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 .
Application Status
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 08/19/2026 has been entered.
In response to FINAL-Office Action mailed on 03/20/2026, applicants' response, arguments and amendments filed on dated 08/19/2026 is acknowledged; in said response applicants’ have amended claims 1-9, 20-22 and 25. Thus, amended claims 1-9 and 11-25 are pending and are now under consideration; elected Group 3, amended claims 4-9 and 11-20 reading on the elected invention is now under consideration for examination; claims 1-3 and 21-25 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a non-elected invention, there being no allowable generic or linking claim. Rejections and/or objections not reiterated from previous office action are hereby withdrawn.
Priority
Applicants’ claim for the benefit of priority under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, or 365(c) is acknowledged. This application is a 371 of PCT/US2021/020898 filed on 03/04/2021, which claims the benefit of priority under 35 U.S.C. 119(e) to the US Provisional applications: 63/026,805 filed on 05/19/2020 and 62/985,467 filed on 03/05/2020.
Information disclosure statement
The information disclosure statement (IDS) submitted on 07/16/2026 and 08/19/2026 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDS statements are considered and initialed by the examiner.
Withdrawn-Claim Rejections: 35 USC § 112(a)
Previous rejection of claims 4-6 and 11-20 rejected under 35 U.S.C. 112(a) for written description and enablement, is being withdrawn due to claim amendments and persuasive arguments.
Withdrawn-Claim Rejections: 35 USC § 103
Previous rejection of claims 4-7, 9 and 11-20 rejected under 35 U.S.C. 103(a) as being unpatentable over Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016) and further in view of Ito et al., (Biochem., 2010, Vol. 49: 2604-2614), Schwartz et al., (US 2011/0223646 A1), Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019) and Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199), is being withdrawn due to claim amendments.
New-Claim Rejections: 35 USC § 103
Necessitated by claim amendments
The following is a quotation of 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102 of this title, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negatived by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims under 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of 35 U.S.C. 103(c) and potential 35 U.S.C. 102(e), (f) or (g) prior art under 35 U.S.C. 103(a).
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103(a) 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.
Claims 4-7, 9 and 11-20 are rejected under 35 U.S.C. 103(a) as being unpatentable over Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016) and further in view of Moh SXE., (PhD., Thesis, Macquarie Univ., Australia, 2018, pages 1-165), Ito et al., (Biochem., 2010, Vol. 49: 2604-2614), Schwartz et al., (US 2011/0223646 A1), Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019) and Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199).
Regarding claims 4-6, 9 and 16-20, Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016) disclose a method of preparing hypersialylated (hsIgG), the method comprising: (a) providing a mixture of IgG antibodies; and (b) incubating the mixture of IgG antibodies in a reaction mixture comprising: human b-1,4-Galactosyltransferase I (4GalT1) and a 2,6 sialyltransferase (ST6Gal1) activities (as in claims 4-6 and 16-20); and said reference a 2,6 sialyltransferase (ST6Gal1) having 100% sequence identity to SEQ ID NO: 14 of the instant invention (see provided sequence alignments). Applicants are directed to the following sections in Prod’Homme et al., (US 10,464,996 B2): Abstract; Fig. 1-2 and 4; col. 2, lines 4-51; col. 8, lines 54-60; col. 11, lines 62-67; col. 12, lines 54-57 to col. 13, lines 1-6; col. 18, lines 20-67 to col. 20, lines 1-60; Example 1; and entire document; certain relevant sections from US 10,464,996 B2 is reproduced below.
US 10,464,996 Prod’Homme et al.,
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The disclosure of Prod’Homme et al., (US 10,464,996 B2) as applied to claims 4-6, 9 and 16-20 is described above. However, Prod’Homme et al., are silent regarding wherein a polypeptide comprising an enzymatically active a portion of human ß1,4- Galactosyltransferase I (B4GalT1) bound to a solid support, wherein the portion of human B4GalT1 has galactosyltransferase enzymatic activity, wherein the polypeptide comprising a portion of human ß4GalT1 further comprises an affinity tag, wherein the affinity tag is attached to the solid support and wherein the enzymatically active portion of human 4GalT1 comprises SEQ ID NO: 8 (as in claims 4-7); wherein the polypeptide comprising an enzymatically active portion of human 4GalT1 further comprises an affinity tag, wherein the affinity tag is C-terminal (as in claim 11 and 12); wherein said tag comprising poly-histidine (as in claim 13-14); and wherein the solid support is a magnetic bead (as in claim 15).
Regarding claims 4-7 and 11-13, wherein a polypeptide comprising an enzymatically active a portion of human ß1,4-Galactosyltransferase I (B4GalT1) bound to a solid support, wherein the portion of human B4GalT1 has galactosyltransferase enzymatic activity, wherein the polypeptide comprising a portion of human ß4GalT1 further comprises an affinity tag, wherein the affinity tag is attached to the solid support, the following references teaches structural and functional elements of the instant invention:
Regarding claims 4-7 and 11-13, Moh SXE., (PhD., Thesis, Macquarie Univ., Australia, 2018, pages 1-165) teach platforms for in vitro glycoengineering of proteins utilizing glycosyltransferases, said reference method comprising “galactosylating a glycoprotein in vitro using a recombinantly expressed His-tagged human ß1,4-Galactosyltransferase I (B4GALT1) immobilised onto Ni-NTA resin, as a proof of concept of creating a mini-Golgi column for in vitro designer protein glycosylation (Chapter 3, pages 72-87); immobilization protocol of 8X His-tagged human ß1,4-Galactosyltransferase I (B4GALT1) and activity assay after immobilization on resin column format (pages 76-79); activity of enzyme up to 68% of glycans were fully glycosylated (Fig. 3, page 80); stationary phase format up to 43% of the glycans fully glycosylated (Fig. 5, page 82 & page 84); said reference provides teaching, suggestion and motivation for optimization in large scale format and the projected glycosylation >90% (page 85).
Regarding claims 4-7 and 11-12, Ito et al., (Biochem., 2010, Vol. 49: 2604-2614) disclose human ß1,4-Galactosyltransferase I (B4GalT1) bound to a solid support/immobilized enzyme, wherein the portion of human ß1,4-Galactosyltransferase I (B4GalT1) has galactosyltransferase enzymatic activity, wherein the polypeptide comprising a portion of human galactosyltransferase as fusion protein comprising maltose binding protein tag and His6 tag (see Abstract; Scheme 1, page 2605; Preparation of fusion protein, col. 1, page 2606; Table 2, page 2610; Fig. 6-7, page 2611; Conclusion; and entire document).
Regarding claims 12-14, Schwartz et al., (US 2011/0223646 A1) disclose expression of soluble active glycosyltransferases including 4GalT1 and ST6Gal1 as fusion proteins comprising purification tags including hexa-histidine tags and assays performed by the use of said reference enzymes in solid-phase format using acceptors and donors such as CMP-NANA (see Abstract; paragraphs [0009], hexa-histidine tags, [0089-0092]; Examples, paragraphs [0219-0233]; Claims and entire document).
Regarding claims 7 and 9, analogous art Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019) also provide teaching, suggestion and motivation to a skilled artisan in a method of glycoengineering of IgG antibodies of interest by the use fusion proteins comprising the enzymatically active portion of human 4GalT1 and a 2,6 sialyltransferase, said reference 4GalT1 having 100% sequence identity to SEQ ID NO: 8 of the instant invention; and said reference a 2,6 sialyltransferase (ST6Gal1) having 100% sequence identity to SEQ ID NO: 14 of the instant invention (see provided sequence alignments; also see Abstract; Abstract; Fig. 1-2, 4; glycosylation enzymes and fusion proteins col. 12, lines 56-67 to col. 16, lines 1-5; Claims; and entire document).
Regarding claims 4-6 and 15, wherein the solid support is a magnetic bead, the following reference teaches structural and functional elements of the instant invention: Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199) disclose method of making and method of use of affinity separation of his-tagged proteins using magnetic silica nanoparticle/beads (see Abstract; Fig. 1, page 3194; Conclusion, page 3199; and entire document).
Furthermore, the many advantages of recombinant production of useful proteins, construction of fusion proteins, selection of vectors including vectors comprising constitutive and inducible promoters, transformation of host cells with any desired characteristics and cellular context are well known within the art (for example, see Chapters 1-3, 16 and Vectors-Appendix 5 in Current Protocols in Molecular Biology, Ed., Ausubel et al., Published by John Wiley and Sons, New York, NY, USA, 1990; reference not enclosed), as are recombinant methods of obtaining the necessary genes. These advantages include a) the ability to produce much larger quantities of the protein cloned into suitable expression vectors, b) being able to produce the protein in more easily handled organisms or organisms of interest with suitable characteristics depending on the experimental need (host cells), c) construction of fusion proteins with suitable tags/heterologous polypeptides for easy detection and purification of expressed proteins or endowing said polypeptide with additional biological and biochemical properties, d) appropriate targeting of expressed polypeptides to the sub-cellular compartment of interest in the host cell of interest by expressing said polypeptide as a fusion protein comprising heterologous signals such as leader sequences, e) for reducing the number of steps necessary for the purification of a protein, f) producing the protein in a purer form by using an organism that does not include naturally occurring contaminants of the protein, and g) and advantages of using different cellular context for the expression and production of polypeptide or fusion protein of interest.
As such, disclosure of strategy and methods for generating “wherein the enzymatically active portion of human 4GalT1 comprises SEQ ID NO: 8; wherein the polypeptide comprising an enzymatically active portion of human 4GalT1 further comprises an affinity tag, wherein the affinity tag is attached to the solid support ; wherein said tag comprising poly-histidine; and wherein the solid support is a magnetic”, such as that of references of Moh SXE., Ito et al., Schwartz et al., Anthony et al., and Mohapatra et al., teaching the advantages of said modifications, clearly suggests to a skilled artisan to modify the teachings of Prod’Homme et al., and incorporate the structural and functional elements of Moh SXE., Ito et al., Schwartz et al., Anthony et al., and Mohapatra et al., in the claimed method for preparing hypersialylated (hsIgG) and as claimed in the instant invention. One of ordinary skill in the art would have a reasonable expectation of success, since method for preparing hypersialylated (hsIgG) including the structural and functional elements of the instant invention are well known in the art (for details see the rejection above).
Therefore, claims 4-7, 9 and 11-20 are rejected under 35 U.S.C. 103(a) as being unpatentable over Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016) and further in view of Moh SXE., (PhD., Thesis, Macquarie Univ., Australia, 2018, pages 1-165), Ito et al., (Biochem., 2010, Vol. 49: 2604-2614), Schwartz et al., (US 2011/0223646 A1), Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019) and Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199).
Applicants’ have traversed the above 35 U.S.C. 103(a) rejection following claim amendments and said arguments are relevant to the new rejection (see pages 11-19 of Applicants’ REMARKS dated 08/19/2026).
Applicants’ argue (A): “…The Office relies on the newly cited reference Ito for allegedly teaching human β4GalT1 bound to a solid support/immobilized enzyme and a fusion protein comprising maltose-binding protein and His6 tags. However, Ito does not teach or suggest the amended claim element wherein ß4GalT1 is bound to a solid support via an affinity tag. Specifically, Ito's His6 tag is used for purification, not for attachment of ß4GalT1, an active reaction reagent, to the solid support. Ito describes recombinant hGalT-Sor as an MBP-fused hGalT construct having a C- terminal LPETG sorting signal followed by His6 and states that rhGalT-Sor was purified by Ni affinity chromatography and DEAE-Sepharose chromatography. Ito then immobilizes rhGalT- Sor by SrtA-mediated transpeptidation involving the engineered LPETG motif and amino groups displayed on EAH-Sepharose. See, Ito, p. 2608 and Fig. 3. Thus, Ito uses different structural features for different purposes than set forth in the instant claims: Ito's His6 tag is used for purification. Accordingly, Ito does not disclose or suggest the currently claimed mechanism of immobilization, i.e., ß4GalT1 bound to the solid support via an affinity tag.”
Reply (A): Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Contrary to applicants’ arguments and assertions, claims 4-7, 9. 11 and 15-20 do not recite any specific affinity tag or specific structure and thus applicants’ arguments are directed at limitations not recited in the claims; therefore, examiner continues to maintain the position that Ito et al., (Biochem., 2010, Vol. 49: 2604-2614) disclose human ß1,4-Galactosyltransferase I (B4GalT1) bound to a solid support/immobilized enzyme does indeed teach and suggest the structural and functional elements of the instant invention (for details see the rejection above).
Additionally, examiner has provided a new reference regarding claims 4-7 and 11-13, Moh SXE., (PhD., Thesis, Macquarie Univ., Australia, 2018, pages 1-165) teach platforms for in vitro glycoengineering of proteins utilizing glycosyltransferases, said reference method comprising “galactosylating a glycoprotein in vitro using a recombinantly expressed His-tagged human ß1,4-Galactosyltransferase I (B4GALT1) immobilised onto Ni-NTA resin, as a proof of concept of creating a mini-Golgi column for in vitro designer protein glycosylation (Chapter 3, pages 72-87); immobilization protocol of 8X His-tagged human ß1,4-Galactosyltransferase I (B4GALT1) and activity assay after immobilization on resin column format (pages 76-79); activity of enzyme up to 68% of glycans were fully glycosylated (Fig. 3, page 80); stationary phase format up to 43% of the glycans fully glycosylated (Fig. 5, page 82 & page 84); said reference provides teaching, suggestion and motivation for optimization in large scale format and the projected glycosylation >90% (page 85).
Examiner continues to maintain that Schwartz et al., (US 2011/0223646 A1) is a valid/relevant reference that discloses expression of soluble active glycosyltransferases including 4GalT1 and ST6Gal1 as fusion proteins comprising purification tags including hexa-histidine tags and assays performed by the use of said reference enzymes. Therefore, examiner continues to take the position that each and every element of the instant invention is taught in the combination of cited references and that the combined teachings in the cited prior art provides a reasonable expectation of success and predictability for claimed method.
Applicants’ further argue (B): “…As the Office is aware, an alleged prima facie case of obviousness is rebutted by objective indicia of non-obviousness, including unexpected results demonstrating a meaningful advantage attributable to the claimed immobilized-enzyme configuration.
Specifically, Example 2 of the application shows that galactosylation using β4GalT1 immobilized on a solid support via an affinity tag achieves galactosylation levels comparable to those obtained using free, soluble ß4GalT1, while requiring approximately 50-80% less enzyme. This efficiency gain is directly attributable to the claimed configuration in which ß4GalT1 is bound to a solid support via an affinity tag and is used in the galactosylation reaction. The present amendment further aligns the claim language with that configuration, reciting that the ß4GalT1 polypeptide is "bound to a solid support via an affinity tag."
Importantly, this efficiency gain is relevant in comparison with the cited references. Schwartz and Mohapatra do not provide a comparable teaching because Schwartz uses soluble enzyme in assays described as solid-phase format, and Mohapatra concerns affinity separation or capture of His-tagged proteins rather than catalytic antibody galactosylation using affinity-tag- immobilized ß4GalT1. The ß4GalT1 in Ito is immobilized by sortase-mediated covalent chemistry involving the engineered LPETG motif and amino groups on a solid support, not by attachment via an affinity tag; thus, Ito does not teach or suggest that β4GalT1 bound to a solid support via an affinity tag would achieve comparable IgG galactosylation while substantially reducing enzyme consumption in the claimed hsIgG process. Accordingly, the advantageous reduction in enzyme usage and process efficiency provide strong secondary considerations supporting patentability and standing in rebuttal to any alleged prima facie case of obviousness.”
Reply (B): Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Contrary to applicants’ arguments and assertions, examiner has provided a new reference examiner has provided new reference regarding claims 4-7 and 11-13, Moh SXE., (PhD., Thesis, Macquarie Univ., Australia, 2018, pages 1-165) teach platforms for in vitro glycoengineering of proteins utilizing glycosyltransferases, said reference method comprising “galactosylating a glycoprotein in vitro using a recombinantly expressed His-tagged human ß1,4-Galactosyltransferase I (B4GALT1) immobilised onto Ni-NTA resin, as a proof of concept of creating a mini-Golgi column for in vitro designer protein glycosylation (Chapter 3, pages 72-87); immobilization protocol of 8X His-tagged human ß1,4-Galactosyltransferase I (B4GALT1) and activity assay after immobilization on resin column format (pages 76-79); activity of enzyme up to 68% of glycans were fully glycosylated (Fig. 3, page 80); stationary phase format up to 43% of the glycans fully glycosylated (Fig. 5, page 82 & page 84); said reference provides teaching, suggestion and motivation for optimization in large scale format and the projected glycosylation >90% (page 85).
.
Some of the Applicants' arguments are based on superior/unexpected results by the Applicants’ method (see response dated 08/19/2026, pages 18-19). This argument is not found particularly persuasive because the evidence necessary to overcome a prima facie case of obviousness must not only be clear and convincing, but must also be commensurate in scope with the claimed subject matter. Examiner would like to point out that Example 2 specification is limited to a single species immobilization of SEQ ID NO: 38. Further, it is well recognized that “unexpected” effects are highly unpredictable and are very dependent on the specific conditions including particular structures and examiner has also provided ample evidence regarding structural and functional heterogeneity in the claimed enzymes (for details see 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, rejection for written-description and enablement above). Thus, any combination for which synergism or “unexpected” effect is not clearly established would be properly rejected because non-obviousness would not have been established. The scope of the showing must be commensurate with the scope of claims to consider evidence probative of unexpected results, for example. In re Dill, 202 USPQ 805 (CCPA, 1979), In re Lindner 173 USPQ 356 (CCPA 1972), In re Hyson, 172 USPQ 399 (CCPA 1972), In re Boesch, 205 USPQ 215, (CCPA 1980), In re Grasselli, 218 USPQ 769 (Fed. Cir. 1983), In re Clemens, 206 USPQ 289 (CCPA 1980). It should be clear that the probative value of the data is not commensurate in scope with the degree of protection sought by the claim.
Therefore, examiner continues to take the position that each and every element of the instant invention is taught in the combination of cited references and that the combined teachings in the cited prior art provides a reasonable expectation of success and predictability for the claimed method herein and the claimed benefits are very much expected and predictable.
The Supreme Court has acknowledged: When a work is available in one field of endeavor, design incentives and other market forces can prompt variations of it, either in the same field or a different one. If a person of ordinary skill can implement a predictable variation...103 likely bars its patentability...if a technique has been used to improve one device, and a person of ordinary skill in the art would recognize that it would improve similar devices in the same way, using the technique is obvious unless its actual application is beyond that person's skill. A court must ask whether the improvement is more than the predictable use of prior-art elements according to their established functions ...... the combination of familiar elements according to known methods is likely to be obvious when it does no more than yield predictable results (see KSR International Co. v. Teleflex Inc., 82 USPQ2d 1385 U.S. 2007) (emphasis added).
Examiner continues to hold the position that the cited references render claims 4-7, 9 and 11-20 prima facie obvious to one of ordinary skill in the art when one applies the Teaching, Suggestion and Motivation (TSM) test under the rationale for arriving at a conclusion of obviousness as suggested by the KSR ruling. The rationale applied for this rejection is as follows:
(A) Combining prior art elements according to known methods to yield predictable results;
(B) Simple substitution of one known element for another to obtain predictable results;
(C) Use of known technique to improve similar devices (methods, or products) in the same way;
(D) Applying a known technique to a known device (method, or product) ready for improvement to yield predictable results;
(E) “Obvious to try”–choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success;
(F) Known work in one field of endeavor may prompt variations of it for use in either the same field or a different one based on design incentives or other market forces if the variations are predictable to one of ordinary skill in the art;
(G) Some teaching, 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.
The combined teachings in the cited prior art provides a reasonable expectation of success and predictability for the claimed invention. In view of the foregoing, when all of the evidence is considered, the totality of the rebuttal evidence of nonobviousness fails to outweigh the evidence of obviousness.
Maintained-Double Patenting rejection
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 §§ 706.02(l)(1) - 706.02(l)(3) 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).
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Claims 4-9 and 11-20 are provisionally rejected on the ground of nonstatutory double patenting over: (i) amended claims 45-46, 48, 50, 52-57, 59 and 61-64 (dated 12/19/2025) of co-pending Application No. 17/802,441 (US 2023/0303984 A1); ((ii) amended claims 1-6, 12-16, 18-20, 22-23, 27 and 32 (dated 06/04/2026) of Application No. 17/925,999 (US 2023/0192814 A1; now allowed 07/07/2026); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 (dated 06/05/2026) of co-pending Application No. 18/022,061 (US 2023/0357813 A1) and further in view of Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016), Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019), Hall et al., (US 11,447,789 B2); Schwartz et al., (US 2011/0223646 A1) and Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199). This is a provisional double patenting rejection because the patentably indistinct claims have not in fact been patented.
The subject matter claimed in the instant application is fully disclosed in the referenced co-pending applications and would be covered by any patent granted on those co-pending applications (i) amended claims 45-46, 48, 50, 52-57, 59 and 61-64 (dated 12/19/2025) of co-pending Application No. 17/802,441 (US 2023/0303984 A1); ((ii) amended claims 1-6, 12-16, 18-20, 22-23, 27 and 32 (dated 06/04/2026) of Application No. 17/925,999 (US 2023/0192814 A1; now allowed 07/07/2026); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 (dated 06/05/2026) of co-pending Application No. 18/022,061 (US 2023/0357813 A1) and further in view of Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016), Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019), Hall et al., (US 11,447,789 B2); Schwartz et al., (US 2011/0223646 A1) and Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199), since the referenced co-pending applications and the instant application are claiming common subject matter, as follows: “genera of polypeptides undefined and unlimited structures including variants, mutants and homologs having human b-1,4-Galactosyltransferase I (4GalT1), an enzymatically active portion of human b-1,4-Galactosyltransferase I (4GalT1) and a 2,6 sialyltransferase (ST6Gal1) activities (as in claims 4-6 and 11-20; no structure is recited in claims; also see claims objections); said ST6Gal1 is an enzymatically active portion that comprises SEQ ID NO: 37, 38 or 39 in the claimed method (as in claim 8)”, as claimed in claims 4-9 and 11-20 of the instant application and falls entirely within the scope of (i) amended claims 45-46, 48, 50, 52-57, 59 and 61-64 (dated 12/19/2025) of co-pending Application No. 17/802,441 (US 2023/0303984 A1); ((ii) amended claims 1-6, 12-16, 18-20, 22-23, 27 and 32 (dated 06/04/2026) of Application No. 17/925,999 (US 2023/0192814 A1; now allowed 07/07/2026); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 (dated 06/05/2026) of co-pending Application No. 18/022,061 (US 2023/0357813 A1) and said reference polypeptides having 100% sequence identity to SEQ ID NOs: 8, 14 and 37-39 of the instant invention (see provided sequence alignments). Additionally, the following references of prior art Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016), Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019), Hall et al., (US 11,447,789 B2); Schwartz et al., (US 2011/0223646 A1) and Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199) provides Teaching, Suggestion and Motivation for modifying the instant claims 4-9 and 11-20, by providing the structural and functional elements including the method of generating fusion proteins comprising the poly-histidine tags and the use of magnetic beads (for details see 35 U.S.C. 103(a) rejection above). Therefore, the method claims 4-9 and 11-20 of the instant invention are deemed as an obvious variation of(i) amended claims 45-46, 48, 50, 52-57, 59 and 61-64 (dated 12/19/2025) of co-pending Application No. 17/802,441 (US 2023/0303984 A1); ((ii) amended claims 1-6, 12-16, 18-20, 22-23, 27 and 32 (dated 06/04/2026) of Application No. 17/925,999 (US 2023/0192814 A1; now allowed 07/07/2026); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 (dated 06/05/2026) of co-pending Application No. 18/022,061 (US 2023/0357813 A1), and furthermore the instant claims and the co-pending claims of the cited references use open-ended transitional term “comprising” which is inclusive of additional, unrecited elements. This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
Applicants’ have traversed the above ODP rejection with the following arguments: (see pages 19-20 of Applicants’ REMARKS dated 08/19/2026).
Applicants’ argue: “…As an indication of allowability of the present claims has not been received, Applicant respectfully requests addressing these rejections be held in abeyance until such time as an indication of allowability is available.”
Reply: Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Examiner is maintaining the rejection for reasons made of record in the Office-action dated 03/20/2026, as none of the claims are allowed.
Summary of Pending Issues
The following is a summary of issues pending in the instant application.
Claims 4-7, 9 and 11-20 are rejected under 35 U.S.C. 103(a) as being unpatentable over Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016) and further in view of Moh SXE., (PhD., Thesis, Macquarie Univ., Australia, 2018, pages 1-165), Ito et al., (Biochem., 2010, Vol. 49: 2604-2614), Schwartz et al., (US 2011/0223646 A1), Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019) and Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199).
Claims 4-9 and 11-20 are provisionally rejected on the ground of nonstatutory double patenting over: (i) amended claims 45-46, 48, 50, 52-57, 59 and 61-64 (dated 12/19/2025) of co-pending Application No. 17/802,441 (US 2023/0303984 A1); ((ii) amended claims 1-6, 12-16, 18-20, 22-23, 27 and 32 (dated 06/04/2026) of Application No. 17/925,999 (US 2023/0192814 A1; now allowed 07/07/2026); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 (dated 06/05/2026) of co-pending Application No. 18/022,061 (US 2023/0357813 A1) and further in view of Prod’Homme et al., (US 10,464,996 B2; prior publication data US 2016/0090409 A1, 03/31/2016), Anthony et al., (US 11,674,125 B2; PCT Publication date 06/27/2019), Hall et al., (US 11,447,789 B2); Schwartz et al., (US 2011/0223646 A1) and Mohapatra et al., (J. Nanosci. Nanotechnol., 2007, Vol. 7: 3193-3199).
Claims 1-3 and 21-25 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a non-elected invention, there being no allowable generic or linking claim.
Conclusion
None of the claims are allowable. Claims 4-9 and 11-20 are rejected for the reasons identified in the Rejections and Summary sections of this Office Action. Applicants’ must respond to the rejections in each of the sections in this Office Action to be fully responsive for prosecution.
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/GANAPATHIRAMA RAGHU/ Primary Examiner, Art Unit 1652
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