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 .
Election/Restrictions
Applicant’s election without traverse of claims 11-19 in the reply filed on 02/12/2026 is acknowledged. Claims 1-10 and 20-28 have been cancelled.
Priority
The instant application claims benefit of Provisional application 63/354,637 filed 06/22/2022.
Specification
The disclosure is objected to because of the following informalities: The numbering of paragraphs in the specification is not consistent. For example, on pages 76-77, paragraphs [0050] – [0052] are inserted between paragraphs [00288] and [00289]. Appropriate correction is required. The lengthy specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant’s cooperation is requested in correcting any errors of which applicant may become aware in the specification.
Claim Interpretation
Claim 1 recites the limitation “engineered cyclic peptide” (line 2). The specification defines the term “engineered” as follows: “The term “engineered” as used in reference to a cyclic peptide molecule, e.g., an engineered cyclic peptide, to a protein, or to a nucleic acid sequence, implies that such molecules are created by human intervention and/or they are non-naturally occurring” (para 315).
Claim 1 is drawn to A plurality of host cells permissive for replication of a virus, which is a composition with intended use. The recitation of intended use does not impart further structural limitations to the composition beyond the limitations recited in the body the claim, and therefore does not further limit the claim. If the body of a claim fully and intrinsically sets forth all of the limitations of the claimed invention, and the preamble merely states, for example, the purpose or intended use of the invention, rather than any distinct definition of any of the claimed invention’s limitations, then the preamble is not considered a limitation and is of no significance to claim construction. Shoes by Firebug LLC v. Stride Rite Children’s Grp., LLC, 962 F.3d 1362, 2020 USPQ2d 10701 (Fed. Cir. 2020). See MPEP 2111.02(II).
Claim Rejections - 35 USC § 112(a)
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.
Claims 11-19 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
From M.P.E.P. § 2163, the analysis of whether the specification complies with the written description requirement calls for the examiner to compare the scope of the claim with the scope of the description to determine whether applicant has demonstrated possession of the claimed invention from the standpoint of one of skill in the art at the time the application was filed. For inventions in emerging and unpredictable technologies, or for inventions characterized by factors not reasonably predictable which are known to one of ordinary skill in the art, more evidence is required to show possession.
For claims drawn to a genus, possession may be shown (for example) 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. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. A “representative number of species” means that the species which are adequately described are representative of the entire genus, and is an inverse function of the skill and knowledge in the art. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. See, e.g., Eli Lilly. If a representative number of adequately described species are not disclosed for a genus, the claim to that genus must be rejected as lacking adequate written description under 35 U.S.C. 112, para. 1.
Claim 11 is drawn to a plurality of host cells permissive for replication of a virus, wherein each host cell of the plurality of host cells comprises an engineered cyclic peptide, and wherein the engineered cyclic peptide increases viral titer or transduction efficiency of viral vectors produced by the plurality of host cells by at least 2-fold compared to a corresponding characteristic of viral vectors produced by a plurality of reference host cells under essentially identical conditions.
Claim 11 recites a structure: a plurality of host cells, wherein each host cell of the plurality of host cells comprises an engineered cyclic peptide. Claim 11 also recites a function: wherein the engineered cyclic peptide increases viral titer or transduction efficiency of viral vectors produced by the plurality of host cells by at least 2-fold compared to a corresponding characteristic of viral vectors produced by a plurality of reference host cells under essentially identical conditions. Thus, the claim is drawn to a product comprising a very large genus of a host cell comprising an engineered cyclic peptide comprising the claimed function.
Neither the specification nor the prior art establishes a structure-function relationship wherein a plurality of host cells, wherein each host cell of the plurality of host cells comprises an engineered cyclic peptide, as claimed in claim 11, would be capable of functioning as claimed with any degree of predictability.
The instant specification appears to only have the following engineered cyclic peptides capable of functioning according to claim 11: engineered cyclic peptides comprising an amino acid sequence having at least 90% or more sequence identity to any one of the amino acid sequences selected from the group consisting of SEQ ID NO: 34- SEQ ID NO: 62, SEQ ID NO: 64- SEQ ID NO: 228, and SEQ ID NO: 230 (para 324). The specification does not disclose any other embodiments which would be encompassed within the pending claim. The specification further recites that “An engineered nucleic acid sequence can include any type of modification that can be made to a nucleic acid (e.g., introduction, substitution, deletion, replacement, rearrangement, epigenetic modification, etc.)” (para 201). Although this description is in relation to an engineered nucleic acid sequence, rather than an engineered cyclic peptide sequence, the modifications described (e.g., substitution, deletion) are also applicable to peptide sequences. Thus, the breadth of the engineered cyclic peptides encompassed in claim 11 is broad. The specification does not identify what changes, mutation, etc. could be made to the amino acid sequences selected from the group consisting of SEQ ID NO: 34- SEQ ID NO: 62, SEQ ID NO: 64- SEQ ID NO: 228, and SEQ ID NO: 230, and that would be encompassed by the structural limitations of claim 11 (i.e., a cyclic peptide), and would predictably result in the claimed function of claim 11. Furthermore, the specification recites that in some embodiments, an engineered cyclic peptide may be further modified to obtain a further engineered cyclic peptide to have improved characteristics compared to the starting engineered cyclic peptide, for example, increased membrane permeability or increased stability in host cells (para 201), and that the sequence of a further engineered cyclic peptide can contain 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, or more amino acid differences (e.g., substitutions and/or additions) compared to the sequence of starting engineered cyclic peptide (para 201). However, the specification does not identity what structural changes correspond to, or result in, improved characteristics such as increased membrane permeability or increased stability in host cells. As such, the instant specification does not provide a sufficient representative sampling of engineered cyclic peptide that are capable of providing for said function as claimed.
The prior art is unpredictable. Bauche (WO 2019/097290 A1) teaches culturing cells in the presence of a cyclic peptide, wherein the cyclic peptide has the following formula:
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122
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wherein X represents any amino acid which can be different or identical for each position, and m+n is less than or equal to 5, increases the production of a biological agent compared to culturing the cells in the absence of the cyclic peptide (claim 1). However, Bauche does not teach what modifications may be made to the sequence set forth in SEQ ID NO: 9 therein, such that the cyclic peptide satisfies the function of increasing production of a biological agent. Thus, the prior art cannot be relied upon for making up for the deficit of the instant specification with regard to a sufficient representative number of species of cyclic peptides that provide for said function as claimed.
Accordingly, neither the specification nor the prior art establishes a known structure-function relationship wherein the genus of cyclic peptides is capable of providing for the function as claimed with any predictability. In this case, the skilled artisan would not have reasonable concluded at the time of the invention that application was in possession of the invention as claimed. Claims 12-19 are included in the rejection because they depend from claim 11.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claim(s) 11, 13, 15-16, and 18-19 are rejected under 35 U.S.C. 103 as being unpatentable over Bauche (WO 2019/097290 A1), as evidenced by Kim (PLoS ONE, 2012, 7(11): e50148).
Bauche teaches a method of obtaining increased biological agent production from eukarytoic cells transfected with plasmids, wherein the method comprises culturing the cells in the presence of a cyclic peptide (p 2, Summary, para 1-2; p 3, para 2; p 6, Detailed Description, para 1). Bauche teaches that fertilin ß, or peptides containing the cyclic FEE tripeptide (FEEc) of fertilin ß or homologous sequences, have the ability to increase the production and/or yield of viral vectors from cultured cells (p 7, lines 24-26; p 11, lines 4-25) (claim 11). Bauche teaches that the peptide can be cyclized by any method known to those skilled in the art (p 8, line 15). Bauche teaches that the viral vectors may encode a therapeutic agent (p 4, lines 32-33) (claim 18),
Bauche teaches an example, wherein 0.5x105 to 2.1 x 105 HEK293T cells per well (claims 16, 19) were transiently transfected with a transfer vector plasmid, packaging plasmid, and envelope plasmid (Example 2 on p 12, lines 14-21).
The transfer vector plasmid, pARA-CMV-GFP, encodes a non-replicative recombinant proviral DNA derived from HIV-1 (claim 13, (i)) comprising an expression cassette (p 12, lines 22-25). The cassette comprises a GFP transgene (reads on payload), a human ubiquitin promoter for transgene expression, and sequences added to increase the transgene expression and to allow the lentiviral vector to transduce all cell types (p 12, lines 22-27) (claim 11, (iv)). Non-coding sequences and expression signals include: (i) the Long Terminal Repeat sequences (LTR) with the whole cis-active elements for the 5’LTR (U3-R- U5) and the deleted one for the 3’LTR, hence lacking the promoter region; (ii) (AU3-R-U5), for transcription and integration mechanisms; and (iii) the encapsidation sequences (SD and 5’Gag) (claim 11, (iv)); (iv) the central PolyPurine Tract/Central Termination Site for nuclear translocation of the vectors; and (v) Bovine Growth Hormone polyadenylation signal to stabilize the RNA (p 12, line 30 – p 13, line 2). Kim shows that all lentiviral vector systems, including the 2nd generation lentiviral vector as taught in Bauche, comprise the viral packaging signal sequence, Psi, which must be placed immediately downstream of the 5’ LTR in the transgene plasmid in order to package and deliver the transgene mRNA (Abstract; p 1, col 2, para 2) (claim 13, (v)).
The packaging plasmid, pARA-Pack, is a kanamycin-resistant plasmid encoding the structural lentiviral proteins POL (claim 11, (i); claim 13, (ii)), GAG (claim 11, (ii); claim 13, (iii)), REV (claim 11, (iii); claim 13, (iv)), and TAT (p 13, lines 3-11). The envelope plasmid, pENV1, encodes glycoproteins G from the VSV-G Indiana strain for pseudotyping lentiviral vectors (p 13, lines 12-19) (claim 11, (ii); claim 13, (iii)). Following transfection, a fertilin analog was added to the culture medium at different concentrations and at pH conditions at different times (p 14, lines 1-14) (claim 15). Lentiviral titers were determined using flow cytometry (p 14, lines 15-29).
Bauche teaches that lentiviral vector production, as measured by titration of lentiviral vectors and calculated as transduction efficiency (p 14, lines 15-29; Fig 2A), increased to up to 130% upon addition of fertilin ß (p 15, lines 23-24). Bauche teaches that the cyclic peptides taught therein can be used to enhance any laboratory or industrial production involving eukaryotic cells, and that the cyclic peptides can be added to the culture medium at different times and in different concentrations (p 3, lines 9-17; p 11, lines 15-25).
Bauche does not teach that the engineered cyclic peptide increases the viral titer or transduction efficiency by at least two-fold.
It would have been prima facie obvious to a person of ordinary skill in the art before the effective
filing date of the claimed invention to have optimized the concentrations and timing of the addition of fertilin ß to the culture medium to achieve two-fold increase in viral titer or transduction efficiency, to arrive at the claimed invention. See MPEP 2144.05(II)(A). As noted in In re Aller, 105 USPQ 233 at 235, where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.
Claim(s) 11 and 12 are rejected under 35 U.S.C. 103 as being unpatentable over Bauche (WO 2019/097290 A1), in view of Addgene (“Adeno-associated Virus (AAV) Guide,” 2022).
The teachings of Bauche are set forth above. Bauche renders obvious claim 11.
Regarding claim 12: Bauche teaches that the cyclic peptides taught therein can be used to enhance any laboratory or industrial production involving eukaryotic cells, such as the production of viral vectors by mammalian cells (p 11, lines 15-17).
Bauche does not explicitly teach the viral vector being an AAV vector.
Addgene teaches that AAV plasmids are commonly used in optogenetics experiments, and that they are preferred over lentiviral vectors because AAVs remain primarily episomal, while lentiviruses integrate into the genome (p 1, “Common Uses of AAV,” para 1) (claim 12, (i)). Addgene teaches that the AAV genome consists of two open reading frames, Rep (claim 12, (ii)) and Cap (claim 12, (iii)), flanked by two 145-base inverted terminal repeats (ITRs) (claim 12, (v)) (p 1, “AAV Components,” para 1). Addgene teaches that in addition to Rep and Cap, AAV requires a helper plasmid containing genes from adenovirus (p 1, “AAV Components,” para 2). These genes (E4, E2a and VA) mediate AAV replication (claim 12, (iv))). The transfer plasmid, Rep/Cap, and the helper plasmid are transfected into HEK293 cells, which contain the adenovirus gene E1+, to produce infectious AAV particles (p 1, “AAV Components,” para 2).
It would have been prima facie obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention to have modified the invention of Bouche by using an AAV vector, as taught in Addgene. One of ordinary skill in the art would have been motivated to make this modification because Addgene teaches that AAV vectors are preferred over lentiviral vectors in research applications because AAVs, unlike lentiviruses, remain primarily episomal. One of ordinary skill in the art would have had a reasonable expectation of making this modification because Bouche teaches that the cyclic peptides taught therein can be used to enhance any laboratory or industrial production involving eukaryotic cells, such as the production of viral vectors by mammalian cells, and an AAV vector is a viral vector.
Claim(s) 11 and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Bauche (WO 2019/097290 A1), in view of Addgene (“Adeno-associated Virus (AAV) Guide,” 2022) and Urabe (Human Gene Therapy, 2002, 13: 1935-1943).
The teachings of Bauche and Addgene are set forth above.
Bauche renders obvious claim 11.
Regarding claim 17: Bauche teaches that the cyclic peptides taught therein can be used to enhance any laboratory or industrial production, such as the production of viral vectors, involving eukaryotic cells (p 11, lines 15-17). Although insect cells are eukaryotic, Bauche does not explicitly teach the use of insect host cells.
As set forth above in the rejection for claim 12, Bauche, in view of Addgene, renders obvious the host cells of claim 11, wherein the virus in an AAV. Bauche, in view of Addgene, does not teach the use of insect host cells.
Urabe teaches the use of Sf9 cells (insect cells) to produce rAAV (Abstract). Urabe teaches coinfecting Sf9 cells in suspension culture with three recombinant baculoviruses (a Rep-baculovirus, a VP-baculovirus, and an AAV ITR vector genome baculovirus) and recovered rAAV particles three days later (Abstract). Urabe teaches that the rAAV particles produced using Sf9 host cells are indistinguishable from HEK293 cell-produced rAAV, and that the yield of genome-containing particles produced per Sf9 cell approached 5 × 104; thus, 1000 ml of cultured Sf9 cells produced the equivalent of between 500 to 1000 × 175 cm2 flasks of HEK293 cells (Abstract).
It would have been further prima facie obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention to have modified the invention of Bauche, in view of Addgene, by using Sf9 insect cells as the host cell in lieu of HEK293 cells, as taught in Urabe. One of ordinary skill in the art would have been motivated to make this modification because Urabe teaches that the use of Sf9 host cells increases AAV yield compared to the use of HEK293 host cells. One of ordinary skill in the art would have had a reasonable expectation of making this modification because Bauche 1) teaches that the cyclic peptides taught therein can be used to enhance any laboratory or industrial production involving eukaryotic cells, and Sf9 cells are eukaryotic cells, and 2) Urabe teaches that Sf9 cells can be used as host cells for AAV production.
Claim(s) 11 and 14 are rejected under 35 U.S.C. 103 as being unpatentable over Bauche (WO 2019/097290 A1), in view of Tavassoli (US 2024/0279646 A1) and Rogers (PNAS, 2018, 115(43): 10959-10964).
The teachings of Bauche are set forth above. Bauche renders obvious claim 11.
Regarding claim 14: Bauche teaches that the peptide can be cyclized by any method known to those skilled in the art (p 8, line 15).
Bauche does not teach the engineered cyclic peptide being produced ribosomally in each host cell of the plurality of host cells.
Tavassoli teaches a method for non-toxic production of a cyclic peptide in a mammalian cell, as well as a mammalian cell expressing a cyclic peptide (Abstract; para 3, 21, 32). Tavassoli teaches that mammalian cells are susceptible to toxicity arising from active inteins, which is a byproduct of SICLOPPS cyclization (para 18). The SICLOPPS method makes use of a construct containing a C-terminus intein domain followed by an extein polypeptide sequence to be cyclised, and an N-terminus intein domain. The construct is arranged as such so that, following translation of the mRNA sequence, the N- and C-terminus intein domains flanking the intervening extein are capable of non-covalently associating to form a functional active intein that subsequently catalyses the splicing reaction that produces the cyclic polypeptide (para 71, Fig 1). Tavassoli teaches that the method disclosed therein obviates the intein-associated toxicity allowing the split intein system to be widely used in mammalian cells for the production of cyclic peptides (para 18).
Rogers teaches that essentially any nonproteinogenic amino acid can be loaded onto tRNA by flexizymes and delivered to the ribosome for use during in vitro translation (Fig 1, caption).
It would have been prima facie obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention to have modified the invention of Bouche by using a mammalian host cell expressing an engineered cyclic peptide, as taught in Tavassoli, to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to make this modification because Tavassoli teaches that mammalian cells are susceptible to toxicity arising from active inteins, which is a byproduct of SICLOPPS cyclization, and the method disclosed therein obviates the intein-associated toxicity allowing the split intein system to be widely used in mammalian cells for the production of cyclic peptides (para 18). One of ordinary skill in the art would have had a reasonable expectation of making this modification because 1) Rogers teaches that essentially any nonproteinogenic amino acid can be loaded onto tRNA by flexizymes and delivered to the ribosome for use during in vitro translation, and 2) Bauche teaches that the peptide can be cyclized by any method known to those skilled in the art (p 8, line 15).
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 11-19 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 12-19 of copending Application No. 19/508,282 (reference application), in view of Bauche (WO 2019/097290 A1).
Although the claims at issue are not identical, they are not patentably distinct from each other. Copending claim 12 differs from instant claim 11 in requiring that each host cell of the plurality of host cells comprises a Synthetic Helper Gene Product (lines 1-2), as opposed to an engineered cyclic peptide of instant claim 11. A synthetic helper gene product, as recited in copending claim 12, is generic to an engineered cyclic peptide, as recited in instant claim 11.
Bauche teaches that an analog or derivative (reads on synthetic) of fertilin ß, which is a cyclic peptide, increases the production and/or yield of viral vectors from cultured cells (p 7, lines 24-26; p 11, lines 4-25).
It would have been prima facie obvious for a person of ordinary skill in the art before the effective filing date of the claimed invention to have modified the invention of copending claim 12 by using fertilin ß, which is an engineered cyclic peptide, as the Synthetic Helper Gene Product. One of ordinary skill in the art would have been motivated to make this modification because Bauche teaches that fertilin ß increases the production and/or yield of viral vectors from cultured cells. One of ordinary skill in the art would have had a reasonable expectation of making this modification because fertilin ß is a Synthetic Helper Gene Product.
Following the discussion above, copending claim 13 reads on instant claim 12; copending claim 14 reads on instant claim 13; copending claim 15 reads on instant claim 14; copending claim 16 reads on instant claim 15; copending claim 16 reads on instant claim 16; copending claim 17 reads on instant claim 17; copending claim 18 reads on instant claim 18; and copending claim 19 reads on instant claim 19.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
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/RISA TAKENAKA/Examiner, Art Unit 1632
/PETER PARAS JR/Supervisory Patent Examiner, Art Unit 1632
Prosecution Insights