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 .
Election/Restrictions
Applicant’s election without traverse of claims 46-59 in the reply filed on 12/17/2025 is acknowledged. The species elections of porters (claim 48), MdfA SEQ ID NO: 2 (claims 48-51), LNnT (claim 54), N-acetylglucosamine β-1,4-galactosyltransferase (claim 55), 70 g/L or more (claim 56), and microorganism (claim 57) are acknowledged.
Claims 60-65 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 12/17/2025.
In view of the prior art search, the species election is expanded to include MdfA according to SEQ ID NO: 3.
Priority
This application is a 371 of PCT/EP2022/051163 (1/20/2022) which claims priority to EP21152592.8 (1/20/2021) as reflected in the filing receipt issued on 1/30/2024.
Information Disclosure Statement
The information disclosure statements (IDS) filed on 7/17/2023, 11/29/2023, 12/20/2023, and 1/19/2024 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
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 48-51 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Regarding written description, 35 U.S.C. 112(a) and the first paragraph of pre-AlA 35 U.S.C. 112 require that the "specification shall contain a written description of the invention ...." This requirement is separate and distinct from the enablement requirement. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1340, 94 USPQ2d 1161, 1167 (Fed. Cir. 2010). To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention (MPEP § 2163(I)).
MPEP 2163(II)(A)(3)(a)(i and ii) states that 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.
A "representative number of species" means that the species which are adequately described are representative of the entire genus. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., .759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
In the instant case, claims 48-49 recite a cell wherein the membrane protein is a porter membrane protein that is a functional fragment or functional homolog of elected SEQ ID NO: 2, or has 80% identity to SEQ ID NO: 2. Claims 50-51 recite a protein that is a functional fragment or functional homolog of elected SEQ ID NO: 2, or has 90% identity to SEQ ID NO: 2.
There is not sufficient written description support for a functional homolog or functional fragment of SEQ ID NO: 2, or for a polypeptide sequence with 80% or 90% identity to the SEQ ID NO: 2, that retains the claimed functions, as there is not a disclosed structure-function relationship. There is no disclosure of which regions or structural elements of SEQ ID NO: 2 are required or essential for activity, and which regions can be modified, to produce a variant having the recited sequence identity and the enzyme function as set forth in claim 46.
The term “functional homolog”, as set forth on p. 10 para. 29 of the instant specification, describes those molecules that have sequence similarity and also share at least one functional characteristic such as a biochemical activity. “Functional fragment” refers to a clone or any part of a polynucleotide molecule, particularly a part of a polynucleotide that retains a usable, functional characteristic (instant specification p. 11 para. 33). However, there is no disclosure of which positions or residues can or cannot be mutated, deleted, or truncated in any of these sequences while still maintaining protein function. Therefore, a structure-function relationship for a functional homolog or fragment is not disclosed.
SEQ ID NO: 2 has 411 amino acids. This means that anywhere from 1-82 residues may be substituted or mutated, with 19 potential amino acids at each position, within the scope of 80% identity. For a sequence with 90% identity, 41 residues may differ. Thus, 80 or 90% identity encompasses a vast number of potential sequences, and it would not be clear to a skilled artisan which of these potential variants would maintain the function as set forth in claim 46. There are no examples in the specification directed to any derivatives, variants, or fragments of SEQ ID NO: 2, other than specifically claimed SEQ ID NOs as set forth in claims 48-51, which have the claimed enzyme activity, or any indication of which residues can or cannot be modified.
For these reasons, it is not clear that applicant was in possession of the full scope of the invention, i.e. a cell expressing a membrane protein that is 80 or 90% identical to SEQ ID NO: 2 which has the function set forth in claim 46, or a functional fragment or homolog of SEQ ID NO: 2. Thus, claims 48-51 fail to comply with the written description requirement.
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 46-59 and 66-67 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
The terms “improved”, “enhanced, and “better” in claim 46 are relative terms which render the claim indefinite. The terms are not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. The threshold of what is considered a “better” titer, production rate, cell performance index, etc., is not clear. Similarly, the threshold for “improved” or “enhanced” production or efflux is not clear. The claims do not provide a basis for comparison, i.e. better, improved, or enhanced compared to what?.
Additionally, the parentheses in claim 46 around the limitations “gram oligosaccharide per liter”, “gram oligosaccharide per liter per hour”, “gram oligosaccharide per gram biomass”, “gram oligosaccharide per gram biomass per hour”, “gram oligosaccharide per gram sucrose”, “gram sucrose per gram per hour”, “gram lactose per hour” render the scope of this claim unclear. Specifically, it is not clear if the limitations in parentheses are required claim elements, or exemplary.
Claims 47-59 and 66-67 are included in this rejection because the depend on a rejected claim and do not clarify the issue.
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 46-59 and 66-67 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Englert et al., US 2023/0304052 A1 (effective filing date 6/26/2020) as evidenced by NCBI multidrug efflux MFS transporter MdfA.
Regarding claim 46, Englert teaches a genetically engineered bacterial cell for production of an oligosaccharide of interest (Englert “Abstract”). Englert teaches that a cell for producing lacto-N-triose II (or lacto-N-triose, LN3, LNT-II, see instant specification p. 21 para. 52) expresses a functional β-1,3-N-acetylglucosaminyltransferase (Englert p. 3 para. 40; p. 8 para. 99). Englert teaches that in a first step, the 1,3-N-acetylglucosaminyltransferase is used to convert lactose to lacto-N-triose with the nucleotide sugar donor UDP-N-acetylglucosamine (UDP-GlcNAc), i.e., a GlcNAc residue is transferred from UDP-GlcNAc to a lactose acceptor (Englert p. 8 para. 99). Englert teaches that this cell additionally overexpresses an endogenous membrane protein, mdfA, for enhanced translocation of lacto-N-tetraose across the inner membrane (Englert p. 8 para. 100).
Regarding claim 47, Englert teaches that the cell exhibits enhanced efflux (export) of the oligosaccharide into the cell’s surrounding environment (Englert p. 8 para. 100).
Regarding claim 48, Englert teaches that the membrane protein is a porter, specifically MdfA from E. coli (Englert p. 8 para. 100, p. 9 para. 111). Englert teaches that MdfA is overexpressed in E. coli BL21 (DE3) (Englert p. 12 para. 158). The amino acid sequence of MdfA from E. coli BL21 (DE3) is 88.2% identical to instant SEQ ID NO: 2 and 100% identical to instant SEQ ID NO: 3 (see NCBI reference, sequence alignment in OA appendix). Therefore, Englert teaches a strain according to claim 46 wherein the membrane protein is a porter, MdfA, with a sequence that is at least 80% identical to SEQ ID NO: 2, and is 100% identical to SEQ ID NO: 3.
Regarding claim 49, Englert teaches a cell overexpressing MdfA with a sequence that is at least 80% identical to SEQ ID NO: 2 (see NCBI reference, sequence alignment in OA appendix).
Regarding claims 50 and 51, “functional homolog” as set forth in the instant specification p. 10 para. 29, refers to those molecules that have sequence similarity and also share at least one functional characteristic such as a biochemical activity. The MdfA protein as taught by Englert has 88.2% sequence identity and shares the same functional characteristic as the protein represented by SEQ ID NO: 2, which is a multidrug efflux transporter which increases export of an oligosaccharide comprising LN3 (Englert p. 8 para. 100, p. 9 para. 11). Therefore, the MdfA protein of Englert is a functional homolog of the protein represented by instant SEQ ID NO: 2.
Regarding claims 52-54, Englert teaches that the oligosaccharide comprising a lacto-N-triose as a core trisaccharide is lacto-N-neotetraose, which is a mammalian milk oligosaccharide (Englert p. 3 para. 34). Lacto-N-neotetraose is a neutral oligosaccharide (Englert p. 8 para. 99).
Regarding claim 55, Englert teaches that the cell expresses a β-1,4-galactosyltransferase which converts lacto-N-triose II into lacto-N-neotetraose, i.e. transfers a galactose from a UDP-Gal donor in LN3 (Englert pp. 8-9 para. 101).
Regarding claim 56, the limitation “wherein the cell produces” is a functional limitation of the claimed cell. Any cell having the same structure as the cell of claim 46 is capable of performing the function of claim 56. Therefore, the cell taught by Englert, which has the same structure as the cell of claim 46, reads on claim 56.
Regarding claims 57-58, Englert teaches that the cell is a microorganism, E. coli bacterium (Englert p. 12 para. 158).
Regarding claim 59, the limitation “wherein the cell is capable of synthesizing” is a functional limitation of the claimed cell. Any product having the same structure as the cell of claim 46 is capable of performing the function of claim 59. Therefore, the cell taught by Englert, which has the same structure as the cell of claim 46, reads on claim 59.
Regarding claim 66, Englert teaches that the membrane protein is an overexpressed endogenous membrane protein which provides improved efflux of lacto-N-neotetraose (Englert p. 8 para. 100, p. 12 para. 158).
Regarding claim 67, the limitation “wherein the membrane protein reduces intracellular accumulation” is a functional limitation of the claimed cell. Any product having the same structure as the cell of claim 46 is capable of performing the function of claim 67. Therefore, the cell taught by Englert, which has the same structure as the cell of claim 46, reads on claim 67. Additionally, Englert teaches that the membrane protein, MdfA, increases export of lacto-N-neotetraose into the cell’s surrounding environment (Englert p. 8 para. 100). If the export of the oligosaccharide is increased, the accumulation of the oligosaccharide intracellularly would be reduced.
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 46-59 and 66-67 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 11-12 of U.S. Patent No. 12077788 B2 in view of Englert et al., US 2023/0304052 A1 (effective filing date 6/26/2020).
Regarding claims 46-47, 52-53, and 66, claim 1 of ‘788 recites a metabolically engineered cell which expresses an N-acetylglucosaminyltransferase and a galactosyltransferase. Claim 11 of ‘788 recites that the cell comprises i) modified expression of an endogenous membrane protein, ii) modified activity of an endogenous membrane protein, iii) expression of a homologous membrane protein, or iv) expression of a heterologous membrane protein, wherein said membrane protein is involved in secretion of at least one of said at least four different neutral non-fucosylated mammalian milk oligosaccharides. Claim 12 of ‘788 recites that the membrane protein is a porter.
Regarding claims 57-58 and 67, claim 20 of ‘788 recites that the cell is a bacterium.
Regarding claims 56 and 59, these claims recite functional limitations of the claimed bacterial cell. Any cell comprising the same structural features recited in claim 46 reads on the invention of claims 56 and 59.
The claims of ‘788 do not recite a galactoside beta-1,3-N-acetylglucosaminyltransferase that transfers an N-acetylglucosamine (GlcNAc) residue from a UDP-GlcNAc donor to a lactose acceptor thereby synthesizing LN3 (claim 46), that the membrane protein is MdfA according to SEQ ID NO: 2 or a functional fragment thereof (claims 48-51), lacto-N-neotetraose (claim 54), or N-acetylglucosamine beta-1,4-galactosyltransferase (claim 55).
Regarding claim 46, Englert teaches a genetically engineered bacterial cell for production of an oligosaccharide of interest (Englert “Abstract”). Englert teaches that a cell for producing lacto-N-triose II (or lacto-N-triose, LN3, LNT-II, see instant specification p. 21 para. 52) expresses a functional β-1,3-N-acetylglucosaminyltransferase (Englert p. 3 para. 40; p. 8 para. 99). Englert teaches that in a first step, the 1,3-N-acetylglucosaminyltransferase is used to convert lactose to lacto-N-triose with the nucleotide sugar donor UDP-N-acetylglucosamine (UDP-GlcNAc), i.e., a GlcNAc residue is transferred from UDP-GlcNAc to a lactose acceptor (Englert p. 8 para. 99). Englert teaches that this cell additionally overexpresses an endogenous membrane protein, mdfA, for enhanced translocation of lacto-N-tetraose across the inner membrane (Englert p. 8 para. 100).
Regarding claim 48, Englert teaches that the membrane protein is a porter, specifically MdfA from E. coli (Englert p. 8 para. 100, p. 9 para. 111). Englert teaches that MdfA is overexpressed in E. coli BL21 (DE3) (Englert p. 12 para. 158). The amino acid sequence of MdfA from E. coli BL21 (DE3) is 88.2% identical to instant SEQ ID NO: 2 and 100% identical to instant SEQ ID NO: 3 (see NCBI references, sequence alignment in OA appendix). Therefore, Englert teaches a strain according to claim 46 wherein the membrane protein is a porter, MdfA, with a sequence that is at least 80% identical to SEQ ID NO: 2, and is 100% identical to SEQ ID NO: 3.
Regarding claim 49, Englert teaches a cell overexpressing MdfA with a sequence that is at least 80% identical to SEQ ID NO: 2 (see NCBI references, sequence alignment in OA appendix).
Regarding claims 50 and 51, “functional homolog” as set forth in the instant specification p. 10, refer to those molecules that have sequence similarity and also share at least one functional characteristic such as a biochemical activity. The MdfA protein as taught by Englert has 88.2% sequence identity and shares the same functional characteristic as the protein represented by SEQ ID NO: 2, which is a multidrug efflux transporter (Englert p. 9 para. 11). Therefore, the MdfA protein of Englert is a functional homolog of the protein represented by instant SEQ ID NO: 2.
Regarding claim 54, Englert teaches that the oligosaccharide comprising a lacto-N-triose as a core trisaccharide is lacto-N-neotetraose, which is a mammalian milk oligosaccharide (Englert p. 3 para. 34). Lacto-N-neotetraose is a neutral oligosaccharide (Englert p. 8 para. 99).
Regarding claim 55, Englert teaches that the cell expresses a β-1,4-galactosyltransferase which converts lacto-N-triose II into lacto-N-neotetraose, i.e. transfers a galactose from a UDP-Gal donor in LN3 (Englert pp. 8-9 para. 101).
It would have been obvious for a skilled artisan to combine the teachings of ‘788 and Englert, arriving at the instant invention. Englert teaches a cell for oligosaccharide production which expresses an N-acetylglucosaminyltransferase, a galactosyltransferase, and a membrane protein. A skilled artisan would have found it obvious to utilize the specific enzymes taught by Englert in a cell as claimed in ‘788. Both ‘788 and Englert are directed to HMO production by modified cells. ‘788 claims a cell which produces neutral HMOs, which includes lacto-N-neotetraose as taught by Englert. Therefore, a skilled artisan would have found it obvious, with a reasonable expectation of success, to modify the cell of ‘788 with the specific enzymes taught by Englert, and would have been motivated to do so in order to produce the neutral oligosaccharide lacto-N-neotetraose.
Claims 46-47, 52-59, and 66-67 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 101, 107, and 111 of copending Application No. 18/040,356 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because both are directed to cells metabolically engineered for oligosaccharide production expressing the same enzymes.
Regarding claims 46, 47, 55, and 66, claim 101 of ‘356 recites a metabolically engineered cell that expresses an β-1,3-N-acetylglucosaminyltransferase and a β-1,4-galactosyltransferase. Claim 107 of ‘356 recites that the cell overexpresses an endogenous membrane protein or expresses a homologous membrane protein that is involved in secretion of oligosaccharides outside the cell.
Regarding claims 52, 53, 54, 56, 59, and 67, these claims recite functional limitations of the claimed bacterial cell. Claims 101 and 107 of ‘356 recite a cell having the same structural features of the cell of claim 46. It is thus considered that the cell of ‘356 is capable of producing the oligosaccharides of claims 52-54.
Regarding claims 57 and 58, claim 110 of ‘356 recites that the cell is a bacterium.
This is a provisional nonstatutory double patenting rejection.
Claims 48-51 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 101, 107, and 111 of copending Application No. 18/040,356 in view of Englert et al., US 2023/0304052 A1 (effective filing date 6/26/2020).
Copending ‘356 recites a cell according to claim 46 as discussed above. The claims of ‘356 do not recite the specific enzymes of claims 48-51. However, the teachings of Englert regarding claims 48-51 are set forth above.
It would have been obvious for a skilled artisan to combine the teachings of ‘356 and Englert, arriving at the instant invention. Englert teaches a cell for oligosaccharide production which expresses an N-acetylglucosaminyltransferase, a galactosyltransferase, and a membrane protein. A skilled artisan would have found it obvious to utilize the specific enzymes taught by Englert in a cell as claimed in ‘356. Both ‘356 and Englert are directed to HMO production by modified cells. ‘356 claims a cell which expresses the same types of enzymes as taught by Englert, including a membrane protein for export of oligosaccharides. Therefore, a skilled artisan would have found it obvious, with a reasonable expectation of success, to modify the cell of ‘356 with the specific membrane protein taught by Englert.
This is a provisional nonstatutory double patenting rejection.
Claims 46-47, 52-59, and 66-67 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 80, 95, 104, and 112 of copending Application No. 18/041,154 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because both are directed to cells metabolically engineered for oligosaccharide production expressing the same enzymes.
Regarding claims 46, 47, 55, and 66, claim 80 of ‘154 recites a cell for producing di or oligosaccharides. Claim 104 recites that the cell comprises a β-1,3-N-acetylglucosaminyltransferase and N-acetylglucosamine β-1,4-galactosyltransferase. Claim 95 of ‘154 recites that the cell comprises membrane transporter proteins or polypeptides having transport activity so as to transport compounds across the outer membrane of a cell wall.
Regarding claims 52, 53, 54, 56, 59, and 67, these claims recite functional limitations of the claimed bacterial cell. Claims 80, 95, and 104 of ‘154 recite a cell having the same structural features of the cell of claim 46. It is thus considered that the cell of ‘154 is capable of producing the oligosaccharides of claims 52-54.
Regarding claims 57 and 58, claim 112 of ‘154 recites that the cell is a bacterium.
This is a provisional nonstatutory double patenting rejection.
Claims 48-51 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 80, 95, 104, and 112 of copending Application No. 18/041,154 in view of Englert et al., US 2023/0304052 A1 (effective filing date 6/26/2020).
Copending ‘154 recites a cell according to claim 46 as discussed above. The claims of ‘154 do not recite the specific enzymes of claims 48-51. However, the teachings of Englert regarding claims 48-51 are set forth above.
It would have been obvious for a skilled artisan to combine the teachings of ‘154 and Englert, arriving at the instant invention. Englert teaches a cell for oligosaccharide production which expresses an N-acetylglucosaminyltransferase, a galactosyltransferase, and a membrane protein. A skilled artisan would have found it obvious to utilize the specific enzymes taught by Englert in a cell as claimed in ‘154. Both ‘154 and Englert are directed to HMO production by modified cells. ‘154 claims a cell which expresses the same types of enzymes as taught by Englert, including a membrane protein for export of oligosaccharides. Therefore, a skilled artisan would have found it obvious, with a reasonable expectation of success, to modify the cell of ‘154 with the specific membrane protein taught by Englert.
This is a provisional nonstatutory double patenting rejection.
Conclusion
Claims 46-59 and 66-67 are rejected. No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to EMILY F EIX whose telephone number is (571)270-0808. The examiner can normally be reached M-F 8am-5pm ET.
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/EMILY F EIX/Examiner, Art Unit 1653
/JENNIFER M.H. TICHY/Primary Examiner, Art Unit 1653