Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Priority
This application is a 371 of PCT/KR2021/015411 filed on 10/29/2021. PCT/KR2021/015411 claims foreign priority to 10-2020-0143546 KR filed 10/30/2020 and 10-2021-0006608 KR filed 01/18/2021.
Should applicant desire to obtain the benefit of foreign priority under 35 U.S.C. 119(a)-(d) prior to declaration of an interference, a certified English translation of the foreign application must be submitted in reply to this action. 37 CFR 41.154(b) and 41.202(e).
Failure to provide a certified translation may result in no benefit being accorded for the non-English application.
Election/Restrictions
Applicant’s election without traverse of Group I (Claims 60-74) in the reply filed on 02/03/2026 is acknowledged. Claims 75-80 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected methods for visualizing host cell distribution and cancer treatment, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 02/03/2026. Applicant’s election without traverse of Ribosome Binding Site (RBS), and SEQ. ID NO. 5. in the reply filed on 02/03/2026 is acknowledged.
Claim Status
Claims 60-74 are pending and under examination. Claim 60 is the only independent claim.
Specification
The specification is objected to because the use of improperly demarcated trademarks has been noted in this application. Although the use of trademarks is permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner that might adversely affect their validity as trademarks. See MPEP §608. 01(v). 9. Examples of such an improperly demarcated trademarks “NUPACK”, “UNAfold”, and “pBlueScript” which appears in the present specification in paragraphs [0034], [0034], and [0065], respectively. Examiner notes that the provided examples are not meant to be a complete list of improperly demarcated trademarks found in the present specification. Applicant should review the entire specification and correct all instances of improperly demarcated trademarks. Appropriate corrections required. Each letter of a trademark should be capitalized or otherwise the trademark should be demarcated with the appropriate symbol indicating its proprietary nature (e.g., ™, ©, ®) and accompanied by generic terminology. Applicants may identify trademarks using the USPTO's trademark database. Trademark Electronic Search System (TESS), on the Internet at https://tmsearch.uspto.go
Claim Interpretation
For purposes of examination, certain claim terms that are broad or otherwise require construction have been interpreted in accordance with their broadest reasonable interpretation consistent with the specification, as is required during prosecution. See MPEP 2111; In re Am. Acad. of Sci. Tech. Ctr., 367 F.3d 1359, 1369, 70 USPQ2d 1827, 1834 (Fed. Cir. 2004). The following claim constructions have been applied in this office action.
Regulatory Gene - Under the broadest reasonable interpretation consistent with the specification, a regulatory gene is a nucleic acid fragment that “regulates the expression of a gene encoding monomeric streptavidin” wherein the transcription and/or translation of the gene are either activated or inhibited (see [0018]). As examples, the regulatory gene structurally comprises one or more of the following elements: “site for DNA-dependent RNA polymerase, transcription initiation sites and binding sites for transcription factors, repressor and activator protein binding sites, and any other sequences of nucleotides known to those skilled in the art to act directly or indirectly to regulate the amount of transcription” (see [0019]) “a ribosome binding site (RBS), a 5'-untranslated region (5'-UTR)”,which act directly or indirectly to regulate the amount of translation (see [0021]). The regulatory gene is “operably linked 5' upstream of the initiation codon of the gene encoding the monomeric streptavidin” (see [0020]).
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 67 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
The claims require that a “regulatory gene” causes expression of monomeric streptavidin in the periplasm of the host cell. The specification describes a “regulatory gene” as including elements such as ribosome binding sites, promoters, and transcription factor binding sites. These elements are known to regulate at the transcription and translation levels, but do not direct subcellular localization of proteins. Expression of proteins in the periplasm requires signal peptides or secretion sequences that direct proteins through cellular export pathways, and such elements are not disclosed as part of the regulatory gene (see Karyolaimos et al. (Frontiers in Bioengineering and Biotechnology, 2021), pg. 3 left col. 1st para.). The specification teaches using a secretion sequence with mannose binding protein (MBP) fused monomeric streptavidin (mSA) in plasmids involved in example 4 of the specification. This is not a known signal peptides or secretion sequences that direct proteins through cellular export pathways. Though the specification does not teach how the claimed result, periplasmic expression, can be achieved using the recited regulatory gene, and a person of ordinary skill in the art would not be able to practice the full scope of the claimed invention without undue experimentation. Therefore, the claims are not enabled.
In determining whether the specification enables the full scope of the claimed invention, the factors set forth in In re Wands have been considered.
(A) The breadth of the claims: The breadth of the claims is significant, as the claims require that a regulatory gene causes expression of monomeric streptavidin in the periplasm of a host cell. The claims are not limited to any particular sequence, mechanism, or structural feature that would direct localization to the periplasm, thereby encompassing a wide range of embodiments without corresponding guidance in the specification.
(B) The nature of the invention: The nature of the invention involves recombinant protein expression and subcellular localization. Achieving expression of a protein in the periplasm requires specific biological mechanisms, including the use of signal peptides or secretion sequences that direct proteins through cellular export pathways.
(C) The state of the prior art: The art is silent towards regulatory genes that control cellular localization in gram-negative bacteria. The state of the prior art establishes that “[t]o reach the periplasm, a protein has to be equipped at its N-terminus with a cleavable signal peptide so that it can cross the cytoplasmic membrane” (see Karyolaimos et al. (Frontiers in Bioengineering and Biotechnology, 2021), pg. 3 left col. 1st para.). Periplasmic localization of proteins is achieved through known mechanisms such as signal peptides (e.g. MalE, PelB, OmpA, DsbA, PhoA) that direct proteins to the periplasm via secretion pathways. Mirzadeh et al. (Microb. Cell Fact., 2020) teaches that while different signal peptides impact periplasmic localization for recombinant proteins in an unpredictable manner (see pg. 1 Background) and that changes to the translation initiation region may help overcome this unpredictability, the signal peptides are still required (see pg. 1 Results). Such mechanisms are distinct from regulatory sequences that control transcription or translation levels. Given that the state of the art has established that signal peptide is required for periplasmic localization, a person of ordinary skill in the art would not be able to make/use the invention without undue experimentation because the claimed mechanism contradicts known periplasmic localization mechanisms and the art is silent to a regulatory gene controlling cellular localization.
(D) The level of one of ordinary skill: The level of ordinary skill in the art is relatively high, as practitioners in the field of molecular biology and recombinant protein expression are familiar with gene expression systems and protein targeting mechanisms. However, even a person of ordinary skill would require appropriate guidance to achieve the claimed results using the specific elements recited in the claims.
(E) The level of predictability in the art: Although aspects of recombinant protein expression are generally predictable, the predictability of achieving subcellular localization using the elements described in the specification is limited. In particular, regulatory sequences such as promoters and ribosome binding sites are not known to control protein localization, and therefore do not predictably result in periplasmic expression.
(F) The amount of direction provided by the inventor: The specification provides minimal direction or guidance regarding how to achieve periplasmic expression using the claimed regulatory gene. While regulatory elements such as promoters and ribosome binding sites are described, the specification does not teach the sue of signal peptides or other localization sequences required to direct proteins to the periplasm.
(G) The existence of working examples: The specification does not provide working examples demonstrating expression of monomeric streptavidin in the periplasm of a host cell using the claimed regulatory gene. In example 4 of the specification, the applicants utilized a plasmid containing a secretion sequence with the MBP-mSA fusion, which is separate from the claimed regulatory gene. The absence of examples using the regulatory gene to drive periplasmic expression weighs against enablement, particularly given the specific localization required by the claims.
(H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure: The quantity of experimentation required to practice the full scope of the invention would be substantial. A person of ordinary skill in the art would need to identify and incorporate appropriate signal peptides or secretion mechanisms not disclosed in the specification, and further determine how to achieve the claimed periplasmic expression, thereby requiring undue experimentation.
Considering the above factors together, undue experimentation would be required for a person of ordinary sill in the art to practice the full scope of the claimed invention. Accordingly, claim 67 is not enabled.
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.
Claim 65, 68-69 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Where applicant acts as his or her own lexicographer to specifically define a term of a claim contrary to its ordinary meaning, the written description must clearly redefine the claim term and set forth the uncommon definition so as to put one reasonably skilled in the art on notice that the applicant intended to so redefine that claim term. Process Control Corp. v. HydReclaim Corp., 190 F.3d 1350, 1357, 52 USPQ2d 1029, 1033 (Fed. Cir. 1999). The term “regulatory gene” in claims 65-72 is used by the claim to mean “non-coding regulatory sequences,” while the accepted meaning is “a segment of DNA that contains instructions for building one or more molecules (see NIH, “Gene”). The term is indefinite because the specification does not clearly redefine the term.
Furthermore, Claims 65 recites the limitation "the gene encoding monomeric streptavidin" in line 2. There is insufficient antecedent basis for this limitation in the claim.
The term “total Gibbs free energy change (ΔGtotal)” in claims 68 is indefinite. The claim recite the “regulatory gene has a total Gibbs free energy change of (ΔGtotal) of 0 or less.” However, a gene, as a sequence of nucleotides, does not inherently possess a Gibbs free energy change absent a defined process or interaction. Gibbs free energy change is a thermodynamic parameter that depends on specific conditions and interactions, such as RNA folding, ribosome binding, or hybridization, none of which are specified in the claim. It is therefore unclear what physical or biochemical process the recited ΔGtotal refers to, and a person of ordinary skill in the art would not be able to determine the scope of the claim with reasonable certainty. Accordingly, the claim is indefinite.
The term “translation initiation rate controlled within a predetermined range” in claim 69 is indefinite. The claim recites that “the regulatory gene has a translation initiation rate (TIR) controlled within a predetermined range.” However, translation initiation rate is not a property of a gene itself, but rather a property of the process of translation of an mRNA molecule, which depends on factors such as ribosome binding, mRNA secondary structure, and cellular conditions. It is therefore unclear how a gene, as a nucleotide sequence, can be said to “have” a translation initiation rate. Additionally, the phrase “controlled within a predetermined range” lacks clarity, as the claim does not specify the range, the method of control, or how the translation initiation rate is measured. Accordingly, a person of ordinary skill in the art would not be able to determine the scope of the claim with reasonable certainty, and the claim is indefinite.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 61 and 62 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. The “for an in vivo cell tracking platform” and “for a cancer pretargeting platform” limitations of claims 61 and 62, respectively, are intended uses that do not structurally distinguish the claimed composition from the composition of claim 60. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 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 (i.e., changing from AIA to pre-AIA ) 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.
Claims 60-66, and 70-74 are rejected under 35 U.S.C. 102(a)(1)/102(a)(2) as being anticipated by Demonte et al. (“Expression and purification of soluble monomeric streptavidin in Escherichia coli”, Applied Microbiology and Biotechnology, 2014, on IDS, as evidenced by Addgene plasmid #52319).
In regards to claim 60, Demonte teaches “A composition comprising host cells transformed by introduction of a gene encoding biotin-biotin protein thereinto” (see pg. 6286 right col. last para., disclosing transformation methods for generating a culture of E. coli expressing monomeric streptavidin).
In regards to claims 61 and 62, Demonte teaches the composition of claim 60, and while the “for an in vivo cell tracking platform” and “for a cancer pretargeting platform” limitations are intended uses that do not structurally distinguish the claimed composition from the composition of claim 60 or that disclosed in Demonte, Demonte does disclose application such as “detection, purification, labeling,
crosslinking, and immobilization” and other molecular recognition systems, which would be expected to be part of a “cell tracking platform” or “cancer pretargeting platform” as claimed (see “Introduction, 1st para.).
In regards to claim 63, Demonte teaches that the biotin binding protein is monomeric streptavidin (see Title, Abstract, plasmid map, and throughout).
In regards to claim 64, Demonte teaches expressing the monomeric streptavidin as a fusion protein in an effort to improve solubility and expression of the recombinant protein (see Abstract).
In regards to claims 65 and 66, Demonte teaches regulatory elements that control expression within the construct, including T7 promoter which regulates expression of the gene encoding the biotin-binding protein. Such promoters and associated regulatory sequences are well known in the art to control transcription and expression of recombinant genes in host cells. Demonte further teaches that the construct comprises an ribosome binding site (RBS), that helps regulate ribosome binding and subsequent protein production (see map for plasmid #52319). These components read on the limitation requiring “a regulatory gene that regulates expression of the gene encoding monomeric streptavidin“ in claim 65 and include the RBS from the group in claim 66.
In regards to claim 70 and 71, Demonte teaches the use of a ribosome binding site with a sequence length of 15-39 bp (23 bp), which comprises SEQ ID 5 (AGG). Furthermore, Demonte also teaches a T7 promoter sequence which is 19 bp in length and includes SEQ IDS. 5-7 (ATAGG).
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In regards to claim 72, as shown above in regards to claims 70 and 71, the spacing between SEQ ID: 5 and the start of the gene encoding monomeric streptavidin is between 6 to 13 bp.
In regards to claim 73, Demonte demonstrates transforming E. coli to express biotin binding fusion protein construct (see Demonte pg. 6286 right col. last para.).
In regards to claim 74, Demonte teaches compositions of cells transformed by induction of a gene encoding biotin-binding protein thereinto (monomeric streptavidin) and biotinylated compounds (biotinylated ligands; see pg. 6285 right col. 2nd para.)
Claim Rejections - 35 USC § 103
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 (i.e., changing from AIA to pre-AIA ) 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 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 60-67 and 70-74 are rejected under 35 U.S.C. 103 as being unpatentable over Demonte et al. (Applied Microbiology and Biotechnology, 2014, as evidenced by Addgene plasmid #52319) as applied to claims 60-66, and 70-74 above, and included here for reasons supra, in view of Dammeyer et al. (“Broad host range vectors for expression of proteins with (Twin-) Strep-tag, His-tag and engineered, export optimized yellow fluorescent protein”, Microbial Cell Factories, 2013, as evidence by Addgene plasmid #45944).
In regards to claim 67, Demonte teaches a gene construct comprising a gene encoding a biotin-binding protein, namely monomeric streptavidin, fused to a fusion partner (MBP) for improving solubility and expression, and further comprising regulatory sequences including a ribosome binding site that regulate expression of the encoded protein. Demonte additionally teaches that the construct is engineered to produce soluble protein and reduce formation of inclusion bodies during expression in Escherichia coli. Demonte does not teach expression in the periplasm of a host cell.
Dammeyer teaches that recombinant proteins expressing in E. coli may be directed to the periplasmic space through the use of signal peptides, such as PelB leader sequence, and that periplasmic expression provides advantages including enhanced protein folding and disulfide bond formation (see Dammeyer pg. 3 left col. 2nd para.). Dammeyer further teach that periplasmic targeting via such signal sequences results in localization of expressed proteins in the periplasm of the host cell (see Dammeyer Fig. 4).
It would have been prima facie obvious to one of ordinary skill in the art at the time of filing to modify the construct of Demonte to include a signal peptide, such as the PelB leader sequence taught by Dammeyer in order to direct expression of the monomeric streptavidin to the periplasm of the host cell. Such as modification would have been motivated by the well-known advantages of periplasmic expression, including improved protein folding and formation of disulfide bonds, particularly for proteins prone to misfolding or aggregation.
Although Demonte utilizes cytoplasmic expression conditions, including engineered host strains, to promote proper folding and reduce inclusion body formation, this does not teach away from periplasmic expression. Rather, it reflects one of multiple known strategies in the art for improving protein folding and solubility. Dammeyer, explicitly teaches an alternative approach, periplasmic targeting via signal peptides, to achieve a similar goal. A person of ordinary skill in the art would have recognized these approaches as interchangeable and would have selected between them as a matter of routine optimization depending on the desired expression outcome.
Claims 60-74 are rejected under 35 U.S.C. 103 as being unpatentable over Demonte et al. (Applied Microbiology and Biotechnology, 2014, as evidenced by Addgene plasmid #52319) in view of Dammeyer et al. (Microbial Cell Factories, 2013, as evidence by Addgene plasmid #45944) as applied to claims 60-67 and 70-74 above, and included here for reasons supra, in view of Salis, H. (“Ribosome Binding Site Calculator”, Methods in Enzymology, 2011).
In regards to claim 68, As outlined above, Demonte teaches the limitations of claim 65 for which claims 68 depends. Demonte teaches a gene construct comprising a gene encoding a biotin-binding protein (monomeric streptavidin), a fusion partner (MBP) for improving solubility and expression, and regulatory sequences including ribosome binding site that regulates expression of the encoded protein. Demonte does not teach the physical parameters of the regulatory gene, specifically related to the Gibbs free energy.
Salis, however, teaches that expression of recombinant proteins can be controlled by designing regulatory sequences, including ribosome binding sites and adjacent untranslated regions, using thermodynamic models, including calculations of the total Gibbs free energy change (ΔGTotal) associated with ribosome binding and mRNA folding (see Salis Section 4, pgs. 27-38). Salis further teaches that optimizing ΔGTotal, including values of 0 or less, improves translation initiation and protein expression.
It would have been prima facie obvious to one of ordinary skill in the art at the time of filing to optimize the regulatory sequence of the construct of Demonte, including ribosome binding site and adjacent untranslated region, using known thermodynamic design principles as taught by Salis, in order to improve expression of the recombinant protein. Such optimization of ΔGTotal represents routine tuning of known expression elements to achieve predictable improvements in protein production, which is a stated objective of Demonte.
In regards to claims 69, Demonte teaches a gene construct comprising a gene encoding a biotin-binding protein and a regulatory sequence including a ribosome binding site that regulates expression of the encoded protein. Demonte does not teach controlling the regulatory gene translation initiation rate (TIR).
However, Salis teaches that translation initiation rate can be controlled by designing regulatory sequences, including ribosome binding sites and adjacent untranslated region, and that such rates can be tuned within the desired ranges by modifying sequence features affecting ribosome binding and mRNA structure (see section 2.5, pg. 24). Salis further teaches that translation initiation rate can be tuned across a wide range by modifying sequence features and that such rates are commonly expressed in arbitrary units based on predictive models, such that “[a] protein CDS translated at 1000 au will produce 10 times more protein than one translated at 100 au, assuming that all other conditions are equal…” (see section 1.1, pg. 20).
It would have been obvious to a person of ordinary skill in the art to modify the regulatory sequence of the construct of Demonte to control translation initiation rate within the desired range as taught by Salis, in order to achieve predictable levels of protein expression. Such optimization of expression parameters, including tuning thermodynamic properties and translation initiation rates, represents routine experimentation to achieve predictable improvements in protein expression.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 60-74 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 21-40 of copending Application No. 18/251,176 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because both application are drawn to a gene expressing biotin-binding protein, specifically monomeric streptavidin. The claims go on to describe the fusion construct and regulatory gene parameters, which are identical between the applications. Furthermore, the applications share identical specifications and drawings. The sole distinction between the two applications is that in copending application 18/251,176 the claims are drawn to the gene construct itself, while in the present application the claims are drawn to a composition, which one of ordinary skill in the art would recognize as the product of transforming cells with the gene construct of the copending application. Claim 35 of the copending application further recites “A host cell transformed by introduction of the recombinant vector of claim 31 thereinto,” which would result in a composition of claim 60. For the majority of the claims, the only difference between the claims in the copending applications is the preamble, which would be obvious to one of ordinary skill in art to apply as described in copending application 18/251,176 to achieve.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No Claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Matthew H Raymonda whose telephone number is (703)756-5807. The examiner can normally be reached Monday - Friday 10:00 am - 4:00 pm.
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/MATTHEW HAROLD RAYMONDA/Examiner, Art Unit 1684
/AARON A PRIEST/Primary Examiner, Art Unit 1681
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