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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 01DEC2025 has been entered.
Claim Status
Applicant’s amendments received 01DEC2025 are acknowledged.
Claims 2-4, 6-12, and 14-17 have been canceled.
Claims 1, 5, and 22 have been amended.
Claims 1, 5, 13, and 18-23 are pending in the instant application (i.e., Claim 1 is independent).
Claims 22-23 remain withdrawn.
Claims 1, 5, 13, and 18-21 are examined on the merits.
Priority
The present application is a 371 National Stage of PCT International Application No. PCT/IL2020/050359, filed 26MAR2020, which claims the benefit of US Provisional Patent Application No. 62/844303, filed 07MAY2019. Applicant’s claim for the benefit of prior-filed application is acknowledged.
Drawings
The drawings are objected to because drawings filed 26OCT2021 do not include Fig 33C as disclosed in ¶0652 of the specification filed 04JUN2025. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Specification
The disclosure is objected to because of the following informalities:
¶0555 of the marked up specification filed 04JUN2025 appears to be an incomplete sentence. Appropriate correction is required.
¶0652 mentions Fig 33C; however, the brief description of the figures only disclose Fig 33A and Fig 33B. In this instance if the drawings are updated, the brief description of the figures should also be updated.
¶0660 fails to disclose that Fig 36 is showing the binding of Constructs 13, 15, and 17 to 5T4 rather than CD3ε. Appropriate correction is required.
Claim Objections
Claim 1 is objected to because of the following informalities: The abbreviation of Trophoblast glycoprotein should be in parentheses, for example, “Trophoblast glycoprotein (TPBG, 5T4);….” Appropriate correction is required.
Claim Rejections - 35 USC § 112
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 5 is 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 5 is rendered indefinite because it depends from canceled claim 4, and therefore fails to set forth the metes and bounds of patent protection because it is unclear what claim 5 is attempting to further limit. For the purpose of expediting prosecution, claim 5 will be examined on the merits as being dependent on claim 1.
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.
Scope of Enablement
Claims 1, 5, 13, and 18-21 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for:
“A precursor tri-specific antibody construct, comprising:
(a) a first binding domain that binds to a first tumor associated antigen (TAA), wherein the TAA is Trophoblast glycoprotein (TPBG or 5T4);
(b) a second binding domain that binds to the TAA 5T4;
(c) a third binding domain that binds to an extracellular epitope of human CD3ε wherein the first binding domain and the second binding domain are each located C-terminal to the third binding domain; and
(d) a regulatory domain located N-terminal to the third binding domain, said regulatory domain comprising:
(i) a protease cleavage domain comprising a protease-cleavable amino acid sequence cleavable by a serine protease, a cysteine protease, an aspartate protease, a matrix metalloprotease (MMP), or a combination substrate cleaved by one or more of MMP2/9, urokinase-type plasminogen activator (uPA),matriptase and legumain, or any combination thereof;
(ii) a half-life prolonging (HLP) domain comprising a human serum albumin (HSA) polypeptide; and
(iii) a Cap component comprising an amino acid sequence of the extracellular epitope of human CD3ε that reduces the ability of the third binding domain to bind the extracellular epitope of human CD3ε,
wherein the first binding domain and/or the second binding domain, comprises a single chain variable fragment (scFv) comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 172 and 174;
wherein the third binding domain comprises a Fab antigen binding fragment comprising a VH and VL comprising amino acid sequences set forth in SEQ ID NO: 114 and 116, respectively; and
wherein the Cap comprises the amino acid sequence set forth in SEQ ID NO: 5;” does not reasonably provide enablement for more.
The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims.
In the instance of claim 1, the nature of the invention drawn to a precursor trispecific antibody construct having two binding regions that bind to 5T4, one binding region that binds CD3ε, a protease cleavage domain comprising a protease cleavable amino acid sequence, human serum albumin, and a Cap component which masks the CD3ε binding region, is not fully enabled. The broadest claim is not fully enabled because of:
The breadth VH/VL domains that bind to the extracellular epitope of human CD3ε;
The breadth of Cap components required to be tested for reducing binding of the third binding domain to the extracellular epitope of human CD3ε; and
The breadth of 5T4 scFv binding domains, which would require one of ordinary skill in the art undue experimentation to make and/use the presently claimed invention. Claims 5, 13, and 18-21 are also rejected since they depend from claim 1, but do not remedy this deficiency.
The specification discloses constructs 1-24, of which the construct of Fig 1, wherein the anti-TAA scFvs are both anti-5T4 scFvs as set forth in SEQ ID NO: 172, the Cap is set forth in SEQ ID NO: 5 and the VH/VL pair of the anti-CD3 Fab is set forth in SEQ ID NOs: 114/116 (i.e., construct 15) is enabled. Although Fig 38 shows that the 5T4 scFv structure (i.e., VL/VH or SEQ ID NO: 172) results in fully masking the anti-CD3 Fab binding moiety (i.e., inhibits the third binding region) in the cleavable/non-cleavable ProTribody; Fig 19A shows that scFv structure (i.e., VL/VH) may affect the overall fusion protein structure, which impedes the Cap from fully masking CD3ε binding. Additionally, because there are no examples comparing SEQ ID NOs: 172 and 174 (i.e., VL/VH and VH/VL, respectively) of the anti-5T4 scFv within the ProTribody construct nor any other anti-5T4 scFv sequences, it is unclear how significant the scFv structures could impact the overall structures of the ProTribody. Furthermore, alternative cap components are not supported in the specification. Therefore, although these examples support that specific components having specific SEQ ID NOs can be combined to successfully make and/or use a ProTribody construct, the specific components must be carefully selected.
Furthermore, the literature teaches that masking components are typically grouped into i) masks with affinity for the binding domain (i.e., epitope peptide sequences for the binding region) or ii) masks with no affinity for the binding domain that rely on steric hinderance to block binding, which requires significant testing/optimization to make a masking component for use in a pro-antibody construct (Orozco, et al., Mabs, 2022, 14, 1-16, see entire document, specifically see abstract and p 11, col 1). Therefore the literature supports the lack of predictability for making a cap component for use within in this instance a ProTribody.
Thus, one skilled in the art would be unable to make and/or use the Pro-Tribody having two binding regions to essentially anywhere on 5T4 and a third binding region to essentially anywhere on CD3ε, wherein the CD3ε binding region is linked to a protease cleavable unit and a cap component to inhibit CD3ε binding and a protease cleavable unit and a half-life prolonging component to increase the half-life in vivo. Therefore, the implementation of the invention in view of the breadth of variables (i.e., essentially any epitope of 5T4 or CD3ε and therefore finding a cap which would inhibit the Fab binding CD3ε), lack of predictability in the art, and lack of support from the working examples would require undue experimentation for one of ordinary skill in the art to make and/or use the instantly claimed invention.
Written Description
Claims 1, 5, 13, and 18-21 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.
In The Regents of the University of California v. Eli Lilly (43 USPQ2d 1398-1412) 19 F. 3d 1559, the court held that disclosure of a single member of a genus (rat insulin) did not provide adequate written support for the claimed genus (all mammalian insulins). In this same case, the court also noted: “A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. See Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen). It is only a definition of a useful result rather than a definition of what achieves that result. Many such genes may achieve that result. The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin [e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate."). Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.”
The court has further stated that “Adequate written description requires a precise definition, such as by structure, formula, chemical name or physical properties, not a mere wish or plan for obtaining the claimed chemical invention.” Id. at 1566, 43 USPQ2d at 1404 (quoting Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606). Also see Enzo-Biochem v. Gen-Probe 01-1230 (CAFC 2002). Recent court cases have emphasized the need for correlation between a well-defined structure and recited functional limitations. For example, the courts have indicated that recitation of an antibody which has specific functional properties in the absence of knowledge of the antibody sequences that give rise to said functional properties do not satisfy the requirements for written description. See for example AbbVie Deutschland GmbH v. Janssen Biotech. Inc. 759 F.3d 1285 (Fed. Cir. 2014) as well as Amgen v. Sanofi, (Fed Cir, 2017-1480. 10/5/2017). Indeed, in Amgen the court indicates that that it is improper to allow patentees to claim antibodies by describing something that is not the invention, i.e., the antigen, as knowledge of the chemical structure of an antigen does not give the required kind of structure-identifying information about the corresponding antibodies, with the antibody-antigen relationship be analogized as a search for a key on a ring with a million keys on it. As such, knowledge of where an antibody binds provides no information as to what such an antibody necessarily looks like (i.e., its primary amino acid structure). Applicant is reminded that the courts have long ruled that “Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895. As such, disclosure of a screening assay to test for functional properties of a reagent (such as the epitope to which the reagent binds or the fact that it does or does not inhibit some process) does not provide evidence of possession of the reagent itself.
In Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017), relying upon Ariad Pharms., Inc. v. Eli Lily & Co., 94 USPQ2d 1161 (Fed Cir. 2010), the following is noted. To show invention, a patentee must convey in its disclosure that they “had possession of the claimed subject matter as of the filing date. Demonstrating possession “requires a precise definition” of the invention. To provide this precise definition” for a claim to a genus, a patentee must disclose “a representative number of species within the scope of the genus of structural features common to the members of the genus so that one of skill in the art can visualize or recognize the member of the genus” (see Amgen at page 1358). Further, an adequate written description must contain enough information about the actual makeup of the claimed products – “a precise definition, such as structure, formula, chemic name, physical properties of other properties, of species falling with the genus sufficient to distinguish the gene from other materials”, which may be present in “functional terminology when the art has established a correlation between structure and function” (Amgen page 1361). Indeed, the courts have long ruled that “When a patent claims a genus using functional language to define a desired result, the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus.” See Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005). Also, “A sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can "visualize or recognize" the members of the genus.” See AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69. It should also be noted that the USPTO has released a Memo on the Clarification of Written Description Guidance For Claims Drawn to Antibodies and Status of 2008 Training Materials, 02/22/2018. See https://www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf. This Memo clarifies the applicability of USPTO guidance regarding the written description requirement of 35 U.S.C. § 112(a) concerning the written description requirement for claims drawn to antibodies and states: “In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional”. Further, the courts have indicated that the enablement and written description requirements of 35 USC 112 are separable as can be seen in for example Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111.
Applicant has broadly claimed a precursor trispecific antibody construct having essentially any two binding regions that bind to 5T4, essentially any one binding region that binds CD3ε, a protease cleavage domain comprising i) an amino acid sequence cleavable by a serine protease, cysteine protease, aspartate protease MMP, or a combination substrate cleaved by one or more of MMP2/9, uPA, matriptase, legumain, or any combination thereof, ii) a human serum albumin polypeptide, and iii) a Cap component which masks the CD3ε binding region. The broadest claims do not require the precursor trispecific antibody or ProTribody to have any function apart from binding 5T4 or CD3ε, being cleaved by a protease (i.e., protease cleavage domain), or reducing the binding of the anti-CD3ε Fab and CD3ε epitope (i.e., the cap). No claims recite the overall specific structure of the ProTribody that gives rise to the specific binding, cleavage, and inhibition of binding functions.
To support such broad claims, the specification teaches precursor trispecific antibody constructs 1-24 and the in vitro binding properties for constructs 1-6, and 13, 15, and 17. In the instance of the anti-EGFR x anti-CD3 constructs (i.e., constructs 1, 3, and 5), inclusion of human serum albumin (i.e., constructs 3 and 5) increased the half-life in healthy subjects by approximately 3 times. With regards to the in vitro binding properties, EGFR constructs 1, 3, 4, and 5 and 5T4 constructs 13, 15, and 17 have been thoroughly investigated regarding inhibition of binding to CD3ε due to the cap component, EGFR or 5T4 binding, CD3ε binding in the presence and absence of recombinant MMP9 (i.e., 100 μg/mL), and in the instance of 5T4 constructs 13, 15, and 17 the ability to induce T cell mediated cytotoxicity in the presence of T cell effector cells and MCF7 or NCI-H226 target cancer cells (i.e., 10:1 ratio). Although the claims are inclusive of 5T4 constructs of Fig 2F, the experimental data teach constructs of Fig 1, wherein both scFv anti-TAA binding regions are the same SEQ ID NO and also the same TAA (i.e., EGFR or 5T4, or constructs 3 and 4 or 15 and 16). Additionally, although essentially any anti-CD3ε Fab is claimed and any cap which reduces binding of the Fab to CD3ε antigen, the experimental data teach a specific VH/VL pair of the anti-CD3ε Fab, which specifically binds to the cap construct (i.e., SEQ ID NO: 5). Thus, if the cap construct is SEQ ID NO: 5, then the anti-CD3ε Fab binding region is defined by its function of binding CD3ε and also SEQ ID NO: 5; however, if the cap construct is only defined as reducing binding between the third binding region and CD3ε, then both the cap and anti-CD3ε Fab components are defined by their functions rather than structures and therefore lack written description. Furthermore, with regard to the T cell mediated cytotoxicity by the Tribody, ProTribody-C, and ProTribody-NC of Fig 43 and 44 teach that there is negligible difference between utilizing a protease (i.e., MMP9) cleavable linker (i.e., ProTribody-C) and non-protease cleavable linker (i.e., ProTribody-NC). Thus, it is unclear, whether the inclusion of the MMP2/9 cleavable linker results in the expected function of activating the ProTribody to allow recruitment of T cells to effectively induce cytotoxicity in MCF7 or NCI-H226 cancer cells expressing 5T4 and MMP9. Although alternative protease cleavable linkers are claimed, there are no working examples to support such claims.
Furthermore, the literature supports that the MMP9 concentration in plasma while elevated in cancer patients compared to normal, healthy patients is still well under the concentrations used for the in vitro studies of the instant application and that the choice of the cap component can influence the efficacy of a pro-antibody. Specifically, Iizasa, et al., teach that the normal concentration of MMP9 in plasma ranges from 11.4-59.4 ng/mL and the MMP9 plasma concentration in cancer patients ranges from 10-130 ng/mL, with approximately 45% of the NSCLC patients having elevated (i.e., greater than 59.4 ng/mL) MMP9 plasma concentrations (Iizasa, et al., Clin Cancer Res, 1999, 5, 149-153, see entire document). The instant application MMP9 in vitro studies (i.e., using 100 μg/mL MMP9) is more than 750 times the upper limit of MMP9 concentrations in cancer patients. Therefore, while the off-target effects of an unmasked CD3ε binding agent are reduced, the overall efficacy of ProTribody activation (i.e. function) will be significantly lower in vivo than in vitro at least in the instance of cleaving the regulatory domain using MMP9. Furthermore, the lack of efficacy can be compounded by the choice of masking component, which are typically grouped into i) masks with affinity for the binding domain (i.e., epitope peptide sequences for the binding region) or ii) masks with no affinity for the binding domain that rely on steric hinderance to block binding and that for any mask to effectively function, optimization of four parameters is necessary (Orozco, et al., Mabs, 2022, 14, 1-16, see entire document). For example, Chen, et al., teach that the use of epitope sequences recognized by the binding region as the mask or cap, which typically have high affinity, may remain bound after proteases have cleaved the linker between the antibody and the epitope peptide (i.e., SEQ ID NO: 5 of the instant application); a technical challenge that pro-antibody structures typically face (Chen, et al., Sci Rep, 2017, 7, 1-12, see entire document, specifically see ¶3 of the Discussion section). Therefore the literature supports that the Cap component and the protease cleavable linker significantly effect the efficacy of the masking/unmasking of a pro-antibody or in this specific instance one arm of a ProTribody. Furthermore, for a trispecific antibody, it is well known in the art, that three pairs of VH/VL regions are required, and each VH/VL pair consists of six CDRs for a total of 18 CDRs. Artisans are also well aware that knowledge of a given antigen (for instance a specific epitope of CD3ε or 5T4) provides no information concerning the sequence/structure of antibodies that bind the given antigen. For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well (Edwards, et al., J Mol Biol, 2003, 334, 103-118, see entire document). Goel et al. disclose the synthesis of three monoclonal antibodies that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (Goel, et al., J Immunol, 2004, 173, 7358-7367, see entire document). Further, it should be noted that degenerate binding of the same structural motif by antibodies does not require the existence of sequence homology or identity at any of their CDRs or other chemical similarities at the antigen-binding sites; side chain mobility of epitope residues can confer steric and electrostatic complementarity to differently shaped combining sites, allowing functional mimicry to occur (Lescar et al., J Biol Chem, 1995, 270, 18067-18076, see entire document, in particular Abstract and Discussion). As such, it does not seem possible to predict the sequence/structure of an antibody that binds a given antigen as there does not appear to be any common or core structure present within all antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound in a population of antibodies that bind to a given antigen no number of species appears to reasonably representative of the breadth of the genus of antibodies that bind the given antigen.
In this instance, the prior art supports at least six CDRs for each binding region of the precursor-trispecific antibody for a total of 18 CDRs, a defined sequence for the cap component, and a defined sequence for the protease cleavable linker sequence to appropriately function as a ProTribody for activation or binding at three different regions. As presently written, the claims recite that the binding regions, cap component, and protease cleavable linker functions to bind 5T4 or CD3ε, mask binding of the CD3ε binding region to CD3ε, and be cleaved in the presence of a protease allowing for activation of the trispecific antibody, respectively. However, the specification and working examples fail to disclose any data indicating that the breadth of structures (i.e., VH/VL pairs for 5T4 or CD3ε, multiple Cap components, or multiple protease cleavable linkers) encompassed by the language of the instant claims will have the same function (i.e., binding, masking, and cleaving). Therefore, as presently written, the claimed broad genus of a precursor trispecific antibody lacks adequate written description because there does not appear to be any correlation between the structure of all components of the ProTribody and the ability to bind, mask and cleave. Thus, one of ordinary skill in the art would reasonably conclude that the applicant was not in possession of the full breadth of the claimed genus of a precursor trispecific antibody that bind, mask, and cleave at the time the instant application was filed.
Double Patenting
Applicant’s arguments, see p 7-8, Response to provisional obviousness-type double patenting rejection section, filed 01DEC2025, with respect to the rejection(s) of claim(s) 1-4, 10, 14-15, and 18-20 (claims 2-4, 10, and 14-15 have been cancelled) under non-statutory double patenting have been fully considered and said rejections of claims 1 and 18-20 have been withdrawn in view of the claim amendments filed as part of said response.
Claim Rejections - 35 USC § 103
Applicant’s arguments, see p 8-16, Response to rejections under 35 USC §103 section filed 01DEC2025, with respect to the rejection(s) of claim(s) 1-11, 13-15, and 18-21 (claims 2-4, 6-11, and 14-15 have been cancelled) under 35 USC §103 have been fully considered and said rejections of claims 1, 5, 13, and 18-21 have been withdrawn in view of the claim amendments filed as part of said response.
Allowable Subject Matter
Examiner notes that the sequences of the VL-VH and VH-VL anti-5T4 scFv first and/or second binding domains consisting of SEQ ID NOs: 172 and 174, respectively are free of the prior art.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SAMANTHA L. HOPKINS whose telephone number is (703)756-4666. The examiner can normally be reached Mon-Thurs 6:00 AM to 4:00 PM EST.
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/SAMANTHA LAKE HOPKINS/Examiner, Art Unit 1641
/MICHAEL SZPERKA/Primary Examiner, Art Unit 1641