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 .
DETAILED ACTION
Applicant’s amendment submitted on 9/5/2025 is acknowledged. Claims 1, 4, and 64 are currently amended. Claim 65 has been canceled.
Claims 16, 31, 35, 39, 42, 93, and 95 remain withdrawn pursuant to 37 CFR 1.142(b) as being drawn to a non-elected invention.
Claims 1-2, 4, 8-9, 14, 16, 21, 31, 35, 39, 42-43, 64, 68, 70, 84, 88, 93, 95, and 105 remain pending in the instant application.
Claims 1-2, 4, 8-9, 14, 21, 43, 64, 68, 70, 84, 88, and 105 are the subject of this office action.
Claim Objections
Claims 1, 2, 21, 64, 68, and 88 are objected to because of the following informalities:
Claims 1, 2, 21, 64, 68, and 88 recite the Roman numerals (i) and (ii), which is redundant. One set of the Roman numerals from the claims can be amended to alphabetic letters to obviate this objection.
Claim 1 should recite an action verb, such as “making” or “creating,” instead of “providing” in step (i) of line 7.
Claim 64 should recite an action verb, such as “making” or “creating,” instead of “providing” in step (i) of line 6.
Appropriate correction is required.
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.
Modified Rejection Necessitated by Amendment: Claims 1-2, 4, 8-9, 14, 16, 31, 35, 39, 42-43, 64, 68, 70, 84, 93, 95 and 105 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 claims contain 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.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, 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. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention.
Scope of the claimed genus. The claims are drawn to identifying a peptide that selectively binds a chimeric antigen receptor (CAR) comprising a CAR antigen-recognition domain, wherein the CAR antigen-recognition domain comprises an antigen-binding domain of FMC63 antibody which comprises a heavy chain variable region (VH) having the amino acid sequence of SEQ ID NO: 71 and a light chain variable region (VL) having the amino acid sequence of SEQ ID NO: 72, wherein the method comprises: (i) providing a cellular library comprising a population of cells comprising a library of vectors, wherein each vector comprises a synthetic polynucleotide that encodes a variable peptide, wherein the population of cells displays at least 106 unique variable peptides, wherein the variable peptides are 5 or more amino acid residues in length, and wherein the synthetic polynucleotide sequence of each vector is (CGN)(NNK)q(TGY)(CCN)(TGG)(NNK)(TGY)(NNK) (SEQ ID NO: 136), wherein NNK is (A,T,G,C)(A,T,G,C)(G,T); wherein CGN is (C)(G)(A,T,G,C); wherein TGY is (T)(G)(T,C); wherein CCN is (C)(C)(A,T,G,C); wherein TGG is (T)(G)(G); wherein q is 1-3; wherein r is 1-3; and wherein s is 1-4; and (ii) selecting a peptide sequence motif that binds the CAR antigen-recognition domain with a binding affinity (KD) of at least 5 μM.
Claims 21 and 88 recite that the selection comprises (i) a negative selection, wherein the negative selection comprises at least one, two, three, four, or five rounds of depletion of cells that bind to a solid support, wherein the solid support comprises binding sites, wherein a plurality of binding sites are unbound or wherein a plurality of binding sites display an isotype control antibody or fragment thereof; and (ii) a positive selection, wherein the positive selection comprises at least one, two, three, four, or five rounds of enrichment of cells that bind to a solid support, wherein the solid support comprises binding sites, wherein a plurality of binding sites display an antibody or fragment thereof comprising the CAR antigen-recognition domain.
Claim 64 is further drawn to identifying a peptide ligand with enhanced binding to a CAR comprising an antigen-binding domain of FMC63 antibody comprising a VH having the amino acid sequence of SEQ ID NO: 71 and a VL having the amino acid sequence of SEQ ID NO: 72 by: (i) providing a cellular library comprising population of cells that display at least 106 variable peptides having unique amino acid sequences, wherein each of the variable peptides comprises an amino acid sequence from N-terminus to C-terminus represented by the formula: [A]x-[M]-[B]z; wherein A, if present, is any amino acid residue; wherein M is a sequence motif identified by the method of claim 1; wherein B, if present, is any amino acid residue; x and z are integers from 1 to 20; wherein either A is present or B is present, or both A and B are present; and (ii) selecting a peptide that binds the CAR antigen-recognition domain.
The steps of providing and selecting in claims 1 and 64 are recited at a high level of generality.
State of the prior art. The state of the art with respect to library-based display technologies has been well-described and optimized. However, display libraries utilizing cells expressing SEQ ID NO: 136 to generate peptides that selectively bind CARs comprising an antigen-binding domain of FMC63 antibody comprising a VH having the amino acid sequence of SEQ ID NO: 71 and a VL having the amino acid sequence of SEQ ID NO: 72 are not described in the prior art. Likewise display libraries for peptides generated by the formula of claim 64 that have enhanced binding to a CAR comprising an antigen-binding domain of FMC63 antibody comprising a VH having the amino acid sequence of SEQ ID NO: 71 and a VL having the amino acid sequence of SEQ ID NO: 72 are not described in the prior art.
Galan et al. (Mol. BioSyst., 2016, Vol. 12, pp.2342-2358; of record) teaches that library-based display technologies have been staggeringly optimized since their appearance in order to mimic the process of natural molecular evolution (see Abstract and passage bridging p.2342 and p.2343). Galan further teaches display libraries are essential for the isolation of specific high-affinity binding molecules for diagnostic and therapeutic applications (see Abstract and passage bridging p.2342 and p.2343). Streamlined procedures for identification of ligand-receptor pairs have relied on the display technologies, in which polypeptides or nucleic acids with desired binding properties can be iteratively selected by biopanning, i.e., multiple rounds of enrichment, followed by functional screening and characterization of the selected variants using appropriate assays (see p.2344, left column, 1st paragraph, and paragraph bridging pp.2345-2346). Sequencing is then used to analyze the variants (see p.2344, left column, 1st paragraph). Galan describes that random phage peptide libraries are one of the most common types of phage display constructs, and with the use of degenerate oligonucleotides linear random peptide libraries can be obtained (see p.2346, right column, 2nd paragraph). Random peptide libraries varying in length from 6 to 43 amino acids have been successfully cloned and expressed as peptide-capsid fusion proteins. Codon degeneracy (NNK) is one of the most common approaches to construct random peptides.
Lobb et al. (WO2019/118918) teaches a method of identifying a stable CD19 variant, comprising obtaining a plurality of CD19 polypeptides, each CD19 polypeptide having one or more amino acid substitutions of the amino acid sequence of SEQ ID NO: 2; determining if a CD19 polypeptide of the plurality is bound by an anti-CD19 antibody or fragment thereof; determining if a CD19 polypeptide of the plurality is more resistant to protease cleavage relative to a polypeptide comprising the amino acid sequence of SEQ ID NO: 2; and/or determining if a CD19 polypeptide of the plurality is more thermally stable relative to a polypeptide comprising the amino acid sequence of SEQ ID NO: 2; wherein a CD19 polypeptide is a stable CD19 variant if the polypeptide (i) is bound by the anti-CD19 antibody or fragment thereof, (ii) is more resistant to protease cleavage relative to the polypeptide comprising the amino acid sequence of SEQ ID NO: 2, and/or (iii) is more thermally stable relative to the polypeptide comprising the amino acid sequence of SEQ ID NO: 2 (see paragraph [0018] and Table 1A-1B). Lobb further teaches the anti-CD19 antibody is FMC63. SEQ ID NO: 2 is the amino acid sequence of human CD19 and is 272 amino acids in length. Lobb teaches an antigen binding moiety selectively binds an antigen target if the binding affinity is less than about 10-5 M, i.e., 100 μM, (see paragraph [0112]). Lobb further teaches mutant CD19 genes were generated using niching mutagenesis with NNK codons at each diversified site, introduced into a pCT-Aga2p-CD19-MYC yeast display vector and transformed into a yeast cellular library (see paragraphs [0242]-[0243]). Table 1A discloses species of single point mutations in SEQ ID NO: 2 and their binding score to FMC63. Table 1B discloses species of triple mutations in SEQ ID NO: 2 and their binding score to FMC63. Selection is performed by magnetic beads or fluorescence activated cell sorting (FACS) and flow cytometry, and the selected variants were then sequenced for analysis (see paragraphs [0026]-[0038], [0131], [0141], [0242], [0254])Lobb does not demonstrate the generation of variable peptides encoded by an sequence comprised in the genus of SEQ ID NO: 136 that bind to FMC63.
Ladner (US2003/0186223; of record) teaches modular display libraries utilizing degenerate codons encoded by SEQ ID NOs: 1-4 which comprise two cysteines separated by at least 9 amino acids and that can form a disulfide bond (see Abstract, and paragraphs [0008], [0010]-[0011], [0024], [0064], and [0072]). The peptides generated by Ladner’s methods were tested for binding to vascular endothelial growth factor receptor-1 (KDR) and the binding affinities (KD) were determined (see paragraphs [0075], [0077]-[0090], and [0094]-[0095], and Tables 1-3). SEQ ID NO: 2 of Ladner is the closest sequence in the prior art to SEQ ID NO: 136 of the claimed invention. SEQ ID NO: 2 consists of: 5’-NNK-NNK-NNK-TGY-NNK-NNK-NNK-NNK-TCC-GGT-CCG-NNK-NNK-NNK-NNK-TGY-NNK-NNK-NNK-3’ (see paragraphs [0010]-[0011]). SEQ ID NO: 2 encodes a peptide sequence of: X-X-X-C-X-X-X-X-SGP-X-X-X-X-C-X-X-X, where X is any amino acid. SEQ ID NO: 136 of the claimed invention encodes a variable peptide sequence of: R-X1-3-CPW-X1-3-C-X1-4 , where X is any amino acid. There are no encoded peptide species within the genus of SEQ ID NO: 2 of Ladner that fall within the genus of peptides encoded by SEQ ID NO: 136 of the claimed invention. Selection comprises a few rounds of contacting a phage library to the target, preferably using immobilized targets on a solid support, such as magnetic beads (see paragraphs [0051]-[0053]). Selected sequences are then characterized through sequencing (see claim 32).
Thus, the state of the art with regards to identifying peptides encoded by SEQ ID NO: 136 that selectively bind a CAR comprising an antigen-binding domain of FMC63 antibody comprising a VH having the amino acid sequence of SEQ ID NO: 71 and a VL having the amino acid sequence of SEQ ID NO: 72 are not described. Furthermore, phage display libraries and yeast display libraries comprising a pCT-Aga2p plasmid are well-described in the art for variable peptide generation. Additionally, selection of a peptide that binds a CAR antigen-recognition domain requires multiple rounds of enrichment followed by sequencing for analysis of the identified mimotopes.
Summary of species disclosed in the original specification. MPEP § 2163 states that a “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
The specification describes peptide species with 10 amino acids comprising SEQ ID NO: 7 as shown in Tables 4-7 of the specification that correspond to the claimed invention and conform to SEQ ID NO: 136 (see Examples 1-6). Peptides within the genus of SEQ ID NO: 7 represent the following species of SEQ ID NO: 136: Arg-Xaa1--Cys-Pro-Trp-Xaa2-Cys-Xaa3-Xaa4-Xaa5. These peptide species are specific for an anti-CD19 CAR comprising a FMC63 scFv identified by SEQ ID NO: 70 and having a VH identified by SEQ ID NO: 71 and a VL identified by SEQ ID NO: 72. To provide a cellular library encoding variable peptides, a yeast surface display technology expressing Aga2p by a pCTCON-2 vector is utilized to produce the variable peptides by degenerate codons. In order to select peptides that bind a CAR comprising an FMC63 antigen-recognition domain, the specification discloses that four rounds of magnetic-activated cell sorting (MACS) enrichment are carried out for FMC63 binding (see Instant Specification – p.146, 1st paragraph). Specifically, FMC63 IgG and a corresponding isotype control antibody, i.e., IgG2a with kappa light chain, were biotinylated, and the biotinylated antibodies were incubated with the yeast cell library encoding the variable peptides. Enrichment was performed using streptavidin-coated microbeads for four rounds of magnetic activated cell sorting (MACS) selection using first bare beads as a negative selection to deplete non-specific binders, a second and third round using IgG isotype control beads, and a fourth round using FMC63 IgG coated beads. Following the MACS enrichment, two rounds of FACS were performed by staining yeast with biotinylated FMC63 IgG antibody and streptavidin-PE conjugates in order to enrich yeast cells expressing mimotopes that specifically bind to the antigen-binding domain of FMC63 antibody. Clones were isolated following FACS analysis and sanger sequencing was carried out to identify the sequences of the high-affinity and low-affinity mimotopes. Finally, the binding affinity of mimotopes were measured by ELISA (see Instant Specification – p. 147, 2nd paragraph). Given the potential variability encompassed by the genus, this disclosure cannot be considered representative of the genus of providing a cellular library and selecting a peptide as claimed.
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied 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. As noted above, the art teaches that phage display libraries and yeast display libraries comprising a pCT-Aga2p plasmid are well-described in the art for variable peptide generation. Additionally, selection of a peptide that binds a CAR antigen-recognition domain requires multiple rounds of enrichment followed by sequencing for analysis of the identified mimotopes. The specification demonstrates variable peptide generation in a yeast surface display library, followed by multiple rounds of MACS and FACS enrichment to detect mimotopes that specifically bind the CAR with a FMC63 antigen-recognition domain of the claimed invention. Selected mimotopes with specific binding are then subjected to ELISA to determine binding affinity of the mimotope to the FMC63 antigen-recognition domain. Finally, sangar sequencing of the selected mimotope is carried out to characterize the selected mimotopes. No other cell display libraries or selection processes are demonstrated with regards to the claimed invention to demonstrate possession of the vast domain of species under the genus of providing a cellular library and selecting a peptide.
For all the reasons presented above, one of skill in the art would not know which of the possible cell display libraries and selection processes--other than a yeast surface display library and multiple rounds of enrichment, followed by ELISA, and sequencing—are adequate to carry out the claimed invention of identifying a peptide ligand that selectively binds a CAR comprising a FMC63 antigen-binding recognition domain as claimed. Therefore, the skilled artisan would not reasonably conclude that the inventors, at the time the application was filed, had full possession of the genus of cellular display libraries and selection processes as broadly claimed.
Given the description of only yeast surface display libraries and selection by multiple rounds of enrichment using MACS and FACS followed by ELISA and sequencing of the selected mimotope, and the fact the species that was described cannot be considered representative of the broad genus, applicant was not in possession of the invention as claimed.
Claim Rejections - 35 USC § 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.
New Rejection Necessitated by Amendment: Claims 1-2, 4, 8-9, 14, 16, 21, 31, 35, 39, 42-43, 64, 68, 70, 84, 88, 93, 95 and 105 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.
Claim 1 recites a method preamble, for identifying a peptide ligand that selectively binds a chimeric antigen receptor (CAR) comprising a CAR antigen-recognition domain, wherein the CAR antigen recognition domain comprises an antigen-binding domain of FMC63 antibody which comprises a heavy chain variable region (VH) having the amino acid sequence of SEQ ID NO: 71 and a light chain variable region (VL) having the amino acid sequence of SEQ ID NO: 72. Claim 1 does not require any active method step of contacting peptides with a CAR comprising a CAR antigen-recognition domain comprising a VH having the amino acid sequence of SEQ ID NO: 71 and a VL having the amino acid sequence of SEQ ID NO: 72 to identify peptide ligands that selectively bind the CAR of the claimed invention. In the absence of this method step, it is not readily apparent how the recited method steps, (i) and (ii), result in the identification of peptide ligands that selectively bind to the specifically claimed CAR. The examples of the specification discloses that four rounds of magnetic-activated cell sorting (MACS) enrichment utilizing negative and positive selection, followed by two rounds of FACS, and then ELISA are carried out to detect mimotope-FMC63 binding and binding affinity of the mimotopes (see p.146, 1st paragraph, and p.147, 2nd paragraph). Claims 21 and 88 recite specific active method steps for negative and positive selection of a peptide that binds the CAR antigen-recognition domain; however, no such active steps are recited in the claimed invention. The structural relationship between (i) providing a cellular library and iii) selecting a peptide motif that binds the CAR domain is indefinite because the method starts with providing a cellular library but does not set forth where the peptide and the CAR domain used in the subsequent step of binding selection come from.
Claim 64 recites a similar preamble and lacks a step of contacting the library of peptides generated to the claimed CAR. Therefore, claim 64 is indefinite for the same reason as in claim 1.
Claims 2, 4, 8-9, 14, 16, 21, 31, 35, 39, 42-43, 68, 70, 84, 88, 93, 95 and 105 are also rejected for being dependent on a rejected base claim and failing to remedy the issues set forth above.
Closest Prior Art:
The claimed invention is free of the prior art. The closest prior art to the claimed invention is to Lobb et al. (WO2019/118918), Blein et al. (US2010/0215651), and Ladner (US2003/0186223; of record).
Lobb et al. teaches a method of identifying a stable CD19 variant, comprising obtaining a plurality of CD19 polypeptides, each CD19 polypeptide having one or more amino acid substitutions of the amino acid sequence of SEQ ID NO: 2; determining if a CD19 polypeptide of the plurality is bound by an anti-CD19 antibody or fragment thereof; determining if a CD19 polypeptide of the plurality is more resistant to protease cleavage relative to a polypeptide comprising the amino acid sequence of SEQ ID NO: 2; and/or determining if a CD19 polypeptide of the plurality is more thermally stable relative to a polypeptide comprising the amino acid sequence of SEQ ID NO: 2; wherein a CD19 polypeptide is a stable CD19 variant if the polypeptide (i) is bound by the anti-CD19 antibody or fragment thereof, (ii) is more resistant to protease cleavage relative to the polypeptide comprising the amino acid sequence of SEQ ID NO: 2, and/or (iii) is more thermally stable relative to the polypeptide comprising the amino acid sequence of SEQ ID NO: 2 (see paragraph [0018] and Table 1A-1B). Lobb further teaches the anti-CD19 antibody is FMC63. SEQ ID NO: 2 is the amino acid sequence of human CD19 and is 272 amino acids in length. Lobb teaches an antigen binding moiety selectively binds an antigen target if the binding affinity is less than about 10-5 M, i.e., 100 μM, (see paragraph [0112]). Lobb further teaches mutant CD19 genes were generated using niching mutagenesis with NNK codons at each diversified site, introduced into a pCT-Aga2p-CD19-MYC yeast display vector and transformed into a yeast cellular library (see paragraphs [0242]-[0243]). Table 1A discloses species of single point mutations in SEQ ID NO: 2 and their binding score to FMC63. Table 1B discloses species of triple mutations in SEQ ID NO: 2 and their binding score to FMC63. Lobb does not demonstrate the generation of variable peptides encoded by an sequence comprised in the genus of SEQ ID NO: 136 that bind to FMC63.
Lobb does not teach the claimed FMC63 CAR comprising a heavy chain variable region (VH) having the amino acid sequence of SEQ ID NO: 71 and a light chain variable region (VL) having the amino acid sequence of SEQ ID NO: 72 or vectors comprising the synthetic polynucleotide sequence of SEQ ID NO: 136.
Blein teaches an FMC63 with heavy chain and light chain sequences (SEQ ID NOs: 1 and 2, respectively) that are identical to the VH and VL of the FMC63 CAR of the claimed invention (see paragraph [0192] and Appendix B for sequence alignment).
Ladner teaches modular display libraries utilizing degenerate codons encoded by SEQ ID NOs: 1-4 which comprise two cysteines separated by at least 9 amino acids and that can form a disulfide bond (see Abstract, and paragraphs [0008], [0010]-[0011], [0024], [0064], and [0072]). The peptides generated by Ladner’s methods were tested for binding to vascular endothelial growth factor receptor-1 (KDR) and the binding affinities (KD) were determined (see paragraphs [0075], [0077]-[0090], and [0094]-[0095], and Tables 1-3). SEQ ID NO: 2 of Ladner is the closest sequence in the prior art to SEQ ID NO: 136 of the claimed invention. SEQ ID NO: 2 consists of: 5’-NNK-NNK-NNK-TGY-NNK-NNK-NNK-NNK-TCC-GGT-CCG-NNK-NNK-NNK-NNK-TGY-NNK-NNK-NNK-3’ (see paragraphs [0010]-[0011]). SEQ ID NO: 2 encodes a peptide sequence of: X-X-X-C-X-X-X-X-SGP-X-X-X-X-C-X-X-X, where X is any amino acid. SEQ ID NO: 136 of the claimed invention encodes a variable peptide sequence of: R-X1-3-CPW-X1-3-C-X1-4 , where X is any amino acid. There are no encoded peptide species within the genus of SEQ ID NO: 2 of Ladner that fall within the genus of peptides encoded by SEQ ID NO: 136 of the claimed invention.
The prior art do not teach or suggest the claimed limitation of vectors comprising SEQ ID NO: 136, and the examiner has not found any motivation to modify the closest known sequence in the prior art to arrive at the claimed sequence. Thus, the claimed invention is free of the prior art.
Response to Arguments
Applicant’s arguments, see paragraph bridging p.10-11-p.12, last paragraph, filed 9/5/2025, with respect to claims 1-2, 4, 8-9, 14, 16, 21, 31, 35, 39, 42-43, 64, 68, 70, 84, 88, 93, 95 and 105 as rejected under 35 U.S.C. § 112(a) have been fully considered and are persuasive. The 35 U.S.C. § 112(a) rejection of claims 1-2, 4, 8-9, 14, 16, 21, 31, 35, 39, 42-43, 64, 68, 70, 84, 88, 93, 95 and 105 has been withdrawn.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JOHN PAUL SELWANES whose telephone number is (571)272-9346. The examiner can normally be reached Mon-Fri 7:30-5:00.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Louise W. Humphrey can be reached at 571-272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/J.P.S./Examiner, Art Unit 1657