DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Restriction/Election
Applicant’s election of Group I (Claims 1-11 and 16-18), as well as Applicant’s election of Species 1C (hydrolase), without traverse in the reply filed on 29 October 2025 are acknowledged.
Claims 12-15 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected Group II, there being no allowable generic or linking claim. It is noted that Applicant has canceled the claims representing nonelected Group III (Claims 19 and 20). All limitations related to the nonelected species, are withdrawn from further consideration at this time. Election was made without traverse, in the timely reply filed on 29 October 2025 to the Restriction/Election Office Action mailed on 15 September 2025.
Status of Claims
Claims 1-18 are pending.
Claims 12-15 are withdrawn.
Claims 1-11 and 16-18 are rejected.
Claims 1 and 6 are objected to.
Priority
Applicant’s claim for the benefit of a prior-filed application 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/US2022/014944, filed on 02/02/2022, which claims benefit of 63/144,755, 02/02/2021.
Applicant has complied with all of the conditions for receiving the benefit of an earlier filing date under 35 U.S.C. §120 or §365(c).
Claims 1-11 and 16-18 have the effective filing date of 02 February 2021.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 01 August 2023 and 29 October 2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the Examiner.
Drawings
The drawings were received on 01 August 2023. These drawings are accepted.
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency - The Incorporation by Reference paragraph required by 37 CFR 1.821(c)(1) is missing or incomplete. See item 1) a) or 1) b) above.
Specifically, the incorporation by reference paragraph cites the size of the file in kilobytes (i.e., "105 KB"); however, it should be cited in bytes.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required incorporation-by-reference paragraph, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Claim Objections
Claims 1 and 6 are objected to because of the following informalities:
(1) Claim 1 recites: "...at least one Ubx protein...". However, the acronym "Ubx" should be accompanied by a meaning for the acronym. The specification recites: "FIG. 1 is an exemplary schematic of a fusion protein containing an enzyme fused to an Ultrabithorax (Ubx) protein" (originally-filed specification, pg. 3, para. [0013]). Therefore, claim 1 should read: "...at least one Ultrabithorax (Ubx) protein..."
(2) Claim 6 recites: "The system of claim 2, wherein the enzymes or catalytic fragment thereof...", which should read, for the purpose of claim language consistency, "The system of claim 2, wherein the enzyme or catalytic fragment thereof..."
Appropriate correction is required.
Claim Rejections - 35 U.S.C. § 112
35 U.S.C. § 112(b)
The following is a quotation of 35 U.S.C. §112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. §112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 9 and 10 are rejected under 35 U.S.C. §112(b) or 35 U.S.C. §112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claims 9 and 10 are indefinite, because they recite insufficient, improper or unclear antecedent basis for the limitations in the claim(s).
Claim 9 recites: "The system of claim 1, wherein the fusion protein in each chamber is immobilized."
Claim 10 recites: "The system of claim 1, wherein the enzyme or catalytic fragment of the fusion protein in each chamber is stabilized."
However, the term "chamber" is not recited in claim 1.
For the purpose of compact prosecution, the claims will be interpreted to read: Claim 9- "The system of claim 1, wherein the fusion protein is immobilized"; and Claim 10- "The system of claim 1, wherein the enzyme or catalytic fragment of the fusion protein is stabilized."
Alternatively, the claims could depend from claim 3.
Claim Interpretations
(1) Claim 1 recites an intended use in its preamble language.
Claim 1 recites: "A system for catalytically producing a compound comprising:..."
The phrase as an intended use merely states the purpose or intended uses of the invention, rather than any distinct definition of any of the claimed invention's limitations. Also, the intended use terminology does not limit the structure or method steps of the claimed invention. Therefore, the phrases as intended uses do not limit the scope of the claimed subject matter. (See MPEP 2111.02 (I)(II).) That is, the intended use recited in the preamble does not result in a structural or manipulative difference between the claimed invention and the prior art. Deletion of the preamble phrase does not affect the structure or steps of the claimed invention (MPEP 2111.02 (II)).
However, at the discretion of the Examiner, the intended use limitation may be indicated if shown in the prior art.
(2) Claim 1 recites: "A system...comprising: one or more solid matrices comprising a fusion protein,..."
The specification recites: The terms 'solid phase', 'support', 'scaffold', and 'matrices' are used herein interchangeably, and refer to the solid material (e.g., Ubx material structure formed by two or more, i.e., a plurality of Ubx polypeptides) that provides a physical structure to immobilize an enzyme or a catalytic fragment thereof" (originally-filed specification, pg. 7, para. [0041] thru pg. 8, cont. para. [0041]).
That is, the term 'solid matrix' or 'solid matrices' is interpreted to refer to the physical association between the Ubx protein and the enzyme or catalytic fragment thereof, and the three-dimensional complex that it forms.
For the purpose of examination, any reference which shows a fusion protein comprising at least one Ubx protein and an enzyme or a catalytic fragment thereof (as well as any terms relating to said at least one Ubx protein) will be interpreted to address the limitation 'one or more solid matrices'.
For example, Bondos et al. (Pub. No. US 2010/0143436 (cited below in the prior art rejections)) shows a composition comprising a biomaterial. The biomaterial may comprise for example, a Ubx protein (pg. 3, para. [0025]). In some embodiments, the biomaterial comprises a Ubx fusion protein in which a Ubx protein is fused with at least one other protein (pg. 4, para. [0030]). That is, the term 'biomaterial' as described in Bondos et al. will be considered to be a solid matrix.
Claim Rejections - 35 U.S.C. § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. §102 and §103 (or as subject to pre-AIA 35 U.S.C. §102 and §103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. §102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claim 1 is rejected under 35 U.S.C. §102(a)(1) as being anticipated by Kim et al. (Proc. Natl. Acad. Sci. USA, 1994, 91: 883-887).
Regarding claim 1, pertaining to a system for catalytically producing a compound comprising: one or more solid matrices comprising a fusion protein, wherein the fusion protein comprises at least one Ubx protein and an enzyme or catalytic fragment thereof,
[See Claim Interpretations section- (1) and (2) above.]
Kim et al. shows the construction of a chimeric restriction endonuclease by linking the Drosophila Ultrabithorax (Ubx) homeodomain to the cleavage domain (FN) of Fok I restriction endonuclease (pg. 883, column 1, Abstract). A schematic representation of the engineered Ubx-FN hybrid protein is shown in Fig. 1 (pg. 884, column 2, para. 1; and Fig. 1 [i.e., a solid matrix]).
Claims 1-2, 6, 8 and 18 are rejected under 35 U.S.C. §102(a)(1)/(a)(2) as being anticipated by Bondos et al. (Pub. No. US 2010/0143436 A1).
Regarding claim 1, pertaining to a system for catalytically producing a compound comprising: one or more solid matrices comprising a fusion protein, wherein the fusion protein comprises at least one Ubx protein and an enzyme or catalytic fragment thereof, and regarding claim 18,
[See Claim Interpretations section- (1) and (2) above.]
Bondos et al. shows a composition comprising a biomaterial. The biomaterial may comprise for example, a Ubx protein (pg. 3, para. [0025]). In some embodiments, the biomaterial comprises a Ubx fusion protein in which a Ubx protein is fused with at least one other protein (pg. 4, para. [0030]). A protein in a Ubx fusion protein may comprise all or part of an enzyme (pg. 4, para. [0031]). Ubx may, under some conditions, self-associate into fibrils (e.g., nanoscale fibrils) and/or fibrils may self-assemble into higher-order structures such as fibers (pg. 4, para. [0032] [i.e., a solid matrix]).
Regarding claim 2, pertaining to two solid matrices,
Bondos et al. shows that, according to some embodiments, a method of preparing a product from one or more reactants may comprise (a) providing a serial fiber having a first domain comprising a first chimera comprising a first Ubx protein and a first catalyst and a second domain comprising a second chimera comprising a second Ubx protein and a second catalyst (pg. 2, para. [0010] [i.e., producing a compound]).
Regarding claim 6, the first catalyst is operable to react with at least one reactant to form at least one intermediate and the second catalyst is operable to react with the at least one intermediate to produce the product (pg. 2, para. [0010]).
Regarding claim 8, in some embodiments, the first catalyst may be a first enzyme, the second catalyst may be a second enzyme, or the first catalyst may be a first enzyme and the second catalyst may be a second enzyme. A first Ubx protein in some embodiments, may be the same as or different from a second Ubx protein (pg. 2, para. [0010]).
Claim 11 is rejected under 35 U.S.C. §102(a)(1)/(a)(2) as being anticipated by Bondos et al. (Pub. No. US 2010/0143436 A1) as evidenced by ABSS sequence search ((SEQ ID NO.: 5); Downloaded on 26 November 2025, pp. 1-3).
Regarding claim 11, a Ubx protein may comprise an amino acid sequence selected from full length Ubx protein (SEQ ID NO:3), Ubx protein (SEQ ID NO:3) missing residues 19-48, Ubx protein (SEQ ID NO:3) comprising residues 216-356, and Ubx protein (SEQ ID NO:3) comprising residues 88-243 in some embodiments (pg. 1, para. [0007]).
Bondos et al. does not show that SEQ ID NO.: 3 is a Ubx protein comprising an amino acid sequence having at least 90% identity to instant SEQ ID NO: 5, or a fragment thereof.
ABSS sequence search shows that SEQ ID NO.: 3, shown by Bondos et al., has 100% identity with instant SEQ ID NO.: 5.
Claim 16 is rejected under 35 U.S.C. §102(a)(1)/(a)(2) as being anticipated by Alexandru et al. (Pub. No. US 2009/0192084 A1) as evidenced by Szanto et al. (J. Chem. Theory Comput. 2025, 21: 9459-9469).
Regarding claim 16, pertaining to hydrolase [species election] and a ligase,
Alexandru et al. shows complexes comprising UBX-domain-containing polypeptides (UBX-polypeptides) (pg. 1, para. [0003]). In certain aspects, the described disclosure relates to the associations between p97 and other proteins, including UBX-domain-containing proteins (UBX-polypeptides), HIF1α, and a variety of E3 ligases (pg. 4, para. [0031] [nexus to Bondos et al.- Ubx fusion protein comprising Ubx protein and an enzyme]). In one aspect, methods for identifying an active agent that regulates a complex comprising an UBX-polypeptide and a p97 polypeptide is provided (pg. 1, para. [0007]). The p97-UBX-polypeptide complex may further comprise at least one additional component selected from an E3-ligase, a subunit or polypeptide of an E3-ligase (pg. 1, para. [0007] thru pg. 2, cont. para. [0007]).
Alexandru et al. does not show that the p97 polypeptide is a hydrolase.
Szanto et al. teaches that p97 is a member of the AAA+ protein super family of ATPases that binds, hydrolyzes, and releases ATP to regulate various cellular pathways (pg. 9459, column 1, para. 1 [i.e., it is a hydrolase]).
Claim Rejections - 35 U.S.C. § 103
The following is a quotation of 35 U.S.C. §103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102 of this title, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. §102(b)(2)(C) for any potential 35 U.S.C. §102(a)(2) prior art against the later invention.
Claims 1-6, 8-10 and 18 are rejected under 35 U.S.C. §103 as being unpatentable over Bondos et al. (Pub. No. US 2010/0143436 A1) in view of Ono et al. (Lab Chip, 2008, 8: 2168-2173).
Bondos et al. addresses the limitations of claims 1-2, 6, 8 and 18 in the 35 USC §102(a)(1)/(a)(2) rejection above.
Bondos et al. does not explicitly show: 1) reaction chambers [Claims 3, 4 and 5]; and 2) the fusion protein is immobilized in each chamber [Claim 9]; and 3) the enzyme or catalytic fragment of the fusion protein is stabilized in each chamber [Claim 10].
Ono et al. provides information from which one of ordinary skill in the art would have been motivated to have incorporated the biomaterial comprising a(n) Ubx fusion protein, as shown by Bondos et al., into a system comprising reaction chambers, by way of addressing the limitations of claims 3, 4, 5, 9 and 10.
Regarding claims 3, 4 and 5, Ono et al. shows that a microfluidic chip carrying three reaction chambers was designed and constructed to examine sequential multiple enzymatic reactions (pg. 2168, Abstract [nexus to Bondos et al.- fiber with two domains comprising biomaterial involved in sequential enzymatic/catalytic reactions]). Three sequential glycosyltransfer reactions on a chip succeeded in the synthesis of a tetrasaccharide using immobilized enzymes (pg. 2168, Abstract [nexus to Bondos et al.- catalytically producing a compound]). Figure 1 shows the reaction chambers in fluidic communication with each other (pg. 2169, column 2, Fig. 1).
Regarding claim 9, the described heterogeneous system is based on immobilized enzymes (pg. 2168, column 2, lines 7-9).
Regarding claim 10, sequential enzymatic glycosylation reactions using glycosyltransferases were investigated using a microfluidic chip carrying multiple reaction chambers. The necessary enzymes were expressed as fused proteins, which were supported on agarose beads (pg. 2172, column 2, para. 1 [i.e., the enzymes were functional; therefore, the enzymes were stable]).
Accordingly, it would have been obvious to one of ordinary skill in the art at the time that the claimed invention was made, to have modified the system/biomaterial comprising one or more solid matrices comprising a fusion protein, in turn, comprising at least one Ubx protein and an enzyme or catalytic fragment thereof, as shown by Bondos et al., by incorporating the Ubx fusion protein biomaterial into a device with reaction chambers for immobilizing and stabilizing said biomaterial [Claims 3, 4, 5, 9, 10], as shown by Ono et al., with a reasonable expectation of success, because Bondos et al. shows a system as a serial fiber which comprises a first and second domain each containing a Ubx-enzyme fusion protein, which is analogous to the reaction chambers (e.g., as domains) containing enzymes, shown by Ono et al. (MPEP 2143 (I)(G)).
Although Bondos et al. does not explicitly describe the Ubx fusion protein biomaterial as 'immobilized' or 'stabilized' in reaction chambers, one of ordinary skill in the art would have understood that, for the serial fiber system described by Bondos et al. to successfully prepare a product, the first and second Ubx fusion proteins with enzyme catalysts would need to be immobilized in the described separate (first and second) domains, and the enzyme catalysts would need to be functional (i.e., stabilized) (MPEP 2143 (I)(G); MPEP 2144 (I)).
One of ordinary skill in the art would have been motivated to have made those modifications, because Ono et al. teaches that the described results showed that glycosylation was enhanced in the microchannel compared with the batch reaction due to the lack of product inhibition and the size effect of the microchannel (pg. 2172, column 2, para. 1). That is, Ono et al. teaches that in a system in which immobilized enzymes are used to produce a compound or product the incorporation of fluidically-connected reaction chambers enhances the enzymatic reactions and product formation.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill at the time the invention was made.
Claim 7 is rejected under 35 U.S.C. §103 as being unpatentable over Bondos et al. in view of Ono et al., as applied to claims 1-6, 8-10 and 18 above, and further in view of Alexandru et al. (Pub. No. US 2009/0192084 A1) as evidenced by Szanto et al. (J. Chem. Theory Comput. 2025, 21: 9459-9469).
Bondos et al. in view of Ono et al., as applied to claims 1-6, 8-10 and 18 above, do not show: 1) the enzyme or catalytic fragment thereof is an oxidoreductase, a transferase, a hydrolase [species election], a lyase, a ligase, an isomerase, or a catalytic fragment thereof [Claim 7].
Alexandru et al. shows complexes comprising UBX-domain-containing polypeptides (UBX-polypeptides) (pg. 1, para. [0003]). In certain aspects, the described disclosure relates to the associations between p97 and other proteins, including UBX-domain-containing proteins (UBX-polypeptides), HIF1α, and a variety of E3 ligases (pg. 4, para. [0031] [nexus to Bondos et al.- Ubx fusion protein comprising Ubx protein and an enzyme]).
Regarding claim 7, pertaining to a hydrolase [species election] and a ligase,
Alexandru et al. shows that, in one aspect, methods for identifying an active agent that regulates a complex comprising an UBX-polypeptide and a p97 polypeptide is provided (pg. 1, para. [0007]). The p97-UBX-polypeptide complex may further comprise at least one additional component selected from an E3-ligase, a subunit or polypeptide of an E3-ligase (pg. 1, para. [0007] thru pg. 2, cont. para. [0007]).
Alexandru et al. does not show that the p97 polypeptide is a hydrolase.
Szanto et al. teaches that p97 is a member of the AAA+ protein super family of ATPases that binds, hydrolyzes, and releases ATP to regulate various cellular pathways (pg. 9459, column 1, para. 1 [i.e., it is a hydrolase]).
Accordingly, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, to have modified the system/biomaterial comprising one or more solid matrices comprising a fusion protein, in turn, comprising at least one Ubx protein and an enzyme or catalytic fragment thereof, as shown by Bondos et al. in view of Ono et al., as applied to claims 1-6, 8-11 and 18 above, by incorporating a hydrolase [species election] or ligase as the enzyme or catalytic fragment thereof [Claim 7], as shown by Alexandru et al. as evidenced by Szanto et al., with a reasonable expectation of success, because Alexandru et al. shows Ubx fusion proteins which contain enzymes, which is the type of Ubx fusion protein shown by Bondos et al. (MPEP 2143 (I)(G)).
One of ordinary skill in the art would have been motivated to have made those modifications, because Ono et al. teaches that the described results showed that glycosylation was enhanced in the microchannel compared with the batch reaction due to the lack of product inhibition and the size effect of the microchannel (pg. 2172, column 2, para. 1). That is, Ono et al. teaches that in a system in which immobilized enzymes are used to produce a compound or product the incorporation of fluidically-connected reaction chambers enhances the enzymatic reactions and product formation.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill at the time the invention was made.
Claims 16 and 17 are rejected under 35 U.S.C. §103 as being unpatentable over Alexandru et al. (Pub. No. US 2009/0192084 A1) as evidenced by Szanto et al. (J. Chem. Theory Comput. 2025, 21: 9459-9469) in view of Tsai et al. (Adv. Funct. Mater. 2015, 25: 1442-1450).
Alexandru et al. as evidenced by Szanto et al. addresses the limitations of claim 16 in the 35 USC §102(a)(1)/(a)(2) rejection above.
Alexandru et al. as evidenced by Szanto et al. does not show: 1) the enzyme or catalytic fragment of the fusion protein has increased stability as compared to the enzyme or catalytic fragment when it is not fused to the Ubx protein [Claim 17].
Tsai et al. addresses the limitations of claim 17.
Tsai et al. shows the generation of four proteins fused to Ubx, which retain their function once incorporated into materials (pg. 1443, column 1, last para. thru column 2, line 1). Table 1 shows the properties of various proteins fused to Ubx, which includes enzymes (pg. 1444, Table 1, entry "Enzymes" [nexus to Alexandru et al.- a Ubx fusion protein comprising an enzyme]).
Regarding claim 17, Tsai et al. shows that Ubx protein fusions were more stable than as free monomers (pg. 1444, column 2, para. 2.2 Title). The described results imply that Ubx fibers remarkably stabilize proteins incorporated by gene fusion. These results are consistent with prior studies by other laboratories in which immobilization improved enzyme efficiency or stability (pg. 1445, column 1, last six lines of cont. para. 2.2).
Accordingly, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, to have understood that the fusion protein comprising at least one Ubx protein and an enzyme or catalytic fragment thereof, such as a hydrolase or a ligase, as shown by Alexandru et al. as evidenced by Szanto et al., would have exhibited increased stability compared to the enzyme when not fused to the Ubx protein [Claim 17], with a reasonable expectation of success, because Tsai et al. teaches that the enzymes incorporated into Ubx fusion proteins have improved stability vs. their unfused counterparts (MPEP 2143 (I)(G)).
One of ordinary skill in the art would have been motivated to have made that modification, because one of ordinary skill in the art of incorporating enzymes into catalytic reactions would prefer to immobilize said enzymes into platforms (for example, as a Ubx fusion protein) which increase the stability of said enzymes, thereby maximizing the activity and, therefore, productivity of the catalytic reaction.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill at the time the invention was made.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the "right to exclude" granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP 2159. See MPEP 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/ patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/ patents/apply/applying-online/eterminal-disclaimer.
(1) Claim 1 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 7 and 10 of Patent No. 11,059,872 B2.
The claimed subject matter of instant Application No. 18/263,833 is:
Claim 1. A system for catalytically producing a compound comprising: one or more solid matrices comprising a fusion protein, wherein the fusion protein comprises at least one Ubx protein and an enzyme or catalytic fragment thereof.
The claimed subject matter of Patent No. 11,059,872 is:
Claim 1. A biomaterial composition comprising two or more self-assembled Ultrabithorax (Ubx) proteins, wherein at least one of the two or more self-assembled Ubx proteins is a fusion protein in which the Ubx protein is fused with at least one other protein.
Claim 7. The other protein is selected from the group consisting of all or part of an enzyme, an enzyme inhibitor, an antigen,..., an extracellular matrix, and a ligand binding factor.
Claim 10. A biomaterial structure having a fibril film fiber sheet, bundle, lattice, scaffold or encapsulate morphology and comprising the biomaterial composition of claim 1.
Although the claims are not identical, they are not patentably distinct from each other because, as demonstrated above in the claim sets from each application, the biomaterial composition and biomaterial structure comprising at least one Ubx protein fused to an enzyme, described in Patent No. 11,059,872 B2 anticipates the system comprising a fusion protein comprising at least one Ubx protein and an enzyme, described in instant Application No. 18/263,833.
(2) Claim 1 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 6 of Patent No. 12,275,765 B2.
The claimed subject matter of instant Application No. 18/263,833 is:
Claim 1. A system for catalytically producing a compound comprising: one or more solid matrices comprising a fusion protein, wherein the fusion protein comprises at least one Ubx protein and an enzyme or catalytic fragment thereof.
The claimed subject matter of Patent No. 12,275,765 is:
Claim 1. A biomaterial comprising two or more self-assembled Ultrabithorax (Ubx) proteins, wherein at least one of the two or more self-assembled Ubx proteins is a fusion protein in which the Ubx protein is fused with at least one other protein. The Ubx protein comprises a sequence having at least 95% identity to SEQ ID NO.: 3.
Claim 6. The other protein is selected from the group consisting of all or part of an enzyme, an enzyme inhibitor, an antigen,..., an extracellular matrix, and a ligand binding factor.
Although the claims are not identical, they are not patentably distinct from each other because, as demonstrated above in the claim sets from each application, the biomaterial comprising at least one Ubx protein fused to an enzyme, described in Patent No. 12,275,765 B2 anticipates the system comprising a fusion protein comprising at least one Ubx protein and an enzyme, described in instant Application No. 18/263,833.
Conclusion
No claims are allowed.
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/SMP/Examiner, Art Unit 1651
/Michelle F. Paguio Frising/Primary Examiner, Art Unit 1651