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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 06/15/26 has been entered.
Claims 1, 6, 13 and 20 have been amended. Claims 2-3, 5, 7-10, 12, 14-16, 18, 21-24, 26 and 28 were previously canceled. Claims 6, 11, 13, 17, 19-20, 25 and 27 remain withdrawn as being directed to non-elected inventions. Accordingly, claims 1 and 4 are under examination.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1 and 4 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.
Regarding the pending claim language of claim 1, the recited language limits the claims to monoclonal antibodies, however said antibody (is described only in terms of function rather than structure. In particular, the claims may be interpreted as reciting that the antibodies, that has certain desired binding properties, namely that they bind to an epitope consisting of a portion of the free hapten.
Regarding claim 1, the claims encompass a large genus of products that may be characterized by substantial variability; put another way, the claimed genus encompasses many possible species of monoclonal antibodies, and antibody fragments each potentially binding an epitope consisting of a portion of the free hapten as claimed, each characterized by a potentially different antibody sequences. For example, regarding the hybridoma obtained antibodies, every hybridoma created is going to produce a specific antibody, no two having the same sequence.
The claims encompass a large and highly variable genus as there is no way to visualize what antibodies (which specific antibodies characterized by their own distinct sequences of heavy and light chain regions) would bind the specific portion of hapten as claimed (the monoclonal antibodies are described only in terms of what they bind, i.e. the antigens to which they bind, rather than structure specific to the antibodies themselves), and the claims are not limited to any particular antibody producing hybridoma cell line(s). The recited claim language attempts to place limitations on the monoclonal antibodies by what they do, and as a result places no limitations on the sequences/structure of the antibodies themselves (rather defines the antibodies only in terms of desired binding properties, thereby limiting the antibodies of the claims only to those that achieve the desired functions).
The claim scope is potentially enormous depending on how many potential species of the recited genus that meet the structural requirements also meet the functional requirements (the binding described). The originally filed specification fails to disclose any sufficient identifying characteristics specific to the claimed genus of antibodies such to correlate antibody structure with the recited function in a way that would allow one to readily visualize what species of the claimed genus would also exhibit the required functional ability. For example, even in the case of binders that are antibodies, one cannot readily visualize the structure(s) of the antibodies that would be encompassed by the recited claims. Without some identified structure, one cannot readily distinguish between those binders encompassed by the recited language, from those excluded from the claim. As an example, consider binders that are antibodies: one cannot readily visualize what anti-hapten antibodies exhibit the desired binding functions, and bind one of the claimed fragments from those known anti-tacrolimus, anti-everolimus and anti-sirolimus antibodies that do not bind these portions of hapten. As presented (referring to claims 1), the pending claim language would encompass any and all antibodies produced by any hybridoma cell line produced using B-cells from a mammal immunized with tacrolimus, everolimus and sirolimus. Having the sequences of the fragments as claimed (i.e., fragments to which the antibodies bind) fails to provide sufficient structure specific to the antibodies (monoclonal) to allow one to distinguish what species achieve the desired binding functions from those that do not.
The originally filed specification fails to identify any particular species reading on the claimed genus.
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04.
For a claim to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Reagents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). The recitation of a functional property alone, which must be shared by the members of the genus, is merely descriptive of what the members of the genus must be capable of doing, not of the substance and structure of the members. The Federal Circuit has cautioned that, for claims reciting a genus of antibodies with particular functional properties (e.g., high affinity, neutralization activity, competing with a reference antibody for binding, binding to a certain epitope), “[c]laiming
antibodies with specific properties, e.g., an antibody that binds to human TNF-a with A2
specificity, can result in a claim that does not meet written description even if the human TNF-a protein is disclosed because antibodies with those properties have not been adequately described." Centocor Ortho Biotech Inc. vy. Abbott Labs., 97 USPQ2d 1870, 1875, 1877-78 (Fed. Cir. 2011).
Along these same lines, a more recent Federal Circuit decision, Amgen v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017), describes how when an antibody is claimed, 35 U.S.C. § 112(a) requires adequate written description of the antibody itself; not just a description of the sequence to which the antibody binds. Amgen, 872 F.3d at 1378-79.
It is true that functionally defined claims can meet the written description requirement if a reasonable structure-function correlation is established, whether by the inventor as described in the specification or known in the art at the time of the filing date” (AbbVie, 759 F.3d at 1298, reiterating Enzo Biochem, Inc., 323 F.3d at 964)(emphasis added).
In the present case, there is insufficient evidence of such an established structure-function correlation in the case of monoclonal antibodies, for example, that bind the very specific epitope consisting of a portion of the free hapten.
A claimed invention may not be adequately described where an invention is described solely in terms of a method of its making coupled with its function and there is no described or art recognized correlation or relationship between the structure of the invention and its function. A biomolecule defined solely by its ability to perform a function, such as to serve as an antigen recognizing construct, without a known or disclosed correlation between that function and the structure of the sequence, normally is not a sufficient identifying characteristic for written description purposes, even when accompanied by a method of obtaining the biomolecule of interest, see MPEP 2163.
As discussed in the recent case of Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017), see page 17: An adequate written description must contain enough information about the actual makeup of the claimed products—“a precise definition, such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other materials,” which may be present in “functional” terminology “when the art has established a correlation between structure and function.” Ariad, 598 F.3d at
1350. But both in this case and in our previous cases, it has been, at the least, hotly disputed that knowledge of the chemical structure of an antigen gives the required kind of structure-identifying information about the corresponding antibodies. See, e.g., J.A. 1241 (549:5-16) (Appellants’ expert Dr. Eck testifying that knowing “that an antibody binds to a particular amino acid on PCSK9 .. . does not tell you anything at all about the structure of the antibody”); J.A. 1314 (836:9-11) (Appellees’ expert Dr. Petsko being informed of Dr. Eck’s testimony and responding that “[m]y opinion is that [he’s] right”); Centocor, 636 F.3d at 1352 (analogizing the antibody- antigen relationship as searching for a key “on a ring with a million keys on it’) (internal citations and quotation marks omitted).
Amgen Inc. v. Sanofi further notes, pointing to Ariad Pharms., Inc. v. Eli Lilly & Co., 94 USPQ2d 1161 (Fed Cir. 2010): To show invention, a patentee must convey in its disclosure that it “had possession of the claimed subject matter as of the filing date.” Id. at 1350. Demonstrating possession “requires a precise definition” of the invention. Id. To provide this “precise definition” for a claim to a genus, a patentee must disclose “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.” Id. Amgen at pages 7-8.
In this case, there is no disclosure of any species such to be sufficient to represent the claimed genus of monoclonal antibodies having the recited functional properties. There is substantial variability in the genus. Since there are a substantial variety of compounds possible within the genus, without disclosure of any common partial structure or other sufficient identifying characteristics of the genus, the claimed genus is not sufficiently described.
Regarding predictability, without some guidance such as structure-function correlation, it is not possible to visualize the species encompassed by the genus based on recitation of function alone. The teachings of Harlow & Lane (Antibodies, A Laboratory Manual, Cold Spring Harbor laboratory, 1988, pages 25-26 and 37-59) describe how the steps of the humoral immune response to an immunogen are dependent on APC, T-cell and B-cell recognition and processing of the immunogen in ways well known in the art to be highly unpredictable and heavily influenced by the particular immunogen and the specifics of the immunization protocol. Harlow
et al. teach that even small changes in structure, such as loss of a single hydrogen bond, can profoundly affect antibody-antigen interaction (p. 25, last paragraph to page 26, second paragraph).
The principles laid out in Harlow are further illustrated in the teachings of Edwards et al.("The remarkable flexibility of the human antibody repertoire; isolation of over one thousand different antibodies to a single protein, BLyS"” J. Mol. Biol. (2003) 334, 103-118, DOI:10.1016/).jmb.2003.09.054), which shows the immense combinatorial flexibility and capacity of the human antibody repertoire to generate binding sites to an individual protein antigen, the B-lymphocyte growth factor known as “BLyS” (see entire document). Edwards describes in detail how the breadth of antibody structures against a given immunogen can be influenced by the immunization and/or selection methods (see Discussion Section).
Lloyd et al. ("Modelling the human immune response: performance of a
10e11 human antibody repertoire against a broad panel of therapeutically relevant antigens”, Protein Engineering, Design and Selection, Volume 22, Issue 3, 1 March 2009, Pages 159-168, https://doi.org/10.1093/protein/gzn058) also shows a repertoire of 1x1011 human antibody variable regions can generate large numbers of unique, biologically active scFvs against a variety of polypeptide targets (see e.g., at page 161-62 bridging paragraph and in Table 1, cited herewith).
Further, as another example in the art illustrating the potential scope of the genus of binders (e.g., just with respect to antibodies) encompassed by the pending claim language, see also Meyer et al., (“New Insights in Type I and II CD20 Antibody Mechanisms-Of-Action With a Panel of Novel CD20 Antibodies”, British Journal of Haematology, 2018, 180, 808-820, |https://doi.org/10.1111/bjh.15132). Meyer describes the core binding region of the well-known anti-CD20 antibody rituximab corresponds to amino acid residues 170ANPS173, wherein N171 is the key residue for binding. By contrast, the OBZ and B1 anti-CD20 antibodies share an overlapping epitope with rituximab (170OANPSEKNSP178); however, in contrast to rituximab residues at positions 176-178 contribute the most to binding (see page 809, left col., 2nd full paragraph). Meyer also described the production and characterization of a panel of new anti-CD20 antibodies which were shown to bind epitopes contained within or nearby the rituximab 170ANPS173 epitope but to bind to different residues than rituximab binds in this region (see page 811, “New CD20 mAbs with overlapping, but distinct epitopes,” see also page 815-16 bridging paragraph). More particularly, Meyer teaches the newly created anti-CD20 mAbs m1 and m2 were found to bind within but also in the vicinity of the rituximab binding site (m1 and m2) and elsewhere (m2):“detailed epitope mapping was performed for both mIgG2c-CD20 mAbs m1 and m2, by using PepScan technology. We identified the critical residues of m1 to be 168EPANPSEK175 by using linear (Figure $2A) and circular (Fig 2C, left) peptides with a positional amino acid scan covering the larger extracellular loop. Also for m2, a signal decrease below the WT binding signal occurred within the 1683EPANPSEK175 sequence motif but the binding signal to the linear (Figure S$2B) and circular (Fig 2C, right) peptide was rather low. This suggests that the epitope of both mAbs is located on the larger loop in the same region, however their binding characteristics are different. The data suggests that m1 binds a linear epitope, whereas m2 binds to a conformational epitope.” (see ibid).
Moreover, while these antibodies of Meyers bind within or nearby the rituximab 170ANPS173 epitope they do so with heavy and light chain CDRs non-homologous to those of rituximab.
The art establishes that even if multiple antibodies bind epitopes within the same small region of a given polypeptide, it is not uncommon for said antibodies to bind to different amino acid residues even within said small region and for said antibodies to have dissimilar CDRs.
The above cited evidence establishes the unpredictability in the art; one cannot readily visualize or recognize the identities of the members of the claimed genus that would be encompassed by the claim and possess both the required functional and structural characteristics claimed. Applicant was not in possession of all binders as claimed capable of the recited binding function. The characteristics defining the genus of binder are unknown as the recited language sets forth only what the binders do and now what they are. There is no disclosure of partial structure or other common structural feature, common to the members of the claimed genus encompassed by the claim, which are responsible for the recited/required function.
Recent court cases 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 AbbVie Deutschland GmbH y. Janssen Biotech. Inc. as well as Amgen v. Sanofi, as discussed above. 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.
While it is within the skill level of the ordinary artisan to make and screen for antibodies having the claimed functional properties, one cannot envision their structure. Rather, the fact that screening would be necessary to determine which antibodies result in the desired functional ability (necessary in order to determine whether an antibody falls within the scope of the claim) is further evidence that the genus is not adequately described such to convey possession.
Screening amounts to only a plan for identifying the claimed antibodies, and is not a description of the antibodies themselves. Similarly, it was held in the University of Rochester v. G.D. Searle & Co., Inc., 358 F.3d 916, 927 (Fed. Cir. 2004) that the disclosure of "assays for screening compounds, including peptides, polynucleotides, and small organic molecules to identify those that inhibit the expression or activity of the PGHS-2 gene product," did not satisfy the written description requirement for claims requiring administration of a "compound that selectively inhibits PGHS-2"). See also, Ariad Pharmaceuticals, Inc., v. Eli Lilly and Company, 598 F.3d 1336, 1344 (Fed. Cir. 2010) (recognizing distinction between requirements for written description and enablement), and Centocor, 636 F.3d 1350 ("The fact that a fully-human antibody could be made does not suffice to show that the inventors ... possessed such an antibody.").
A biomolecule defined solely by its ability to perform a function, such as to serve as an antigen recognizing construct, without a known or disclosed correlation between that function and the structure of the sequence, normally is not a sufficient identifying characteristic for written description purposes, even when accompanied by a method of obtaining the biomolecule of interest. See MPEP 2163.
For all of these reasons, the specification fails to convey evidence of possession of the entire genus of monoclonal antibodies.
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.
Claims 1 and 4 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, lines 8-9 &12-13 the recitation “an epitope consisting of a portion of the free hapten” is vague and indefinite because it is unclear what portion the applicant is referring to. The claim does not make clear if the epitope is an n-terminal portion, a c-terminal portion, in the middle, if Applicant intends an amino acid sequence, a specific amino acid or if the Applicant intends something else. Also, although the claim appears to try and limit the epitope the claim as currently recited allows for any portion of the free hapten and does not provide a specific epitope. It is unclear what the applicant intends and what the applicant is trying to encompass. Applicant is reminded that although the claims are read in light of the specification limitations from the specification are not read into the claims.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1 and 4 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Sigler et al (US 2008/0081379).
Sigler et al discloses a particle having two monoclonal antibodies for an immunosuppressant drug (hapten) wherein each antibody has specificity for a different site on the immunosuppressant drug (e.g. para 0057). Sigler et al discloses that the immunosuppressant drug can be tacrolimus (e.g. para 0056). Sigler et al discloses that the particles can be a latex particle (e.g. para 0030, 0058).
With respect to the recitations “for detection of a hapten released from its endogenous binding protein/immunophilin complex” and “whereby binding of free hapten to the diagnostic immunoassay reagent results in particle enhanced agglutination for signal detection” as recited in claim 1. These limitations are intended use of the reagent. Applicant is reminded that a recitation of the intended use of the claimed invention, i.e. use of the reagent for binding of hapten, must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. In a claim drawn to a process of making, the intended use must result in a manipulative difference as compared to the prior art. See In re Casey, 152 USPQ 235 (CCPA 1967) and In re Otto, 136 USPQ 458, 459 (CCPA 1963). Sigler et al discloses the same particle and binding partner as recited in the instant claims and therefore the reagent is capable of binding to a free hapten released from it endogenous binding protein/immunophilin complex and would result in particle enhanced agglutination for signal detection.
Response to Arguments
Applicant's arguments filed 06/15/26 have been fully considered but they are not persuasive.
112(a) Rejection:
Applicant argues that the claims have been amended to use the term “monoclonal antibody or antigen binding fragment thereof and that the term antibody is disclosed in the specification.
This argument is not found persuasive because of reasons stated above that the claims encompass a large and highly variable genus and said antibodies are described only in terms of function rather than structure and the . In particular, the claims may be interpreted as reciting that the antibodies, that has certain desired binding properties, namely that they bind to an epitope consisting of a portion of the free hapten.
102 Rejection:
Applicant argues that according to Sigler et al., the antibodies utilized therein are raised against a complex comprising an immunosuppressant drug AND an immunophilin (see, for example, Paragraphs [0056]-[0058] of Sigler et al.). While the antibodies may recognize two different sites on the immunosuppressant drug, those two sites on the drug are NOT the entire epitopes for binding. This is because the epitope for each of the two antibodies constitutes not only the site on the drug but ALSO a portion of the immunophilin. In other words, the site on the drug recognized by the antibody, although necessary, is not sufficient for the antibody binding; because the immunogen is in the form of a drug/immunophilin complex, the epitope will also include adjacent amino acid residues or chemical groups from the immunophilin. Using FK506 (tacrolimus) as an example, when the drug is complexed with the immunophilin FKBP12, the 804 dalton drug is half buried in immunophilin FKBP12 (see figure below), with only about half of the drug molecule exposed for antibody binding. When the two antibodies bind to the drug/immunophilin complex (see left graph), each antibody not only recognizes and binds a site on the drug but also requires recognition of some amino acid residues (or chemical groups) from the neighboring.
This argument is not found persuasive the instant claims are not directed to a method of detecting free hapten but are rather directed to a reagent (product) which is capable of binding to free hapten. In the instant case Sigler et al discloses the same antibodies (monoclonal antibodies) as currently recited and applicant is reminded that the recitations “for detection of a hapten released from its endogenous binding protein/immunophilin complex” and “whereby binding of free hapten to the diagnostic immunoassay reagent results in particle enhanced agglutination for signal detection are intended use of the reagent. Applicant is reminded that a recitation of the intended use of the claimed invention, i.e. use of the reagent for binding of hapten, must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. In a claim drawn to a process of making, the intended use must result in a manipulative difference as compared to the prior art. See In re Casey, 152 USPQ 235 (CCPA 1967) and In re Otto, 136 USPQ 458, 459 (CCPA 1963). Sigler et al discloses the same particle and binding partner as recited in the instant claims and therefore the reagent is capable of binding to a free hapten released from it endogenous binding protein/immunophilin complex and would result in particle enhanced agglutination for signal detection. Further, Applicant’s statement “that while the antibodies may recognize two different sites on the immunosuppressant drug, those site on the drug are not the entire epitopes for binding” appears to provide evidence that the antibodies are capable of binding to an epitope consisting of a portion of the free hapten.
Applicant argues that Sigler et al. does NOT explicitly or implicitly disclose a diagnostic immunoassay reagent that comprises a particle having two monoclonal antibodies (or antigen binding fragments thereof) bound thereto, wherein each of the two monoclonal antibodies (or antigen binding fragments thereof) specifically binds to an epitope consisting of a portion of a free hapten (i.e., a hapten that has been released from its endogenous binding protein/immunophilin complex), as claimed. As such, Applicant respectfully submits that currently pending claims 1 and 4 are not anticipated by Sigler et al.
This argument is not found persuasive because the hapten being in free form or in a complex is irrelevant to the instant reagent because the hapten being in free form is intended use of the reagent. Sigler et al discloses the same monoclonal antibodies as currently recited and therefore the Sigler et al antibodies would bind to the recited hapten and would bind to an epitope as currently recited. With respect to the functionality of the antibodies and intended use of the reagent, the federal circuit affirmed, stating that "once a product is fully disclosed in the art, future claims to that same product are precluded, even if that product is claimed as made by a new process." The above reagent falls within the SAME scope as recited in claims. As disclosed in Sigler the above antibodies are the same as currently recited and are therefore capable of use in a method of detecting a hapten released from its endogenous binding protein/immunophilin complex. Applicant is also reminded that a recitation of the intended use of the claimed invention, i.e. binding an epitope consisting of a portion of the free hapten, must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. In a claim drawn to a process of making, the intended use must result in a manipulative difference as compared to the prior art. See In re Casey, 152 USPQ 235 (CCPA 1967) and In re Otto, 136 USPQ 458, 459 (CCPA 1963).
Conclusion
No claims are allowed.
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/GARY COUNTS/ Primary Examiner, Art Unit 1678
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