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
In response to Non-Final Office Action mailed on 10/29/2025, applicants' response, arguments and amendments filed on dated 02/27/2026 is acknowledged; in said response applicants’ have amended claims 1-9, 11-14, 18 and 21-25 and canceled claim 10. 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4-9 and 11-20 reading on the elected invention is now under consideration for examination; claims 1-3 and 21-25 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a non-elected invention, there being no allowable generic or linking claim. Rejections and/or objections not reiterated from previous office action are hereby withdrawn.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. Upon further review, the instant elected claims 7-9 are only granted the priority date 371 of PCT/US2021/020898 filed on 03/04/2021 as support for the amended claims 7-9 are only found in 371 of PCT/US2021/020898 filed on 03/04/2021.
Applicants’ have traversed the above priority with the following arguments: (see pages 7-9 of Applicants’ REMARKS dated 02/27/2026).
Applicants’ argue: “…Claims reciting ß4GalT1 polypeptides, the portion with galactosyltransferase enzymatic activity, and sequence-identity variants (claims 4-6, 9-11, 16-20) are supported by the structural disclosure of β4GalT1 sequences in the '467 application. The specification provides SEQ ID NO: 1 and SEQ ID NO: 1A as human ß4GalT1 sequences (page 10) and further discloses His- tagged and variant ß4GalT forms (SEQ ID NO: 3 and SEQ ID NO: 4) (pages 11-12). The specification teaches that suitable ß4GalT enzymes may have amino acid sequences at least 80%, 85%, 90%, 95%, 98%, or 100% identical to these sequences (pages 9-11). This provides explicit structural support for the β4GalT1 genus recited in the claims.
Claims reciting ST6Gal1 polypeptides and sequence-identity variants (claims 7-8 and related dependents) are supported by the structural disclosure of ST6Gal1 in the '467 application. The specification provides SEQ ID NO: 2 and SEQ ID NO: 2A as ST6Gal1 sequences (page 10) and states that suitable ST6Gal1 enzymes may comprise sequences at least 80%, 85%, 90%, 95%, 98%, or 100% identical to these sequences (pages 9-10). This directly supports the claimed ST6Gal1 genus and the portion with sialyltransferase enzymatic activity defined by sequence identity.
Reply: Applicants' arguments have been considered but are found to be non-persuasive for the following reasons. Examiner maintains that there is no support for specific structures SEQ ID NOs: 8, 14, 37-39 as recited in amended claims 7-9.
Information disclosure statement
The information disclosure statement (IDS) submitted on 03/04/2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDS statement is considered and initialed by the examiner.
Withdrawn-Claim Rejections: 35 USC § 102 (AIA )
Previous rejection of claims 4-6, 9 and 16-20 rejected under 35 U.S.C. 102(a)(1) and 35 U.S.C. 102(a)(2) as being anticipated by Prod’Homme et al., (US 10,464,996 B2 in IDS; prior publication data US 2016/0090409 A1, 03/31/2016), is being withdrawn due to claim amendments.
Withdrawn-Claim Rejections: 35 USC § 103
Previous rejection of claims 4-20 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) as applied to claims 4-6, 9 and 16-20 (see 35 U.S.C. 102(a)(1) and 35 U.S.C. 102(a)(2) rejection above) and further in view 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), is being withdrawn due to claim amendments.
Maintained-Claim Rejections: 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(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 4-6 and 11-20 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
The purpose of the written description requirement is to ensure that the inventor had possession, at the time the invention was made, of the specific subject matter claimed. For a broad generic claim, the specification must provide adequate written description to identify the genus of the claim.
“A written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula, [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials." Fiers, 984 F.2d at 1171, 25 USPQ2d 1601; In re Smythe, 480 F.2d 1376, 1383, 178 USPQ 279, 284985 (CCPA 1973) (“In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus.”). Regents of the University of California v. Eli Lilly & Co., 43 USPQ2d 1398.
MPEP § 2163 further states that if a biomolecule is described only by a functional characteristic, without any disclosed correlation between function and structure of the biomolecule, it is "not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed biomolecule.”
“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.” MPEP 2163.
Furthermore, 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 disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure ‘indicates that the patentee has invented species sufficient to constitute the gen[us].’ See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) (‘[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated.’). ‘A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.’ In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004).” MPEP 2163.
The claims recite the following broadly claimed genera:
Claims 4-6 and 11-20 recite a 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 and in the claimed method (no structure is recited in claims).
The structural elements recited in claims 4-6 and 11-20 are not sufficient structure to form a human b-1,4-Galactosyltransferase I (4GalT1) or an enzymatically active portion, a 2,6 sialyltransferase (ST6Gal1) or an enzymatically active portion having no specific structural elements of any kind and having associated activity. There in inherent unpredictability in regards to polypeptides/which amino acid sequences may have the associated function i.e., “human b-1,4-Galactosyltransferase I (4GalT1) or an enzymatically active portion, a 2,6 sialyltransferase (ST6Gal1) or an enzymatically active portion thereof” and possibly fall within the claims and those amino acid sequences that do not have “human b-1,4-Galactosyltransferase I (4GalT1) or an enzymatically active portion, a 2,6 sialyltransferase (ST6Gal1) or an enzymatically active portion thereof”. As such, claims 4-6 and 11-20 recite a genera of biomolecules described only by a functional characteristics, polypeptides/which amino acid sequences may have the associated function i.e., “human b-1,4-Galactosyltransferase I (4GalT1) or an enzymatically active portion, a 2,6 sialyltransferase (ST6Gal1) or an enzymatically active portion thereof”, without any disclosed correlation between function and structure of the biomolecule, it is "not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed biomolecule.” Further, without any structural limitations for structural features that actually provide for “human b-1,4-Galactosyltransferase I (4GalT1) or an enzymatically active portion, a 2,6 sialyltransferase (ST6Gal1) or an enzymatically active portion thereof” activity, claims 4-6 and 11-20 have no defined outer bounds for the scope of “human b-1,4-Galactosyltransferase I (4GalT1) or an enzymatically active portion, a 2,6 sialyltransferase (ST6Gal1) or an enzymatically active portion thereof” activity that fall within the scope of the claims. Due to the literal unlimited structural scope of the claims, it is not possible to provide for a representative number of species that adequately described are representative of the entire genus having no fixed structural outer boundaries. Further, such genera of altered enzymes as recited lack “a precise definition, such as by structure, formula, [or] chemical name, of the claimed subject matter sufficient to distinguish it from other materials” and without any required structure that is sufficient for providing the recited enzyme activity, the recited genera lack 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. The claims lack adequate written description in the as-filed specification for the reasons stated.
No information, beyond the characterization of specific structures SEQ ID NO: 8, and SEQ ID NO: 37, 38 or 39 having b-1,4-Galactosyltransferase I (4GalT1) activity; and SEQ ID NO: 14 having a 2,6 sialyltransferase (ST6Gal1) activity as disclosed in the prior art (see 35 U.S.C. 103 rejection below), method of making and method of use said 4GalT1 and ST6Gal1 (see Examples 1-2, pages 35-38 of specification) has been provided by the applicants’, which would indicate that they had possession of the a 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 and in the claimed method (no structure is recited in claims).
The genus of encoded polypeptides required in the claimed invention is an extremely large structurally and functionally variable genus in the claimed genera of engineered host cells. While the argument can be made that the recited genus of polypeptides is adequately described by the disclosure of the structures of amino acid sequences as disclosed in the characterization of specific structures SEQ ID NO: 8, and SEQ ID NO: 37, 38 or 39 having b-1,4-Galactosyltransferase I (4GalT1) activity; and SEQ ID NO: 14 having a 2,6 sialyltransferase (ST6Gal1) activity as disclosed in the prior art (see 35 U.S.C. 103 rejection below), method of making and method of use said 4GalT1 and ST6Gal1 (see Examples 1-2, pages 35-38 of specification), since one could use structural homology to isolate those polypeptides recited in the claims. The art clearly teaches the “Practical Limits of Function Prediction”: (a) Devos et al., (Proteins: Structure, Function and Genetics, 2000, Vol. 41: 98-107), teach that the results obtained by analyzing a significant number of true sequence similarities, derived directly from structural alignments, point to the complexity of function prediction. Different aspects of protein function, including (i) enzymatic function classification, (ii) functional annotations in the form of key words, (iii) classes of cellular function, and (iv) conservation of binding sites can only be reliably transferred between similar sequences to a modest degree. The reason for this difficulty is a combination of the unavoidable database inaccuracies and plasticity of proteins (Abstract, page 98) and the analysis poses interesting questions about the reliability of current function prediction exercises and the intrinsic limitation of protein function prediction (Column 1, paragraph 3, page 99) and conclude that “Despite widespread use of database searching techniques followed by function inference as standard procedures in Bioinformatics, the results presented here illustrate that transfer of function between similar sequences involves more difficulties than commonly believed. Our data show that even true pair-wise sequence relations, identified by their structural similarity, correspond in many cases to different functions (column 2, paragraph 2, page 105).
(b) Whisstock et al., (Quarterly Reviews of Biophysics 2003, Vol. 36 (3): 307-340, in IDS) also highlight the difficulties associated with “Prediction of protein function from protein sequence and structure”; “To reason from sequence and structure to function is to step onto much shakier ground”, closely related proteins can change function, either through divergence to a related function or by recruitment for a very different function, in such cases, assignment of function on the basis of homology, in the absence of direct experimental evidence, will give the wrong answer (page 309, paragraph 4), it is difficult to state criteria for successful prediction of function, since function is in principle a fuzzy concept. Given three sequences, it is possible to decide which of the three possible pairs is most closely related. Given three structures, methods are also available to measure and compare similarity of the pairs. However, in many cases, given three protein functions, it would be more difficult to choose the pair with most similar function, although it is possible to define metrics for quantitative comparisons of different protein sequences and structures, this is more difficult for proteins of different functions (page 312, paragraph 5), in families of closely related proteins, mutations usually conserve function but modulate specificity i.e., mutations tend to leave the backbone conformation of the pocket unchanged but to affect the shape and charge of its lining, altering specificity (page 313, paragraph 4), although the hope is that highly similar proteins will share similar functions, substitutions of a single, critically placed amino acid in an active-site residue may be sufficient to alter a protein’s role fundamentally (page 323, paragraph 1).
(c) This finding is reinforced in the following scientific teachings for specific proteins in the art that suggest, even highly structurally homologous polynucleotides and encoded polypeptides do not necessarily share the same function. For example, Witkowski et al., (Biochemistry 38:11643-11650, 1999, in IDS), teaches that one conservative amino acid substitution transforms a b-ketoacyl synthase into a malonyl decarboxylase and completely eliminates b-ketoacyl synthase activity. Seffernick et al., (J. Bacteriol. 183(8): 2405-2410, 2001, in IDS), teaches that two naturally occurring Pseudomonas enzymes having 98% amino acid sequence identity catalyze two different reactions: deamination and dehalogenation, therefore having different function. Broun et al., (Science 282:1315-1317, 1998, in IDS), teaches that as few as four amino acid substitutions can convert an oleate 12-desaturase into a hydrolase and as few as six amino acid substitutions can transform a hydrolase to a desaturase.
As stated above, no information beyond the characterization of specific structures SEQ ID NO: 8, and SEQ ID NO: 37, 38 or 39 having b-1,4-Galactosyltransferase I (4GalT1) activity; and SEQ ID NO: 14 having a 2,6 sialyltransferase (ST6Gal1) activity as disclosed in the prior art (see 35 U.S.C. 103 rejection below), method of making and method of use said 4GalT1 and ST6Gal1 (see Examples 1-2, pages 35-38 of specification), has been provided by the applicants’, which would indicate that they had possession of the claimed 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 and in the claimed method (no structure is recited in claims). As the claimed genera of polypeptides having widely variable structures and associated function in the in the claimed method, since minor changes in structure may result in changes affecting function and no additional information (species/variant/mutant) correlating structure with function has been provided. Furthermore, “Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features” (See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895).
Therefore, one skilled in the art cannot reasonably conclude that applicant had possession of the claimed invention at the time the instant application was filed. Applicants are referred to the revised guidelines concerning compliance with the written description requirement of 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Applicants’ have traversed the above written-description with the following arguments: (see pages 9-7 of Applicants’ REMARKS dated 02/27/2026).
Applicants’ argue: “…Under MPEP §2163, functional language can satisfy written description when tied to known structural features that correlate with the claimed function. For ß4GalT1, the specification identifies the luminal catalytic domain as the site of activity (Table 2) and specifies residues involved in manganese binding, UDP-Gal binding, and acceptor substrate interaction (Table 3). Structural stabilizing features, including disulfide bonds and N-linked glycosylation, are also described (Table 4). The specification further explains the underlying enzymatic mechanism, namely transfer of galactose from UDP-Gal to GlcNAc-containing acceptors (pages 14-15), thereby linking these defined structural elements to the observed β4GalT1 activity. Crystallographic analyses (e.g., Harrus et al., attached herewith as Exhibit A; PDB ID: 3CU0) further demonstrate that β4GalT1 contains a structurally defined catalytic pocket and dimer interface, with active-site residues - including Gln318 and residues involved in metal coordination - occupying conserved spatial positions within the catalytic domain. These experimentally determined structural features define the boundaries of the enzymatically active genus. Collectively, these disclosed structural features - conserved catalytic residues, donor- and metal-binding sites, and the luminal catalytic domain architecture confirmed by crystallography - demonstrate that the portion of ß4GalT1 with galactosyltransferase enzymatic activity correspond to a structurally bounded luminal catalytic domain correlated with the recited enzymatic activity…”
Reply: Applicants' arguments have been considered but are found to be non-persuasive for the following reasons. Examiner continues to maintain the rejection for reasons stated on record (dated 10/29/2025) and additionally for the following reasons. Examiner for the record would like to state no Exhibit A or Exhibit B is attached with the response dated 02/27/2026 or in the IDS provided on 03/04/2026.
Contrary to applicants arguments, specifically regarding human b-1,4-Galactosyltransferase I (4GalT1) examiner’s position is supported by the following references:
Harrus et al, (PLOS ONE, October 23, 2018, pages 1-17) disclose random mutations in human b-1,4-Galactosyltransferase I (4GalT1) affects the biochemical properties, including dimerization and enzyme kinetics; see Abstract; Biologic relevance, Fig. 4, pages 8-10; and entire document); and
Malissard et al., (Eur. J. Biochem., 2001, Vol. 268: 4352-4358) also disclose random mutations in human b-1,4-Galactosyltransferase I (4GalT1) affects the biochemical properties, including dimerization and enzyme kinetics; see Abstract; Table 3-4, pages 4355-4356; Discussion; and entire document.
Examiner continues to maintain the following: The claims encompass a large genus of proteins which are substantially unrelated or completely unrelated and includes random mutants of human b-1,4-Galactosyltransferase I (4GalT1), see supporting evidence and arguments presented above in maintaining the written-description rejection. Therefore, the scope of the instant claims are broad despite the guidance of the art and specification, the claims remain not commensurate with evidence of possession or in scope with the enabled invention. An important consideration is that structure is not necessarily a reliable indicator of function. Given this scenario, a skilled artisan needs to be provided with the specific structure associated with the function. The specification does not provide support for the full scope and breadth of the claims, thus examiner continues to hold the position the experimentation left to those skilled in the art is unnecessarily, and improperly extensive and undue. Therefore, taking into consideration the extremely broad scope of the claims, the lack of guidance, the amount of information provided, the lack of knowledge about a correlation between structure and the desired function, and the high degree of unpredictability of the prior art in regard to structural changes and their effect on function, one of ordinary skill in the art would have to go through the burden of undue experimentation in order to practice the claimed invention. Thus, Applicant has not provided sufficient guidance to enable one of ordinary skill in the art to make and use the invention in a manner reasonably correlated with the scope of the claims in the claimed method.
MPEP 2163.II.A.2. (a).i) states, “Whether the specification shows that applicant was in possession of the claimed invention is not a single, simple determination, but rather is a factual determination reached by considering a number of factors. Factors to be considered in determining whether there is sufficient evidence of possession include the level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention”;
Examiner would like to reiterate
“The basic quid pro quo contemplated by the Constitution and the Congress for granting a patent monopoly is the benefit derived by the public from an invention with substantial utility”, [u]nless and until a process is refined and developed to this point-where specific benefit exists in currently available form-there is insufficient justification for permitting an applicant to engross what may prove to be a broad field”, and “a patent is not a hunting license”,[i]t is not a reward for the search, but compensation for its successful conclusion.”
Maintained-Enablement
Claims 4-6 and 11-20 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification is enabling for the characterization of specific structures SEQ ID NO: 8, and SEQ ID NO: 37, 38 or 39 having b-1,4- Galactosyltransferase I (4GalT1) activity; and SEQ ID NO: 14 having a 2,6 sialyltransferase (ST6Gal1) activity as disclosed in the prior art (see 35 U.S.C. 103 rejection below), method of making and method of use said 4GalT1 and ST6Gal1 (see Examples 1-2, pages 35-38 of specification). However, specification does not reasonably provide enablement for a 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 and in the claimed method (no structure is recited in claims). The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands (858 F.2d 731, 8 USPQ 2nd 1400 (Fed. Cir. 1988)) as follows: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claim(s).
Claims 4-6 and 11-20 are so broad as to encompass: a 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 and in the claimed method (no structure is recited in claims). The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of encoded polypeptides broadly encompassed by the claims. Since the amino acid sequence of a protein encoded by a polynucleotide determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence and the respective codons in its polynucleotide, if any, are tolerant of modification and which are conserved (i.e., expectedly intolerant to modification), and detailed knowledge of the ways in which the encoded proteins' structure relates to its function. However, in this case the disclosure is limited to the characterization of specific structures SEQ ID NO: 8, and SEQ ID NO: 37, 38 or 39 having b-1,4-Galactosyltransferase I (4GalT1) activity; and SEQ ID NO: 14 having a 2,6 sialyltransferase (ST6Gal1) activity as disclosed in the prior art (see 35 U.S.C. 103 rejection below), method of making and method of use said 4GalT1 and ST6Gal1 (see Examples 1-2, pages 35-38 of specification). It would require undue experimentation of the skilled artisan to make and use the claimed polypeptides i.e., a 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 and in the claimed method (no structure is recited in claims). The specification but provides no guidance with regard to the making of variants and mutants or with regard to other uses. In view of the great breadth of the claims, amount of experimentation required to make and use the claimed polypeptides, the lack of guidance, working examples, and unpredictability of the art in predicting function from a polypeptide primary structure (for example, see Whisstock et al., Prediction of protein function from protein sequence and structure. Q Rev Biophys. 2003, Aug. 36 (3): 307-340. Review), the claimed invention would require undue experimentation. As such, the specification fails to teach one of ordinary skill how to make and use the full scope of the polypeptides encompassed by the claims. However, claims reading on significant numbers of inoperative embodiments would render claims non-enabled when the specification does not clearly identify the operative embodiments and undue experimentation is involved in determining those that are operative.” Atlas Powder Co. v. E.I. duPont de Nemours & Co., 750 F.2d 1569, 1577, 224 USPQ 409, 414 (Fed. Cir. 1984); In re Cook, 439 F.2d 730, 735, 169 USPQ 298, 302 (CCPA 1971); MPEP 2164.08(b). Here, the claims read on a significant number of inoperative embodiments.
While enzyme isolation techniques, recombinant and mutagenesis techniques are known, and it is not routine in the art to screen for multiple substitutions or multiple modifications as encompassed by the instant claims, the specific amino acid positions within a protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
The specification does not support the broad scope of the claims which encompass: a 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 and in the claimed method (no structure is recited in claims), because the specification does not establish: (A) a rational and predictable scheme for modifying specific amino acid residues in 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 having no specific structural elements and an expectation of obtaining the desired biological/biochemical function; (B) defined core regions/motifs involved in the desired catalytic activity of encoded polypeptide; (C) the tertiary structure of the molecule and folding patterns that are essential for the desired activity and tolerance to modifications; and (D) the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful.
While as discussed above, the specification provides guidance with regard to the characterization of specific structures SEQ ID NO: 8, and SEQ ID NO: 37, 38 or 39 having b-1,4-Galactosyltransferase I (4GalT1) activity; and SEQ ID NO: 14 having a 2,6 sialyltransferase (ST6Gal1) activity as disclosed in the prior art (see 35 U.S.C. 103 rejection below), method of making and method of use said 4GalT1 and ST6Gal1 (see Examples 1-2, pages 35-38 of specification), however, the scope of claims 4-6 and 11-20 is so broad and the lack of guidance either in the specification or in the prior art, the claims remains not commensurate in scope with the enabled invention and therefore for the rejected claims, this would clearly constitute undue experimentation.
Thus, applicants’ have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims broadly including encoded polypeptides with an enormous number of modifications. The scope of the claim must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1975)). Without sufficient guidance, determination of polypeptides/enzymes having the desired biological characteristics is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Although the claims are examined in the light of the specification, specification cannot be read into the claims, i.e., the limitations of the specification cannot be read into the claims (see MPEP 2111 R-5).
Applicants’ have traversed the above enablement rejection with the following arguments: (see pages 17-18 of Applicants’ REMARKS dated 02/27/2026).
Applicants’ argue: “…For the current application, the quantity of experimentation required concerns routine molecular biology and enzymology. Expression of recombinant glycosyltransferases, use of affinity tags, immobilization on solid supports, and in vitro glycosyltransferase activity assays using UDP-Gal or CMP-NANA donors are routine. The specification provides substantial guidance, including enzyme sequences, identification of catalytic domains, substrates (UDP-Gal and CMP-NANA), immobilization strategies, and reaction schemes (e.g., pages 14-15), as well as working examples demonstrating galactosylation and sialylation. The nature of the invention involves use of well-characterized enzymes, and the level of skill in the art is high. The claims set forth polypeptides comprising ß4GalT1 or ST6Gal1 or its portion with galactosyltransferase or sialyltransferase activity, which by definition must retain catalytic enzymatic activity; inoperative variants are excluded. The Office's position would appear to require experimental confirmation for every possible variant, which is not the legal standard. MPEP $2164.01 explicitly states that the specification does not always need to "describe with particularity how to make and use every single embodiment within a claimed class", quoting Amgen Inc. et al. V. Sanofi et al., 598 U.S. 594, 610-11 (2023). Under the Wands framework, the disclosure enables the full scope of the claims without undue experimentation.”
Reply: Applicants' arguments have been considered but are found to be non-persuasive for the following reasons. Applicants’ arguments filed on 02/27/2026 for the traversal of enablement rejection is on similar lines to the arguments presented for traversing the written-description, said arguments have been fully considered but they are not persuasive. Examiner continues to maintain the rejection for reasons stated on record, supporting evidence and arguments presented above in maintaining the written-description rejection also applies to enablement rejection.
For the above cited reasons, examiner is maintaining the written-description and enablement rejection for claims 4-6 and 11-20.
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 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 11-12, 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:
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 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 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, 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 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 19-27 of Applicants’ REMARKS dated 02/27/2025).
Applicants’ argue (A): “…Regarding Schwartz, the Office asserts that it discloses soluble active glycosyltransferases (including ß4GalT1) as fusion proteins having purification tags (including hexahistidine tags), and further asserts that Schwartz uses such enzymes in "solid-phase format" assays. However, even accepting that Schwartz discloses a His-tagged ß4GalT1, Schwartz does not teach the critical claimed configuration in which the enzyme itself is directly immobilized on a solid support via the affinity tag and then used in catalysis as an immobilized enzyme preparation
Reply (A): Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Contrary to applicants’ arguments and assertions, examiner has provided new reference Ito et al., (Biochem., 2010, Vol. 49: 2604-2614) disclose human ß1,4-Galactosyltransferase I (B4GalT1) bound to a solid support/immobilized enzyme that does indeed teach and suggest the structural and functional elements of the instant invention (for details see the rejection above). 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): “…Specifically, Example 2 shows that galactosylation using β4GalT1 immobilized on a solid support via an affinity tag achieves galactosylation levels comparable to those obtained using free, soluble β4GalT1, while requiring approximately 50-80% less enzyme. Importantly, this efficiency gain is relevant in comparison with the method of Schwartz or Mohapatra, which employs soluble enzyme and does not reduce enzyme consumption by performing the reaction on a column or solid phase, but instead uses similar enzyme amounts irrespective of reaction format. The claimed immobilized configuration therefore provides a concrete and practically significant process advantage in overall enzyme usage.”
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 new reference Ito et al., (Biochem., 2010, Vol. 49: 2604-2614) disclose human ß1,4-Galactosyltransferase I (B4GalT1) bound to a solid support/immobilized enzyme that does indeed teach and suggest the structural and functional elements of the instant invention (for details see the rejection above) and conclude “one of the most important characteristics in the immobilization of catalytic enzyme is its stability during repeated use” (see col. 1, paragraph 2, page 2610; and entire document).
Some of the Applicants' arguments are based on superior/unexpected results by the Applicants’ method (see response page 25). 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).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
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 12/19/2025) of co-pending Application No. 17/925,999 (US 2023/0192814 A1); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 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 12/19/2025) of co-pending Application No. 17/925,999 (US 2023/0192814 A1); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 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 12/19/2025) of co-pending Application No. 17/925,999 (US 2023/0192814 A1); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 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 4-20, 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 12/19/2025) of co-pending Application No. 17/925,999 (US 2023/0192814 A1); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 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 page 26 of Applicants’ REMARKS dated 02/27/2026).
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 10/29/2025, as none of the claims are allowed.
Summary of Pending Issues
The following is a summary of issues pending in the instant application.
Upon further review, the instant elected claims 7-9 are only granted the priority date 371 of PCT/US2021/020898 filed on 03/04/2021 as support for the amended claims 7-9 are only found in 371 of PCT/US2021/020898 filed on 03/04/2021.
Claims 4-6 and 11-20 are rejected under 35 U.S.C. 112(a) for written-description and enablement.
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 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 12/19/2025) of co-pending Application No. 17/925,999 (US 2023/0192814 A1); (iii) amended claims 1-5, 7, 15, 37-40 and 45-46 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.
THIS ACTION IS MADE FINAL. 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 extension fee 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.
Regarding filing an After Final amendment, Applicants are directed to MPEP 714.13, which states:
II. ENTRY NOT A MATTER OF RIGHT
It should be kept in mind that applicant cannot, as a matter of right, amend any finally rejected claims, add new claims after a final rejection (see 37 CFR 1.116) or reinstate previously canceled claims. Except where an amendment merely cancels claims, adopts examiner suggestions, removes issues for appeal, or in some other way requires ONLY A CURSORY REVIEW by the examiner (e.g., typographical errors), compliance with the requirement of a showing under 37 CFR 1.116(b)(3) is expected in all amendments after final rejection. An affidavit or other evidence filed after a final rejection, but before or on the same date of filing an appeal, may be entered upon a showing of good and sufficient reasons why the affidavit or other evidence is necessary and was not earlier presented in compliance with 37 CFR 1.116(e). See 37 CFR 41.33 and MPEP § 1206 for information on affidavit or other evidence filed after appeal. (Examiner's emphasis) If more than a cursory review is required, Applicants are referred to CFR §1.114.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to GANAPATHIRAMA RAGHU whose telephone number is (571)272-4533. The examiner can normally be reached on M-F 8:30am-5pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert Mondesi can be reached on 408-918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/GANAPATHIRAMA RAGHU/ Primary Examiner, Art Unit 1652