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
This application claims benefit of priority to the Federal Republic of Germany Application No. DE10 2020 111 560.1 filed on 04/28/2020. This application is also a 371 of PCT/EP2021/060401 filed on 04/21/2021. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. However, an English translation of the foreign patents documents has not been filed. Therefore, for the purposes of applying prior art, the effective filing date of the claimed invention is the filing date of the PCT, 04/21/2021.
Amendment and Claim Status
In the reply filed on 01/28/2026, Applicant amended claims 8-12. Applicant previously canceled claim 2 and claims 1 and 3-7 remain withdrawn as they are not encompassed by Applicant’s election.
Claims 1 and 3-12 are currently pending.
Claims 1 and 3-7 are withdrawn.
Claims 8-12 are under examination.
Maintained Rejections (with modification as necessitated by amendment)
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
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.
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (US 20020132320 A1, 09/19/2002) in view of Fernandez et al. (US 20090288219 A1, 11/19/2009).
Regarding claim 8, Wang et al. disclose methods and compositions for the production of glycoconjugates, in particular, organisms are provided with at least one heterologous gene encoding an enzyme for regenerating a sugar nucleotide along with at least one glycosyltransferase (See entire document, Abstract). In this method, a sugar nucleotide is produced and subsequently utilized by the glycosyltransferase to add the sugar residue to an acceptor, producing a glycoconjugate (Paragraph [0039]).
Wang et al. further disclose methods of producing glycoconjugates involving transforming an organism with a vector encoding at least one sugar-nucleotide regenerating enzyme and at least one glycosyltransferase and growing the organism, i.e. culturing, under appropriate conditions to express the enzymes and produce the glycoconjugate (Paragraphs [0149]-[0150]). One source of energy for the organisms is saccharides, which includes sucrose (Paragraph [0042]). The saccharides are broken down to produce high-energy phosphate donors within the cell, such as ATP, PEP, UTP, GTP and UTP (Paragraph [0042]). The resulting high-energy phosphate donors may be used by the organism to produce a sugar nucleotide molecule (Paragraph [0042]). The organism is engineered to efficiently regenerate the sugar-nucleotide, thus, continually producing more sugar-nucleotide for the glycosyltransferase reaction (Paragraph [0056]). An important aspect of the present invention is the ability to tailor the compositions and methods to specific sugar nucleotides because genes encoding enzymes involved in sugar-nucleotide generation and regeneration are known in the art and can be incorporated into the invention (Paragraph [0057]). Examples of sugar nucleotides that may be generated include UDP-Glc and UDP-GlcNAc (Paragraph [0058]). To produce uridine diphosphate glucose (UDP-Glc), reading on a nucleotide sugar, sucrose synthase in the presence of sucrose can be utilized (Paragraph [0065]). In this reaction, uridine diphosphate (UDP) is converted directly to uridine diphosphate glucose (UDPG) with the consumption of sucrose (Figure 18). UDPG can then be converted to glucose-1-phosphate (G1P) with GalT (galactose-1-phosphate uridylyltransferase) (Figures 1 and 2 of Wang et al.).
Regarding the limitation of converting and further converting steps being carried out simultaneously or successively in a common aqueous reaction solution, Wang et al. disclose culturing the microorganisms may be carried out in accordance with the usual culturing process (Paragraph [0174]). Wang et al. further disclose the culturing is carried out under aerobic conditions by shaking culture, aeration stirring culture or the like (Paragraph [0179]). Thus, as the converting and further converting steps are taking place within the organism that is being cultured and the culture is being shaken or stirred, meaning it is an aqueous solution, Wang et al. disclose converting and further converting steps being carried out simultaneously or successively in a common aqueous reaction solution.
Wang et al. do not disclose the production of ADP-glucose (ADPG) or converting the ADPG to G1P in the presence of inorganic pyrophosphate (PPi) and adenosine triphosphate (ATP).
However, Fernandez et al. disclose the use of sucrose synthase for the synthesis of ADPG (Paragraph [0001]). Starch is the main storage form of carbohydrates in plants (Paragraph [0002]) and ADPG is the universal precursor of starch biosynthesis in plants (Paragraph [003]). Sugar nucleotides such as UDPG and ADPG are produced commercially from pyrophosphorylase reactions catalyzed by enzymes such as UDPG pyrophosphorylase (UGPase) and ADPG pyrophosphorylase (AGPase), respectively, based on the use of an expensive substance called glucose-1-phosphate (G1P) (Paragraph [0005]). AGPase and inorganic pyrophosphate (PPi) convert ADPG to G1P with ATP as a byproduct (Figure 2 of Fernandez et al.). An alternative to this practice for production of sugar nucleotides is based on the use of sucrose synthase (SS) (Paragraph [0005]). Fernandez et al. go on to disclose a specific pathway from sucrose to glucose-6-phosphate (G6P) with the first step utilizing sucrose and sucrose synthase in the presence of a nucleotide diphosphate to generate nucleotide diphosphate glucose (NDP-glucose) (Paragraph [0020]). ADP or UDP can be used as the NDP in the pathway from sucrose to G6P (Paragraph [0021]).
Overall, Fernandez et al. disclose a pathway wherein ADP is converted to ADPG in the presence of sucrose and sucrose synthase and further converting the ADPG to G1P in the presence of AGPase.
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the organism of Wang et al. to synthesize ADPG because Wang et al. specifically state their organism can be tailored to generate specific sugar nucleotides because enzymes involved in sugar nucleotide generation are known in the art and Fernandez et al. disclose the specific enzymes necessary to synthesize ADPG, a sugar nucleotide. It would have been further obvious to utilize the organism of Wang et al. to synthesize ADPG because Wang et al. utilize their organism to synthesize UDPG and ADPG and UDPG are similar nucleotide sugars, only differing by the nucleotide, that are synthesizable by similar means, with UDPG utilizing UDP and sucrose synthase and ADPG utilizing ADP and sucrose synthase as taught by Fernandez et al. Additionally, it would have been obvious to one of ordinary skill in the art to further convert the ADPG to G1P via AGPase, a known pathway taught by Fernandez et al., motivated by the desire to reach the desired end product.
Therefore, instant claim 8 is rendered obvious in view of the teachings of Wang et al. and Fernandez et al.
Claims 8-12 are rejected under 35 U.S.C. 103 as being unpatentable over Wang et al. (US 20020132320 A1, 09/19/2002) in view of Fernandez et al. (US 20090288219 A1, 11/19/2009) and further in view of Li et al. (Molecules, 07/28/2011).
The teachings of Wang et al. and Fernandez et al. are discussed above.
Regarding claim 9, Wang et al. disclose methods of producing glycoconjugates containing N-acetylglucosamine wherein an organism comprising a vector is provided polyphosphate and N-acetylglucosamine (Paragraph [0158]). Wang et al. further disclose converting N-acetylgalactosamine (GalNAc) to N-acetylgalactosamine 1-phosphate (GalNAc-1-P) in the presence of ATP via a kinase with ADP as a byproduct (See Figure 8 of Wang et al.). It is noted N-acetylgalactosamine and N-acetylglucosamine only differ by their monosaccharide component, being galactose in N-acetylgalactosamine and glucose in N-acetylglucosamine. Additionally, Wang et al. disclose converting GlcNAc to GlcNAc-6-P and subsequently converting GlcNAc-6-P to GlcNAc-1-P (Figure 7 of Wang et al.).
Wang et al. do not disclose converting N-acetylglucosamine (GlcNAc) to N-acetylglucosamine-1-phosphate (GlcNAc-1-P) via N-acetylhexosamine 1-kinase.
However, Li et al. disclose GlcNAc and GalNAc are important monosaccharides broadly distributed in nature (See entire document, Page 6397, Paragraph 1). Li et al. further disclose N-acetylhexosamine 1-kinase (NahK) catalyzes the direction addition of phosphate from ATP to the anomeric position of N-acetylhexosamine and shows similar activity towards GlcNAc and GalNAc (Abstract).
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized NahK, reading on an N-acetylhexosamine 1-kinase, as the kinase in the conversion of GalNAc to GalNAc-1-P in the organism of Wang et al. because Nahk was a known and effective kinase for catalyzing the conversion of GalNAc to GalNAc-1-P as taught by Li et al. It would have been further obvious to one of ordinary skill in the art to utilize NahK to convert the GlcNAc directly to GalNAc-1-P in the organism of Wang et al. in a simple one step process, instead of a two step process, and NahK was a known and effective kinase for catalyzing the conversion of GlcNAc to GlcNAc-1-P as taught by Li et al.
Regarding claim 10, Wang et al. disclose converting GlcNAc-1-P to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) via GlmU (Paragraph [0067]-[0068], Figure 7). GlmU is an uridine diphosphate-N-acetylglucosamine diphosphorylase. The conversion of GlcNAc-1-P to UDP-GlcNAc utilizes UTP and has PPi as a by-product (Figure 7 of Wang et al.).
Regarding claim 11, Wang et al. disclose GalU is responsible for the formation of UDP-Glc from uridine triphosphate (UTP) and G1P (Paragraph [0234]). The GalU gene encodes G1P uridylyltransferase (Paragraph [0234]), reading on a uridine triphosphate monosaccharide 1-phosphate uridylyltransferase.
Regarding claim 12, Wang et al. disclose the vector that is used to transform the organism can comprise a PgM gene (Claim 1 of Wang et al.). The PgM (phosphoglucomutase) gene is known to interconvert glucose-6-phosphate (G6P) and G1P (Figure 6 of Wang et al.).
USC § 103 - Response to Arguments
Applicant’s arguments, see Pages 5-7, filed 01/28/2026, with respect to the rejection of claims 8-12 under 35 USC § 102 have been fully considered and are persuasive. Therefore, the rejection has been withdrawn. However, upon further consideration, a new grounds of rejection has been set forth above in view of the amendments to the instant claims filed 01/28/2026.
Conclusion
Claims 8-12 are rejected.
No claims are 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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/A.T.W./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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