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 .
DETAILED ACTION
The preliminary amendment filed 09/09/2024 is entered. Claim 12 is cancelled. Claims 1-11 are pending and under consideration in this action.
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. The instant claims are entitled to an effective filing date of 03/06/2023.
Claim Objections
Claim 9 is objected to because of the following informalities:
Claim 9 recites “Corynebacterium glutamicum”, which should be italicized because it is a scientific name.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-11 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 claims contain subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor, at the time the application was filed, had possession of the claimed invention.
The claims are drawn to a genus of protein variants that function as an L-threonine efflux protein. Claim 1 requires an L-threonine efflux protein variant in which the amino acid corresponding to the 133rd position of SEQ ID NO: 1 is substituted with another amino acid. Therefore, claim 1 encompasses any protein that functions as an L-threonine efflux protein and has an amino acid residue that is not glycine at position 133 relative to SEQ ID NO: 1. Claim 2 requires that amino acid at position 133 to be serine, threonine, cysteine, tyrosine, asparagine or glutamine. Claim 3 limits the 133rd residue to serine. However, claims 1-3 do not limit any other structural component of the protein besides residue 133. Claim 4 requires the L-threonine efflux protein variant to have a sequence identity of at least 70% and less than 100% to SEQ ID NO: 1. Since SEQ ID NO: 1 is 206aa in length, claim 4 encompasses up to 62 mutations relative to SEQ ID NO: 1 because 70% of 206aa is 144.2aa and 206-144 is 62. Claim 5 requires a polynucleotide encoding the L-threonine efflux protein variant according to claim 1, but claim 5 does not further limit the structure of that encoded protein. Claim 6 requires a microorganism that comprises the protein of claim 1 or a polynucleotide encoding the same. Claim 7 requires the microorganism to have increased L-threonine productivity compared to a Corynebacterium comprises a wild-type L-threonine efflux protein SEQ ID NO: 1 or a polynucleotide encoding the same. Yet claim 7 does not further limit the structure correlated with the required increase in L-threonine productivity. Claims 8-10 do not limit the structure of the protein variant in anyway. Claim 11 is drawn to the same genus of protein variants or polynucleotides thereof. The specification does not disclose a representative number of species of the claimed genus by reduction to practice, and does not provide adequate guidance with regard to the structural features of the protein that is required to provide the recited L-threonine efflux properties. Therefore, one of skill cannot immediately envision which proteins will have the required functional characteristics, and one could not conclude that Applicant was in possession of the claimed genus of protein variants at the time the filing, as discussed more fully below.
For claims drawn to a genus, MPEP § 2163(3)(a)(ii) indicates 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 the applicant was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. 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.
The instant specification reduces to practice one example of a protein variant that is 99.6% identical to SEQ ID NO: 1 with the only difference being a G133S substitution. In example 1, the specification teaches inducing mutagenesis of the wild-type rhtC (SEQ ID NO: 2) encoding the L-threonine efflux protein. The genomic DNA of E. coli W3110 is used as a template into which the mutation is introduced. See p. 31 last full paragraph. Fifty colonies are selected from the library of E. coli K12 strains transformed with the mutant library and sequencing is performed to determine the mutation rate and the presence/absence of mutations at various locations. See p. 32 last passage. In example 2, it is confirmed that the mutations are introduced into a nucleotide sequence located between the 397th and the 399th bases downstream from the ORF start codon of the rhtC. That is, it confirmed that the nucleotide sequence located between the 427th to the 429th bases are mutated from GGC to AGC or AGT based on SEQ ID NO: 2, thus encoding mutant RhtC(G133S). See the paragraph spanning pgs. 34-35. In example 4, the L-threonine production of the RhtC(G133S) mutant is compared to the parent strain, Corynebacterium glutamicum KCCM12502P. See p. 38 first paragraph. The rhtC(G133S) mutant shows a 33% increase compared to the parental strain. See p. 39 second paragraph. The rhtC(G133S) mutant is understood to be SEQ ID NO: 3, which is 99.6% identical to instant SEQ ID NO: 1. The instant specification does not reduce to practice a protein variant that is less than 99.6% identical to instant SEQ ID NO: 1 and includes the required mutation at position 133.
MPEP 2163(3)(a)(ii) states that “the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are "representative of the full variety or scope of the genus," or by the establishment of "a reasonable structure-function correlation. Such correlations may be established "by the inventor as described in the specification," or they may be "known in the art at the time of the filing date”. Considering the lack of guidance provided in the specification, one would appraise support from the state of the art to extrapolate the correlation between protein variant structure of the L-threonine efflux function.
With respect to the state of the art on L-threonine efflux proteins, Seo (KR102183209B1, as cited in the IDS filed 09/05/2024) teaches L-threonine efflux protein variants comprising a substitution with another amino acid at a position corresponding to the 53rd or 62nd position of SEQ ID NO: 1 having at least 80% and less than 100% sequence homology. See [0008]. Seo discloses that SEQ ID NO: 1 refers to an amino acid having L-threonine excretion activity. See [0021]. Seo’s SEQ ID NO: 1 is 100% identical to instant SEQ ID NO: 1. See pgs. 29-29 of the original patent document for the sequence. Seo suggests that the L-threonine-releasing protein with the 53rd or 62nd amino acid substitute for another amino acid has enhanced activity compared to the wild-type microbial-derived L-threonine releasing protein before mutation. See [0045].
In view of the prior art, the instant disclosure does not satisfy the written description requirement because the species disclosed do not adequately represent the substantial variation within the claimed genus. As discussed above, the breadth of potential structures embraced by the claims is substantial. Seo teaches mutating SEQ ID NO: 1 (identical to instant SEQ ID NO: 1) at positions 53 and 62 for enhanced activity. However, Seo suggests that the L-threonine efflux protein should be at least 80% identical to SEQ ID NO: 1 for L-threonine excretion activity. The instant specification reduced to practice one example of an L-threonine efflux protein variant with a G133S mutation relative to instant SEQ ID NO: 1 that is capable of being used for increased L-threonine production in C. glutamicum. This represents a very small fraction of the possible number of species within the breadth of the claims. Consequently, one of skill could not conclude that Applicant was in possession of the claimed genus of protein variants that function as an L-threonine efflux protein at the time the application was filed.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1-9 and 11 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural product without significantly more.
Claim 1 recites an “L-threonine efflux protein variant” in line 1. Claim 5 recites a “polynucleotide encoding the L-threonine efflux protein variant”. Claim 6 recites a “microorganism”. Claim 11 recites a “composition. Therefore, claims 1-9 and 11 are directed to compositions of matter, which is one of the statutory categories (Step 1:Yes).
Claim 1 requires an L-threonine efflux protein variant in which the amino acid corresponding to the 133rd position of SEQ ID NO: 1 is substitute with another amino acid. Souvorov (NCBI accession no. HBA8368131.1, submitted 06-Mar-2021) evidences a threonine export protein RhtC from E. coli that is that is 99.4% identical to instant SEQ ID NO: 1 with the only difference being a G133S mutation, where the glycine at position 133 of instant SEQ ID NO: 1 is changed to serine in Souvorov’s HBA8368131.1. See the alignment below and in the office action appendix. Compared to closest naturally occurring counterpart, there is no structural difference between the natural product (i.e. Souvorov’s HBA8368131.1) and the instantly claimed product. Because there is no indication in the record that the instantly disclosed L-threonine efflux protein has a markedly different characteristic in structure, function, or other properties as compared to its natural counterpart claims 1-9 and 11 are directed to a natural-product, which is a judicial exception (Step 2A Prong 1: Yes).
Claim 1-4 do not require any additional elements besides the natural product because claims 1-4 merely describe the natural product as having the G133S mutation relative to instant SEQ ID NO: 1. Claim 5 requires a polynucleotide encoding the L-threonine efflux protein variant according to claim 1. As such, claim 5 cannot integrate the natural product into a practical application because claim 5 merely describes the natural product before it is translated into a protein form. Claim 6 requires a microorganism, which comprises the L-threonine efflux protein variant of claim 1 or a polynucleotide encoding the same. Therefore, claim 6 merely describes the natural product as being derived from a microorganism. Claim 7 requires the microorganism of claim 6 to have increased L-threonine productivity compared to a microorganism of the genus Corynebacterium comprising a wild-type L-threonine efflux protein having an amino acid sequence of SEQ ID NO: 1 or a polynucleotide encoding the same. This limitation of claim 7 serves to generally link the natural product for its field of use. Claim 8 requires the microorganism to be of the genus Corynebacterium. Claim 9 requires the microorganism to be Corynebacterium glutamicum. The limitations of claims 8-9 merely indicate a microorganism that naturally contains a L-threonine efflux protein. Claim 11 does not add any additional elements to the natural product that could integrate it into a practical application. Rather, claim 11 requires the composition to be for producing L-threonine, which only serves to generally link the natural product to its field of use. Therefore, the claim as a whole, does not integrate the judicial exception into a practical application (Step 2A Prong 2: No).
The additional elements of 133 substitution to serine, threonine, cysteine, tyrosine, asparagine, or glutamine, fail to amount to an inventive concept. It was well-understood at the time of filing that the naturally occurring rhtC gene from E. coli encoding an L-threonine efflux protein can be expressed in C. glutamicum and increases the L-threonine excretion rate of C. glutamicum. See Gerth (WO2021/048353) p. 1 lines 37-38; claim 1 of Gerth. (Step 2B: No).
For all of these reasons, claims 1-9 and 11 are not patent eligible.
Claim Rejections - 35 USC § 102
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 1-4 and 11 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Souvorov (NCBI accession no. HBA8368131.1, submitted 06-Mar-2021).
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[AltContent: textbox (Alignment between instant SEQ ID NO: 1 (top) and Souvorov’s RhtC HBA8368131.1 (bottom))]Regarding claims 1-3, Souvorov teaches a threonine export protein RhtC from Escherichia coli (accession no. HBA8368131.1) that has a G133S mutation relative to instant SEQ ID NO: 1. See p. 2 of Souvorov for the sequence and the alignment provided below and in the office action appendix.
Regarding claim 4, Souvorov teaches HBA8368131.1, which is 99.4% identical to instant SEQ ID NO: 1, which is at least 70% and less than 100% as instantly required. See the alignment above.
Regarding claim 11, Souvorov teaches a threonine export protein RhtC from Escherichia coli (accession no. HBA8368131.1) that has a G133S mutation relative to instant SEQ ID NO: 1. See p. 2 of Souvorov for the sequence and the alignment provided below and in the office action appendix.
MPEP 2112.01(II) states that "products of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). In the instant case, Souvorov teaches an L-threonine efflux protein variant in which the amino acid corresponding to the 133rd position of SEQ ID NO: 1 is substitute with another amino acid (i.e. serine). Therefore, the Souvorov’s RhtC protein can be used for producing L-threonine, as instantly claimed.
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.
Claims 5-10 are rejected under 35 U.S.C. 103 as being unpatentable over Souvorov (NCBI accession no. HBA8368131.1, submitted 06-Mar-2021) and Gerth (WO 2021/048353).
Regarding claim 5, Souvorov teaches a threonine export protein RhtC from Escherichia coli (accession no. HBA8368131.1) with a glycine to serine mutation at position 133 relative to instant SEQ ID NO: 1. See p. 2 of Souvorov and the alignment above.
Souvorov does not teach a polynucleotide encoding the L-threonine efflux protein variant.
Gerth discloses that the heterologous expression of E. coli rhtC gene in C. glutamicum increases the L-threonine excretion rate of C. glutamicum. See p. 1 lines 37-38. Gerth teaches constructing a plasmid to enable the incorporation of the E. coli threonine exporter gene rhtC. See p. 23 lines 25-26. Gerth teaches RhtC that comprises the amino acid sequence according to SEQ ID NO: 2, which is 100% identical to instant SEQ ID NO: 1. See claim 2 of Gerth. Gerth teaches the nucleotide sequence of the rhtC gene from E. coli comprising SEQ ID NO: 1. See p. 2 lines 12-13.
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to reverse translate Souvorov’s L-threonine efflux protein to its corresponding polynucleotide based on Gerth’s suggestion. One of ordinary skill in the art would have been motivated to do so because Gerth suggests using E. coli rhtC polynucleotide for heterologous expression. There would have been a reasonable expectation of success because Gerth teaches both an L-threonine efflux protein and polynucleotide; and Souvorov teaches an E. coli RhtC protein, which necessarily comes from a polynucleotide.
Regarding claim 6, Souvorov teaches a threonine export protein RhtC from Escherichia coli (accession no. HBA8368131.1) with a glycine to serine mutation at position 133 relative to instant SEQ ID NO: 1. See p. 2 of Souvorov and the alignment above.
Souvorov does not teach a microorganism, which comprises the L-threonine efflux protein variant. However, Souvorov discloses that the L-threonine efflux protein is from the microorganism E. coli.
Gerth teaches a recombinant bacterium of the genus Corynebacterium comprising a L-threonine exporter gene rhtC coding for a L-threonine exporter RhtC from E. coli. See claim 1 of Gerth.
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to substitute Souvorov’s L-threonine efflux protein for Gerth’s RhtC. One of ordinary skill in the art would have been motivated to do so because Gerth suggests that expressing the E. coli rhtC gene in C. glutamicum increases the L-threonine excretion rate of C. glutamicum (see p. 1 lines 37-38). There would have been a reasonable expectation of success because Souvorov teaches RhtC from E. coli. Therefore, Souvorov’s RhtC from E. coli reasonably serves the same function compared to Gerth’s RhtC from E. coli.
Regarding claim 7, Souvorov teaches a threonine export protein RhtC from Escherichia coli (accession no. HBA8368131.1) with a glycine to serine mutation at position 133 relative to instant SEQ ID NO: 1. See p. 2 of Souvorov and the alignment above.
Gerth teaches that expressing the E. coli rhtC gene in C. glutamicum increases the L-threonine excretion rate of C. glutamicum. See p. 1 lines 37-38. Gerth teaches a recombinant bacterium of the genus Corynebacterium comprising a L-threonine exporter gene rhtC coding for a L-threonine exporter RhtC from E. coli. See claim 1 of Gerth. Gerth teaches RhtC that comprises the amino acid sequence according to SEQ ID NO: 2, which is 100% identical to instant SEQ ID NO: 1. See claim 2 of Gerth.
Souvorov and Gerth do not teach increased L-threonine productivity compared to a microorganism of the genus Corynebacterium comprising a wild-type L-threonine efflux protein having an amino acid sequence of SEQ ID NO: 1 or a polynucleotide encoding the same.
The instant specification teaches comparing the L-threonine production of the RhtC(G133S) mutant to the parent strain, Corynebacterium glutamicum KCCM12502P. See p. 38 first paragraph. The rhtC(G133S) mutant shows a 33% increase compared to the parental strain. See p. 39 second paragraph
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention that substituting Souvorov’s L-threonine efflux protein (i.e. G133S mutation relative to instant SEQ ID NO: 1) for Gerth’s RhtC necessarily increases L-threonine productivity. Souvorov’s L-threonine efflux protein is 100% identical to the instantly disclosed RhtC(G133S) mutant, and MPEP 2112.01(II) states that "products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990).
Regarding claim 8, Gerth teaches a recombinant bacterium of the genus Corynebacterium comprising a L-threonine exporter gene rhtC coding for a L-threonine exporter RhtC from E. coli. See claim 1 of Gerth.
Regarding claim 9, Gerth teaches C. glutamicum strain CT-CG-184PpycK01. See p. 41 line 24. Gerth teaches CT-CG-184 containing rhtC from E. coli. See p. 31 table 21.
Regarding claim 10, Souvorov teaches a threonine export protein RhtC from Escherichia coli (accession no. HBA8368131.1) with a glycine to serine mutation at position 133 relative to instant SEQ ID NO: 1. See p. 2 of Souvorov and the alignment above.
Souvorov does not teach a method for producing L-threonine comprising culturing the microorganism [comprising the L-threonine efflux protein variant, or a polynucleotide encoding the same] in a culture medium.
Gerth teaches cultivating (i.e. culturing) C. glutamicum strain CT-CG-184PpycK01 in a nutrient medium (i.e. culture medium) suitable for the production of threonine. See p. 42 lines 9-11. Gerth teaches CT-CG-184 containing rhtC from E. coli. See p. 31 table 21.
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to substitute Souvorov’s L-threonine efflux protein for Gerth’s RhtC. One of ordinary skill in the art would have been motivated to do so because Gerth suggests that expressing the E. coli rhtC gene in C. glutamicum increases the L-threonine excretion rate of C. glutamicum (see p. 1 lines 37-38). There would have been a reasonable expectation of success because Souvorov teaches RhtC from E. coli. Therefore, Souvorov’s RhtC from E. coli reasonably serves the same function compared to Gerth’s RhtC from E. coli.
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 1-11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of copending Application No. 18/844,029 in view of Souvorov (NCBI accession no. HBA8368131.1, submitted 06-Mar-2021).
Copending claim 1 recites an L-threonine efflux protein variant in which the amino acid corresponding to the 143rd position of SEQ ID NO: 1 [i.e. identical to instant SEQ ID NO: 1] is substituted with another amino acid.
Copending claim 2 recites the L-threonine efflux protein variant according to claim 1, wherein the other amino acid is selected from the group consisting of glycine, alanine, valine, leucine, isoleucine, methionine, phenylalanine, tryptophan, and proline.
Copending claim 3 recites the L-threonine efflux protein variant according to claim 2, wherein the other amino acid is isoleucine.
Copending claim 4 recites the L-threonine efflux protein variant according to claim 1, wherein the L-threonine efflux protein variant has sequence identity of at least 70% and less than 100% to the amino acid sequence of SEQ ID NO: 1.
Copending claim 5 recites a polynucleotide encoding the L-threonine efflux protein variant according to claim 1.
Copending claim 6 recites a microorganism, which comprises the L-threonine efflux protein of claim 1 or a polynucleotide encoding the same.
Copending claim 7 recites microorganism according to claim 6, wherein the microorganism has increased L-threonine productivity compared to a microorganism of the genus Corynebacterium comprising a wild-type L-threonine efflux protein having an amino acid sequence of SEQ ID NO: 1 or a polynucleotide encoding the same.
Copending claim 8 recites the microorganism according to claim 6, wherein the microorganism is a microorganism of the genus Corynebacterium.
Copending claim 9 recites the microorganism according to claim 8, wherein the microorganism of the genus Corynebacterium is Corynebacterium glutamicum.
Copending claim 10 recites a method for producing L-threonine, comprising culturing a microorganism which comprises the L-threonine efflux protein of claim 1; or a polynucleotide encoding the same in a culture medium.
Copending claim 11 recites a composition for producing L-threonine, comprising the L-threonine efflux protein variant of claim 1; a polynucleotide encoding the same; a vector comprising the polynucleotide; a microorganism comprising the L-threonine efflux protein variant or the polynucleotide encoding the same; a culture in which the microorganism has been cultured; or a combination of two or more thereof.
The copending claims lack an L-threonine efflux protein variant in which the amino acid corresponding to the 133rd position of SEQ ID NO: 1 is substitute with another amino acid (same as instant claim 1); wherein the other amino acid is selected from the group consisting of serine, threonine, cysteine, tyrosine, asparagine and glutamine (same as instant claim 2); wherein the other amino acid is serine (same as instant claim 3).
Souvorov teaches a threonine export protein RhtC from Escherichia coli (accession no. HBA8368131.1) with a glycine to serine mutation at position 133 relative to instant SEQ ID NO: 1. See p. 2 of Souvorov and the alignment above.
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to substitute Souvorov’s L-threonine efflux protein for the L-threonine efflux protein variant recited in copending claim 1 in order to increase L-threonine productivity.
This is a provisional nonstatutory double patenting rejection.
Conclusion
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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/K.C.B./Examiner, Art Unit 1657
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