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 .
Priority
The instant application is claiming the benefit as a 35 U.S.C. 371 national phase application from, and claims priority to, International Application No. PCT/US20/46181, filing date 08/13/2020, which claims the benefit of the prior-filed United States Provisional Patent Application No. 62/887,523, filing date 08/15/2019.
Status of Application/Claims
The amendment, filed 04/02/2026, is acknowledged. Claims 1-53, 57, 64 are canceled. Claims 54-56, 60, and 62 are currently amended. Claims 65-69 are new. Claims 54-56, 58-63, and 65-69 are currently pending and are examined on the merits herein.
Information Disclosure Statement
No new IDS is submitted.
Withdrawn Objections & Rejections
Regarding the rejection for claim 64 under 35 U.S.C. 112(d) for failing to further limit the subject matter of the claim upon which it depends: Applicant amendment has addressed the issue and claim 64 is canceled. Thus, the rejection is withdrawn.
Regarding the rejection for claims 54, 56, 57-59, 62-63, and 64 and the rejection for claims 54-55, 57 and 58-59, 60-61, 64 under 35 U.S.C. 103 for obviousness: Applicant has canceled claim 57 and 64; thus, the rejections for claims 57 and 64 are withdrawn. Regarding the rejection for claims 54, 56, 57-59, and 62-63 over June and Kaufman (as evidenced by Muraro), and the rejection for claims 54-55, 58-59, 60-61 over June, Kaufman, and Yazaki, applicant arguments are not found to be persuasive. Thus, the rejections for these (amended) claims are maintained in modified form (see rejections and Response to Arguments below).
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.
Maintained in Modified Form
Claims 54, 56, 58-59, 62-63, 66-67, and 69 are rejected under 35 U.S.C. 103 as being unpatentable over June et al., US 2018/0243341A1 (published 08/30/2018; herein referred to as June), and further in view of Kaufmann et al., US 2018/0194859 (published 12/07/2018; herein referred to as Kaufmann); and, as evidenced by Muraro, et al. Generation and characterization of B72.3 second generation monoclonal antibodies reactive with the tumor-associated glycoprotein 72 antigen. Cancer Res. 1988, 15:48(16), p.4588-4596 (herein referred to as Muraro).
June teaches a method of treating cancer in a subject comprising administering a bispecific antibody bound to a T cell (abstract, paras 0009 and 0013 and 0239). June teaches bispecific antibodies comprising a combination of antibodies selected from the group consisting of anti-CD3 including muromonab-CD3 (i.e., humanized OKT3 as evidenced by instant disclosure p.42, lines 4-5; June p.1, [0009]; June p.24, [0261], and June p. 25, [0279]), anti-IgD Fc, and anti-IgA Fc. June teaches that the bispecific antibody is chemically hetero-conjugated (i.e., covalently bound) to an antibody specific for a tumor-associated antigen (TAA), wherein the T cells specifically bind the TAA antibody (i.e., each “antibody” comprises its own Fc domain; p.1, [0009], p.3, [0049], and p.4, [0053]). June further teaches that bispecific antibodies can be OKT3 and specific to any tumor antigen of choice (p.12, [0151], p.25, [0279]; Figs.14-15). June teaches that the antibodies can be of various forms, including polyclonal antibodies, monoclonal antibodies (e.g., M5A or CC49), Fv, Fab, scFv, and humanized antibodies (p.3, [0049]; p.6, [0081]; p.11, [0149; p.13, [0163]; p.14 – p.15, [0181] – [0186]); and that the bispecific antibodies can each bind the same antigen or different antigens (p.4, [0053]). June additionally teaches assessment of cytotoxicity in SK-BR3 (i.e., a breast cancer cell line) and HCT-8 (a colon cancer cell line) tumor cells after treatment of bispecific antibodies comprising HER2 antibody (i.e., HER2Bi) or EGFR antibody (i.e., EGFRBi; Figs.6 and Fig.15, p.2, [0020] – [0021]). June teaches the T cells of the invention may be autologous (p.22, [0247]); and, June teaches T cells wherein a vector may be used to introduce a chimeric intracellular signaling molecule or the CAR into a T cell in order to metabolically enhance a tumor specific T cell (p.15, [0187]; also, see claims 1 and 4, for example). June also teaches techniques for engineering and expressing bispecific antibodies which includes recombinant co-expression of two immunoglobulin heavy chain-light chain pairs having different specificities, “knob-in-hole” engineering, cross-linking two or more antibodies or fragments, using leucine zippers, using “diabody” technology; and using single-chain Fv dimers, preparing trispecific (p.11 – p.12, [0150]).
June does not explicitly teach that the OKT3/CD3 antibody is covalently bound to M5A or CC49 (instant claim 54 and 56); linking the antibodies via a linker or wherein the linker attached to a cysteine within the hinge region of each antibody (instant claims 54 and 56); or, that the OKT3 antibody Fc and CC49 antibody Fc regions are oriented in opposite directions for a 6-lobed bispecific antibody morphology (instant claims 54, 56, and 62). June also does not teach:
Instant claims 58, 61, and 63:
“…a linker that has the formula -L1-L2-L3-L4-L5-, and wherein L1, L2, L3, L4, and L5 are independently a bond, -O-, -S-, -C(O)-, -C(O)O-, -C(O)NH-, -S(O)2NH-, -NH-, -NHC(O)NH-, substituted or unsubstituted alkylene, substituted or unsubstituted heteroalkylene, substituted or unsubstituted cycloalkylene, substituted or unsubstituted heterocycloalkylene, substituted or unsubstituted arylene, or substituted or unsubstituted heteroarylene,”
or instant claim 59, 65, and 66:
“…wherein:
L1 is substituted heteroalkylene;
L2 is unsubstituted fused heterocycloalkylene, unsubstituted fused arylene, or unsubstituted fused heteroarylene;
L3 is unsubstituted heteroalkylene;
L4 is a bond; and
L5 is unsubstituted alkylene.
Kaufmann teaches linked dual antibodies conjugated at the hinge region (abstract and Fig.1) that can be used to target T-cells to a target, including tumor-associated antigens (p.1, [0003 – 0004]). Kaufman teaches that the dual antibodies can be comprised of full-length humanized monoclonal antibodies including muromonab-CD3 (i.e., OKT3) and minretumomab (i.e., humanized anti-TAG-72 (CC49) as evidenced by Muraro p.1-2; Kaufman p.2, [0034]; p.11, col.1, lines 29 and 26, respectively). Kaufmann teaches a linker molecule comprising a first hinge-joining moiety that covalently links both cysteine residues of a disulfide bond-forming cysteine pair of the first hinge and a second hinge of two antibodies (p.1, [0006-0013] and p.10, [0068]). Kaufman teaches that linkers with click chemistry handles (e.g., dibromomaleimide-PEG4-azide/DBM-PEG4-azide and DBM-PEG4-DBCO) can be used for the purpose of conjugating one hinge-containing antibody molecule to another hinge-containing antibody molecule to create a bispecific antibody (p.12, [0076]), which allows for the generation of dual antibodies from native, pre-existing monoclonal antibodies that have binding specificities to two different targets (p.1, [0005]). Kaufmann also teaches the specific linker dibromomaleimide-PEG4-azide (DBM-PEG4-azide; Fig.2A; p.12, [0076]) which comprises, in order: a substituted heteroalkylene (instant L1), an unsubstituted (fused) heterocycloalkylene (instant L2), an unsubstituted heteroalkylene (instant L3), an ether bond (instant L4 = “a bond”) and an unsubstituted alkylene (instant L5); thus, the linker reads on instant claims 58-59 (see Kaufmann DBM-PEG4-azide linker with instant application linkage notations below):
[AltContent: textbox (Kaufmann DBM-PEG4-azide with applicant L1-5 designations noted
[img-media_image1.png])] Further, Kaufman teaches methods for functionalizing hinge-containing antibody molecules comprising: reducing an antibody interchain disulfide bond in a hinge region of an antibody to produce two sulfhydryl groups; contacting the antibody with a linker wherein the linker comprises a sulfhydryl-reactive moiety and a biorthogonal moiety; and wherein the sulfhydryl reactive moiety comprises a DBM moiety and the biorthogonal moiety comprises a click chemistry handle comprising one or more moieties selected from an azide, nitrone, cyclooctyne, aldehyde, ketone, tetrazine, cyclooctene, isonitrile, quadricyclane, nickel bi(dithiolene), and DBCO (p.1, [0006] – p.2, [0015]; Figs.2A and 2B).
It would have been prima facie obvious for one of ordinary skill in the art before the effective filling date of the claimed invention to combine the teachings of June and Kaufman by producing a bispecific antibody (as taught by June and Kaufman) to comprise a humanized anti-CD3/OKT3 antibody that binds an autologous CAR T cell (as taught by June; and also taught as “muromonab” by Kaufman) and a humanized anti-CC49/TAG-72 antibody (i.e., a TAA; as taught by Kaufman as “minretumomab”; i.e., CC49 as evidenced by Muraro) using the DBM-PEG4-azide linker (as taught by Kaufmann) that binds a cysteine within the hinge region of the OKT antibody and a cysteine within the hinge region of a second antibody (as taught by Kaufmann) in order to recruit T-cells to tumor associated antigens (as taught by June and Kaufman). One of ordinary skill in the art would have been motivated to make such modifications and expect success because Kaufmann teaches the benefit of using click chemistry to join native monoclonal bispecific antibodies using linkers, and June teaches the benefit of using a CAR T cell wherein the CAR provides for metabolic enhancement of the T cell. One skilled in the art would also be motivated to use to linker taught by Kaufman because Kaufman teaches that a linker containing click chemistry functionalizing molecules like DBM-PEG4-azide and DBCO could be used to join the two antibodies which would predictably result in the formation of a bispecific antibody that brings T-cells and tumor cells into close proximity in order for the T-cells to therapeutically target the tumor cells. Regarding the morphology of the dual bispecific antibody wherein the Fc regions of each antibody are oriented in opposite directions and wherein the dual bispecific antibody has a 6-lobed morphology (instant claims 57, 60, 62): these claims describe inherent properties of the known dual bispecific antibody taught by the combination of June and Kaufman that does not render the claim patentably new (see MPEP §2112). The instant dual bispecific antibody comprising two antibodies functionalized by DBCO and PEGn-azide necessarily possesses the same linker connection as the dual bispecific antibody comprising two antibodies (taught by June and Kaufman) functionalized by DBCO and PEG4-azide click chemistry molecules forming the linker taught by Kaufman. As evidenced by the instant specification, a dual bispecific antibody formed by this linker would produce a main product wherein the Fc molecules are oriented in opposite directions and the molecule has a 6-lobed structure, wherein 4 lobes are formed by the Fabs of each of the first and second antibodies, 1 lobe each is formed by the Fc regions each antibody (see instant specification p.2, [0008] and Figs.1A-1B). Thus, the combination of June and Kaufman also teaches instant claims 57, 60, and 62 based on inherent structure/function properties.
Maintained in Modified Form
Claims 54-55, 58-59, 60-61, 65, and 67-68 are rejected under 35 U.S.C. 103 as being unpatentable over June, and further in view of Kaufmann, as applied to claims 54, 56, 58-59, 62-63, 66-67, and 69 above; and, in further view of Yazaki et al. A series of anti-CEA/anti-DOTA bispecific antibody formats evaluated for pre-targeting: comparison of tumor uptake and blood clearance. Protein Engineering, Design & Selection (2013), 26:3, p.187-193 (herein referred to as Yazaki).
The combination of June and Kaufmann teaches a bispecific antibody wherein a humanized OKT3 antibody is linked to a TAA antibody through a linker, wherein the linker is covalently attached to cysteines within a hinge region of each antibody using the specific linker taught by Kaufman as applied to instant claims 54, 58-59, 63, and 66 above for the purpose of targeting tumor cells for therapeutic cancer treatment; and, teaches and June teaches the autologous CAR T cell wherein the CAR provides for metabolic enhancement of the autologous T cell, as described above.
The combination of June and Kaufmann does not teach that the bispecific antibody comprises humanized M5A (instant claims 54-55, and 60); or, that the OKT3 antibody Fc and M5A antibody Fc regions are oriented in opposite directions for a 6-lobed bispecific antibody morphology (instant claims 54, 55, and 60).
Yazaki teaches bispecific antibodies wherein the TAA antibody is M5A, which is a humanized monoclonal antibody that recognizes carcinoembryonic antigen (CEA; title; abstract). Yazaki teaches that M5A can be radioiodinated to determine tumor targeting, blood distribution and pharmacokinetic properties (abstract). Yazaki further teaches that the M5A (i.e., “anti-CEA humanized hT84.66-M5A”) antibody has demonstrated high tumor accumulation as a direct radiolabeled agent in preclinical studies (p.187, col.2, para. 3).
It would have been prima facie obvious for one of ordinary skill in the art before the effective filling date of the claimed invention to further combine the teachings of June and Kaufman with the teachings of Yazaki by modifying a humanized anti-OKT3/CD3 bispecific antibody (as taught by both June and Kaufman) to comprise an anti-CEA/humanized hT84.66-M5A antibody (as taught by Yazaki) and to use the DBM-PEG4-azide linker (as taught by Kaufmann) that binds a cysteine within the hinge region of the OKT antibody and a cysteine within the hinge region of a second antibody (as taught by Kaufmann) in order to receive the expected benefit of M5A-mediated high tumor accumulation (as taught by Yazaki); and, to use June’s CAR-expressing T cell for the benefit of providing metabolic enhancement to the autologous T cell. One of ordinary skill in the art would have a reasonable expectation of success because June, Kaufmann, and Yazaki all teach bispecific antibodies for the purpose of T-cell mediated therapeutic targeting to tumor cells via TAA-binding antibodies. Regarding the morphology of the dual bispecific antibody wherein the Fc regions of each antibody are oriented in opposite directions and wherein the dual bispecific antibody has a 6-lobed morphology (instant claims 57, 60, 62): these claims describe inherent properties of the known dual bispecific antibody taught by the combination of June, Kaufman, and Yazaki that does not render the claim patentably new (see MPEP §2112). The instant dual bispecific antibody comprising two antibodies functionalized by DBCO and PEGn-azide necessarily possesses the same linker connection as the dual bispecific antibody comprising two antibodies (taught by June, Kaufman, and Yazaki) functionalized by DBCO and PEG4-azide click chemistry molecules forming the linker taught by Kaufman. As evidenced by the instant specification, a dual bispecific antibody formed by this linker would produce a main product wherein the Fc molecules are oriented in opposite directions and the molecule has a 6-lobed structure, wherein 4 lobes are formed by the Fabs of each of the first and second antibodies, 1 lobe each is formed by the Fc regions each antibody (see instant specification p.2, [0008] and Figs.1A-1B). Thus, the combination of June, Kaufman, and Yazaki also teaches instant claims 57, 60, and 62 based on inherent structure/function properties.
Response to Arguments
Regarding the rejection for claims 54, 56, 57-59, 62-63, and 64 and the rejection for claims 54-55, 57 and 58-59, 60-61, 64 under 35 U.S.C. 103 for obviousness: Applicant traverses in Applicant Arguments/Remarks filed 04/02/2026, p.5-10. Applicant arguments for the obviousness rejections are focused on 1) the 6-lobed morphology wherein the bispecific antibody comprises two antibodies oriented in opposite directions from one another, and 2) the specific antibodies used to form the bispecific antibody.
Regarding morphology:
On the first point, regarding morphology, the 6-lobed/opposite orientation morphology was previously found by the examiner to be taught by the prior art due to inherent properties of the bispecific antibody structure taught by the combination of June and Kaufman (for claims 54, 56, 58-59, and 62-64) and taught by the combination of June, Kaufman, and Yazaki (for claims 54-55, 57-61, and 64); wherein the structures taught by the combination of prior art teachings would be expected to have the same molecular structure and morphology as the claimed bispecific antibody (see non-final office action filed 01/05/2026, p.11-12 and p.13). Applicant argues that the prior art does not teach the 6-lobed/opposite orientation antibody because the prior art includes 2-dimensional graphical schematics that do not illustrate the claimed morphology. Applicant argues based on an illustration and description of June’s Fig.4 which describes one embodiment wherein a bispecific antibody harbors an Fc-Fc linkage rather than the claimed hinge-hinge linkage (see June Fig.4 and [0018] as well as Applicant Arguments, 04/02/2026, p.5). Applicant also assumes, based on Fig.15, that the linkage between the anti-CD3 and anti-HER2 antibodies are also not in the hinge region; though, this is unclear as the description in June [0279] does not state whether the linkage for this embodiment is an Fc-Fc linkage or a hinge-hinge linkage (see June Fig.15 and [0279] and Applicant Arguments, p.5-6).
Examiner Response: Regarding morphology: Applicant arguments are not persuasive. A bispecific antibody comprising the chemical structure of the claimed antibodies joined via the claimed linker, which is taught by the combination of prior art teachings would necessarily have the same 3-dimensional chemical and molecular structure as the claimed bispecific antibody structure, and would also be expected to necessarily possess the same morphology and functions. Further, prior art rejections, including obviousness rejections, are not necessarily limited to species that are graphically represented, but also include text descriptions within the reference in its entirety. Regarding June’s bispecific antibody of Fig.4 that comprises an Fc-Fc linkage, this is merely one example for bispecific antibodies that June teaches. When taken in it’s entirety, regarding linkages for bispecific antibodies, June defines bispecific antibodies (p.4, [0053]) and further provides that bispecific antibodies can be prepared using chemical linkage and cites “Brennan, et al. 1985” among the robust collection of bispecific antibody literature available prior to the effective filing date of the claimed invention (see June p.4, [0053] as well as Brennan, et al. Preparation of bispecific antibodies by chemical recombination of monoclonal immunoglobulin G1 fragments. Science, 1985, 229:4708, p.81-83 in its entirety, herein referred to as Brennan). A closer look at Brennan teaches that chemical linkage of two antibodies to produce a bispecific antibody via linking the antibodies at the hinge regions was known at least since 1985 (see Brennan, Fig.1 for example). As the combinations of June/Kaufman and June/Kaufman/Yazaki teach the same molecular structure of the instantly claimed bispecific antibody including the linkage, the combination of prior art teachings necessarily teaches the same morphology and functions produced by the instantly claimed bispecific antibody. Thus, the rejections are maintained in modified form.
Regarding antibodies:
On the second point, regarding the specific antibodies comprised within the claimed bispecific antibody, applicant argues that the rejection is based on hindsight analysis and “cherry picking” (Applicant Arguments, p.11, para.2). Applicant states that Kaufman “provides a list of about 470 different antibodies” (Applicant Arguments, p.10, para.2), highlights Kaufmann’s working example of a bispecific antibody comprising trastuzumab and cetuximab (Applicant Arguments, p.10, para.3), and states that “there is no reason for the skilled artisan to specifically select OKT3 from June and CC49 (minretumomab) from the list of 470 different antibodies described in Kaufmann (Applicant Arguments, p.10, para.5).
Examiner Response: Regarding the CC49 and M5A antibodies: Applicant arguments are not persuasive. In addition to June teaching the context for bispecific antibody generation comprising OKT3 antibody, June also teaches the concept of joining the OKT3 antibody (on an immune cell) to a second TAA cancer-targeting antibody in order to bring immune cells into close proximity with cancer cells for the purpose of treating cancer. Additionally, June (in its entirety) makes clear that the bispecific antibodies of June are not limited to select examples wherein the linkage is an “Fc-Fc” linkage. Kaufman not only teaches the chemical linker for the claimed bispecific antibody, but also teaches the context (in addition to June) that such dual antibodies conjugated at the hinge region can be used to target T-cells to a target, including tumor-associated antigens (see non-final office action, p.7); and, lists the CC49 antibody specifically. Yazaki not only teaches the M5A antibody as an attractive TAA, but also provides the motivation that the M5A antibody has demonstrated high tumor accumulation as a direct radiolabeled agent in preclinical studies. Yazaki and Kaufman, like June, are both concerned with bispecific antibody optimization for the purpose of targeting tumor cells for the treatment of cancer. Thus, a skilled artisan would be led to Kaufman and Yazaki because the teachings of June, Kaufman, and Yazaki are in the same field of endeavor and specifically concerned with bispecific antibody production and specifically for bringing immune cells into close proximity with cancer cells for cancer treatment. The combination of prior art references leads to the predictable result of a bispecific antibody that tethers T cells with cancer cells via targeting a TAA on a cancer cell.
Further, prior art rejections under 35 U.S.C. 103 do not require a single embodiment taught by a single reference. Prior art rejections under 35 U.S.C. 103 are valid if any of the KSR rationales can be used in an explicit analysis, and that an explicit analysis does not require record evidence of an explicit teaching of a motivation to combine the prior art (see MPEP § 2143). This is in contrast to prior art rejections under 35 U.S.C. 102, which requires that a single prior art reference must disclose each and every element of the claimed invention, either expressly or inherently (see MPEP § 2131). In addition to the combination of teachings and motivation rationales used in the previous office action, it is additionally noted that the “obvious to try” rationale is also applicable in the context of the instantly claimed invention. The fact that Kaufman lists approximately “470 antibodies” does not necessarily preclude the reference from being cited in an obviousness rejection which takes into account the “characteristics of the science or technology, its state of advance, the nature of the known choices, the specificity or generality of the prior art, and the predictability of results in the area of interest” (see MPEP § 2143, Section E). In the context of the claimed invention, at the time of the effective filing date, the bispecific antibody prior art was robust as was the level of knowledge about using bispecific antibodies to target tumor associated antigens. The cited prior art references are additionally focused on solving the same problem: using a bispecific antibody harboring a T cell antigen binding antibody to a tumor associated antigen binding antibody. Additionally, the OKT3, M5A, and CC49 antibodies were well-known at the time of the effective filing date. The instantly claimed antibodies are not otherwise described to have any additional innovative features (e.g., sequence, mutation, etc.) that are able to overcome the obviousness rejections. Therefore, the rejections are maintained in modified form.
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.
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 Jami M Gurley whose telephone number is (571)272-0117. The examiner can normally be reached Monday - Friday, 8am - 4pm.
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/JAMI MICHELLE GURLEY/Examiner, Art Unit 1647
/JOANNE HAMA/Supervisory Patent Examiner, Art Unit 1647
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