion in ‘876 or Hirano which would have led one of ordinary skill in the art to further modify the microorganism such that possess a foreign pitA gene.
For at least this reason, the rejection over ‘876 is withdrawn.
RE: Rejection over U.S. Patent Application Nos. 19/484,198, 19/135,750, 19/135,746, 19/135,744, 19/135,742, and 19/126,551 each in view of Hirano.
Applicant asserts that they will address the obviousness-type double patenting rejection upon indication that the claims are otherwise allowable. As the claims are not currently allowable, the rejections must be maintained but have been reconsidered in light of applicant’s amendments to the claims. The provisional rejections over 19/484,198, 19/135,750, 19/135,746, 19/135,744, 19/135,742, and 19/125,551 are withdrawn.
RE: Rejection of claims 1-10 and 12 over U.S. Patent Application No. 17/296,375 in view of Hirano.
Applicant asserts that the amended claims are nonobvious because ‘375 is directed to a modified microorganism with a pstSCAB operon and does not disclose or suggest microorganisms having increased purine nucleotide production resulting from a foreign pitA gene.
It is noted that ‘375 Issued as U.S. Patent 12,275,972. Accordingly, the rejection of record erroneously cites the application rather than the issued patent.
Nonetheless, applicant’s arguments are not sufficient to overcome the rejection of record.
The instant claims are directed to modified C. stationis having increased purine nucleotide production. Similarly, the claims of the ‘972 patent are directed to methods for producing a purine nucleotide from a modified C. stationis. The claims differ in that the modified microorganism of ‘972 has an enhancement of the pstSCAB operon rather than the pitA gene. The specification can be used as a dictionary to learn the meaning of a term in the claim (MPEP § 804(II)(B)(1)). In this case, the specification of ‘972 teaches that “increase in the activity” may be achieved by introducing a foreign protein or enhancing the activity of an endogenous protein (col. 6, lines 42-45).
As discussed above, Hirano renders obvious a Corynebacterium stationis microorganism in which the activity of a polypeptide encoded by pitA gene is enhanced as compared with endogenous activity, and wherein the pitA gene is a foreign pitA gene. Hirano also teaches that the pitA gene is a phosphate importer gene (abstract).
Accordingly, because ‘972 is directed to methods of producing purine nucleotides including providing a modified C. stationis microorganism wherein the microorganism is modified such that the phosphate importer system is enhanced such as by introducing a foreign protein and because Hirano teaches that foreign pitA can be introduced in C. stationis in order to enhance the phosphate importer system, it would have been obvious to have made this modification in order to arrive at the instant claims.
For at least this reason, rejection over the amended claims is proper and has been applied below.
New grounds of rejection for double patenting
Claims 1, 4-10, and 12-23 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 of U.S. Patent No. 12,275,972 in view of Hirano et al. (US 9,506,094 B2).
The instant claims are directed to modified C. stationis having increased purine nucleotide production. Similarly, the claims of the ‘972 patent are directed to methods for producing a purine nucleotide from a modified C. stationis. The claims differ in that the modified microorganism of ‘972 has an enhancement of the pstSCAB operon rather than the pitA gene. The specification can be used as a dictionary to learn the meaning of a term in the claim (MPEP § 804(II)(B)(1)). In this case, the specification of ‘972 teaches that “increase in the activity” may be achieved by introducing a foreign protein or enhancing the activity of an endogenous protein (col. 6, lines 42-45).
As discussed above, Hirano renders obvious a Corynebacterium stationis microorganism in which the activity of a polypeptide encoded by pitA gene is enhanced as compared with endogenous activity, and wherein the pitA gene is a foreign pitA gene. Hirano also teaches that the pitA gene is a phosphate importer gene (abstract).
Accordingly, because ‘972 is directed to methods of producing purine nucleotides including providing a modified C. stationis microorganism wherein the microorganism is modified such that the phosphate importer system is enhanced such as by introducing a foreign protein and because Hirano teaches that foreign pitA can be introduced in C. stationis in order to enhance the phosphate importer system, it would have been obvious to have modified the methods of ‘972 in order to arrive at microorganisms comprising C. stationis having improved purine production and comprising a foreign pitA gene and methods of use thereof.
Conclusion
No claim is 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.
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/GRANT C CURRENS/Examiner, Art Unit 1651
/MELENIE L GORDON/Supervisory Patent Examiner, Art Unit 1651
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