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 .
Application Status
The amended claims filed on July 25, 2025 are acknowledged. Claims 1-29 are canceled. Claims 30-46 are newly added. Claims 30-46 are pending and under examination herein.
Objections to the Specification and Drawings Withdrawn
The objections to the specification are withdrawn in view of Applicant’s amendments thereto.
The objections to Figures 1, 4-5, and 8 are withdrawn in view of Applicant’s replacement drawings.
Claim Objections Withdrawn
All prior objections of claims 8, 11-12, and 20 are rendered moot by the cancelation of the claims.
Claim Rejections Withdrawn
All prior rejections of claims 1-3, 5-13, 16-24, and 26-29 are rendered moot by the cancelation of the claims.
NEW OBJECTIONS AND REJECTIONS NECESSITATED BY AMENDMENT
Drawings
The drawings set forth in Figures 9 and 10 are objected to because the figures
depict amino acid sequences that are not identified by sequence identification numbers in the
figures or in the Brief Description of the Drawings on pages 3-4. Specifically, Figure 9 comprises “sequences shown which correspond to the immunization peptides used in this invention”, for which the corresponding sequence identifiers (SEQ ID NOs) are not recited in the figure or in the figure caption. Figure 10 shows a sequence highlighted in gray “which corresponds to immunization peptide 3 used in this invention”, for which the corresponding sequence identifier (SEQ ID NO) is not recited in the figure or in the figure caption. Sequences appearing in the specification and/or drawings must be identified by a sequence identifier (i.e., SEQ ID NO) in accordance with 37 C.F.R. 1.821 (d). Sequence identifiers for sequences appearing in the drawings may appear in the drawings or in the brief description of the drawings.
A replacement drawing sheet including the correction is required when the drawings are
objected to by the Examiner. See 37 CFR 1.121 (d). However, this ground of objection would be
withdrawn, such that a replacement drawing would be not be required, if the Applicant were to
amend the Brief Description of the Drawings on pages 3-4 of the specification to include
sequence identification numbers.
Claim Objections
Claim 32 is objected to because the claim recites that the juxtamembrane domain comprises “an amino acid corresponding to residues 431-459 of SEQ ID NO 16”. It is believed that this phrase should instead recite “an amino acid sequence corresponding to residues 431-459 of SEQ ID NO 16”.
This is a new objection necessitated by claim amendment. 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.
Claims 30-36, 40-43, and 45-46 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. This is a new rejection necessitated by claim amendment.
“[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).
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 it may be satisfied by the 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. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species. Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010).
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). “[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.” Ariad, 598 F.3d at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). A “representative number of species” means that those species that are adequately described are representative of the entire genus. 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. For example, the Federal Circuit has found that possession of a mouse antibody heavy and light chain variable regions provides a structural "stepping stone" to the corresponding chimeric antibody, but not to human antibodies. Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1875 (Fed. Cir. 2011).
Amgen Inc. v. Sanofi, Aventisub LLC, 872 F.3d 1367 (Fed. Cir. 2017) supported previous decisions (Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341 (Fed. Cir. 2011); AbbVie Deutschland GmbH & Co. v. Janssen Biotech, Inc., 759 F.3d 1285 (Fed. Cir. 2014)) that defining an antibody solely by what it binds does not satisfy the written description requirement, stating that this would allow patentees to “claim antibodies by describing something that is not the invention, i.e., the antigen”. Thus, claiming an antibody by describing the invention by what it does (function) rather than what it is (structure) is invalid. This can be overcome if a relevant number of species with structure/function correlation is known to the art or present in the specification. See also pages 206-208 of Deng (mAbs (2018) 10(2): 204-209; cited in IDS).
The claimed invention. The nature and scope of the claimed invention at issue is a method for inhibiting and/or reducing TACE/ADAM17 activity in a subject, the method comprising administering to the subject an antibody or fragment thereof that specifically binds to the juxtamembrane domain adjacent to the transmembrane domain 1 (TMD1) of human iRhom2 (as recited in claim 30 and its dependent claims). This limitation fails to satisfy the written description requirement because the antibody or fragment thereof administered in the instantly claimed method is defined by its functional attributes (i.e., binding to a specific epitope of human iRhom2) without reciting a corresponding structure expected to correlate with said function. Claims 31-36, 40-43, and 45-46, which depend from claim 30, do not remedy these written description issues raised by the independent claim.
Claim 31 further sets forth that administration of the antibody or fragment thereof of claim 30 inhibits or reduces TNF-α shedding. The claim further defines the antibody by its functional properties, without reciting a specific structure (e.g., amino acid sequence) expected to correlate with the specifically claimed functions.
Claim 32 further sets forth that the juxtamembrane domain comprises an amino acid [sic] corresponding to residues 431-459 of SEQ ID NO: 16, and claim 33 recites that the epitope bound by the antibody or fragment thereof comprises the amino acid sequence set forth in SEQ ID NO: 3. These claims continue to further define the epitope bound by the antibody administered in the instantly claimed method, without reciting a corresponding structure expected to perform the function of binding to said epitope.
Claim 40 recites that the antibody or fragment thereof comprises a heavy chain variable region (VH) comprising an amino acid sequence having “at least 90% sequence identity” to the amino acid sequence of SEQ ID NO: 33, and claim 41 sets forth that the antibody or fragment thereof comprises the VH amino acid sequence set forth in SEQ ID NO: 33. While these claims partially or completely recite a structure of the VH of the anti-human iRhom2 antibody, it is insufficient to satisfy the written description requirement because claim 40 allows for up to 10% variability in the VH sequence, inclusive of the CDRs (which confer the antigen-binding properties of an antibody VH), and both claims are structurally ambiguous with respect to the corresponding VL. Similarly, claim 42 recites that the antibody or fragment thereof comprises a light chain variable region (VL) comprising an amino acid sequence having “at least 90% sequence identity” to the amino acid sequence of SEQ ID NO: 40, and claim 43 sets forth that the antibody or fragment thereof comprises the VL amino acid sequence set forth in SEQ ID NO: 40. While these claims partially or completely recite a structure of the VL of the anti-human iRhom2 antibody, it is insufficient to satisfy the written description requirement because claim 42 allows for up to 10% variability in the VL sequence, inclusive of the CDRs (which confer the antigen-binding properties of an antibody VL), and both claims are structurally ambiguous with respect to the corresponding VH. Based on the state of the prior art, one of ordinary skill in the art would not be able to visualize or recognize a complete structure (comprising three heavy chain CDRs and three light chain CDRs) expected to correlate with the instantly claimed function of binding to the juxtamembrane domain adjacent to the TMD1 of human iRhom2.
Of note, claims 37- 39 (which recite a complete combination of three heavy chain CDR and three light chain CDR amino acid sequences) and claim 44 (which recites a complete combination of VH and VL amino acid sequences, inclusive of their respective CDRs) recite a sufficient level of structure expected to correlate with the instantly claimed function of binding to a juxtamembrane domain of the TMD1 of human iRhom2 based on Applicant’s disclosure, and are not included in this rejection.
State of the prior art. It is well established in the art that the formation of an intact antigen-binding site in an antibody usually requires the association of the complete heavy and light chain variable regions of a given antibody, each of which comprises three CDRs (or hypervariable regions) that provide the majority of the contact residues for the binding of the antibody to its target epitope. See Almagro (Frontiers in Immunology (2018) 8: 1751; cited in PTO-892 mailed January 28, 2025) at “The IgG Molecule” (page 3) and Figure 1. Sela-Culang (Frontiers in Immunology (2013) 4: 302; cited in PTO-892 mailed January 28, 2025) further teaches, “A major focus in analyzing the structural basis for [antigen] recognition has been in identifying the exact boundaries of the CDRs in a given [antibody]. It is a common practice to identify paratopes through the identification of CDRs” (page 3, left column, “CDRs Identification”).
Although the prior art teaches some understanding of the structural basis of antigen-antibody recognition, it is aptly noted that the art is characterized by a high level of unpredictability, since the skilled artisan still cannot accurately and reliably predict the consequences of amino acid substitutions, insertions, and deletions in the antigen-binding domains. Ni (The Protein Journal (2024) 43: 683-696; cited in PTO-892 mailed January 28, 2025) teaches, “Mutations, even one mutation, introduced in the CDRs through [somatic hypermutation] can change the binding properties and repertoire of antibodies. However, how just one-point mutation can dramatically change the recognition profiles of the antibody is still unclear” (Introduction). Furthermore, while affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody, those techniques involve trial-and-error testing and the changes that maintain or improve affinity are not predictable a priori (Almagro et al., pages 3 and 6-7).
Gershoni (Biodrugs (2007) 21(3): 145-156; cited in PTO-892 mailed January 28, 2025) teaches that antibody binding to the same antigen, or even the same epitope on that antigen, can be accomplished with an impressively wide variety of antibody structures, even when the antibodies are limited to those from a particular source (page 146, Section 1.1). The skilled artisan therefore understands that antibodies from a variety of different sources may bind the same antigen and even mediate the same functional effects, but differ widely in the details of the structure of their antigen-binding sites, particularly in the amino acid sequence. Further, the state of the art recognizes that it is not possible to predict the amino acid sequence when an epitope is recited, because there are many different epitope arrangements, such as linear and discontinuous epitopes, that are dictated by the unique interaction between an antibody and its cognate epitope (Blythe, Protein Science (2005) 14:246-248, at page 246; cited in PTO-892 mailed January 28, 2025).
With respect to iRhom2, Siggs (Immunobiology (2012) 119(24): 5769-5771; cited in IDS) teaches that iRhom2 may be an attractive target for inflammatory diseases in view of its role in the secretion of TNF-α, a proinflammatory cytokine synthesized in response to activation of Toll-like receptor (TLR) signaling pathway (page 5769). Exemplary antibodies to iRhom2 (also known as “RHBDL5” and “RHBDL6”) are described by Bicknell (WO 2009/044158 A2; cited in PTO-892 mailed January 28, 2025), Issuree (US 2015/0241429 A1; cited in IDS), and Blobel (US 10,024,844 B2; cited in PTO-892 mailed January 28, 2025).
Scope of species disclosed in original specification. The working examples discuss the generation of iRhom2 immunization peptides and screening for anti-iRhom2 activity-neutralizing antibodies, wherein iRhom2-knockout mice were immunized with human iRhom2 peptide mixes and hybridoma cells were generated from the resulting splenic lymphocytes (Examples 1-5; Figure 1). A single supernatant collected from the hybridoma cell population “4H8” interfered with LPS-induced TNF-α shedding in THP-1 cells (Example 5). The oligoclonal “4H8” clone was expanded, and three monoclonal subclones (4H8-D4, 4H8-E3, and 4H8-G8) were determined to interfere with TNF-α shedding and further expanded (Example 6).
The purified antibody subclone 4H8-E3 was determined to be of mouse IgM isotype (Examples 7-8; Figure 3). Antibody 4H8-E3 binds to an epitope localized within amino acids 431 to 459 of the extracellular juxtamembrane domain of human iRhom2 (Example 9; Figure 4) and does not bind to related family member human iRhom1 (Example 10; Figure 5). Purified antibody 4H8-E3 was determined to inhibit LPS-induced release of TNF-α from THP-1 cells by 62.6% (Example 11; Figure 6).
The antibody 4H8-E3 clone comprises VH and VL CDRs comprising SEQ ID NO: 34-36, respectively, and SEQ ID NO: 41-43, respectively (as determined with the Paratome CDR Identification tool, which is no longer publicly available), or VH and VL CDRs comprising SEQ ID NO: 37-39, respectively, and SEQ ID NO: 44-46, respectively (as determined with in-house methods), and VH and VL sequences comprising the amino acid sequences of SEQ ID NO: 33 and 40, respectively (pages 15 and 42).
The structures (i.e., amino acid sequences) and epitopes of the remaining antibody subclones (i.e., 4H8-D4 and 4H8-G8) described in the working examples are not disclosed.
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. Although three antibody subclones of the 4H8 hybridoma have been recited in the disclosure, only one subclone (4H8-E3, a murine IgM antibody) is described with sufficient particularity such that the skilled artisan could recognize its structure and how this structure correlates with its functional properties of binding to a specific epitope within residues 431-459 of the extracellular juxtamembrane domain of human iRhom2 and interfering with TNF-α shedding. Additional antibody clones that bind to the same epitope as antibody subclone 4H8-E3 are not described in the disclosure.
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 illustrated by the state of the art, the CDR structures in the VH and VL of conventional antibodies are a critical determinant of functional antigen-binding properties. As recited above, the structure of only one antibody subclone, 4H8-E3, has been described in the disclosure with sufficient detail to satisfy the written description requirement. The disclosure does not provide guidance with respect to which residue(s) within any of the six CDRs of the antibody subclone may be modified while still retaining the claimed functional properties. As such, further testing would be required for the skilled artisan to be able to determine which residues may be substituted while retaining specific binding for the claimed epitopes.
Conclusion. For all of the reasons presented above, one of skill in the art would not know which of the countless other anti-human iRhom2 antibodies encompassed by the highly general structural requirements of the claims would also possess the required functional activity of binding specifically to the juxtamembrane domain adjacent to the transmembrane domain 1 (TMD1) of human iRhom2. Given the lack of shared structural properties that provide the claimed binding activity, the limited number of species described, and the fact that the species that were described cannot be considered representative of the broad genus, the Applicant did not possess the full genus of anti-human iRhom2 antibodies that specifically bind to the juxtamembrane domain adjacent to the transmembrane domain 1 as broadly claimed at the time the application was filed.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 30-32 and 45-46 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4-8, and 21-22 of co-pending Application No. 17/764,819 (reference application ‘819; cited in PTO-892 mailed January 28, 2025). Although the claims at issue are not identical, they are not patentably distinct from each other because the co-pending claims anticipate the instantly claimed invention. This is a new rejection necessitated by Applicant’s claim amendments.
Regarding claims 30-32 and 45-46, co-pending claims 1, 4, and 6-7 recite a means for binding to human iRhom2, comprising a protein binder, that binds at least within a region of Loop 1 thereof of human iRhom2, inhibits and/or reduces TACE/ADAM17 activity when bound to human iRhom2, and reduces or inhibits induced TNF-α shedding. The human iRhom2 comprising the amino acid sequence set forth in SEQ ID NO: 181 in co-pending claim 7 shares 100% sequence identity to the amino acid sequence of human iRhom2 set forth in instant SEQ ID NO: 16 in claim 32. Co-pending claim 8 recites that the means for binding to human iRhom2 is a monoclonal antibody. Co-pending claims 21-22 recite a method for treating or preventing an inflammatory condition that comprises administering to a human subject the means for binding to human iRhom2 of the co-pending invention. Co-pending claim 5 recites that the inhibition or reduction of TACE/ADAM17 activity is caused by interference with iRhom2-mediated TACE/ADAM17 activation.
As evidenced by the instant specification, the residues spanning positions 431-459 of human iRhom2 correspond to the juxtamembrane domain section of the large extracellular loop 1 of human iRhom2, adjacent to TMD1 (page 3; Figure 8), relevant to claim 32. Thus, the epitope recited in the instant claims is within the scope of “within a region of Loop 1” of human iRhom2 recited in the co-pending claims.
This is a provisional nonstatutory double patenting rejection.
Claims 30 and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4-8, and 21-22 of co-pending Application No. 17/764,819 (reference application ‘819; supra) as applied to claims 30-32 and 45-46 above, further in view of Issuree (US 2015/0241429 A1; cited in PTO-892 mailed January 28, 2025). This is a new rejection necessitated by Applicant's claim amendments.
The teachings of the ‘819 reference application recited in the provisional non-statutory double patenting rejection above. However, the co-pending reference application does not teach that the anti-iRhom2 antibody is an IgG antibody or a humanized antibody, or that the fragment thereof is an scFv, Fab, or (Fab)2.
lssuree discloses methods for treating a subject with a Complement-mediated disease (e.g., rheumatoid arthritis, an inflammatory joint disease) by modulating the interaction between iRhom2 and TACE and/or inhibiting the biological activity of iRhom2 (e.g., ¶ 0005, 0007). lssuree additionally teaches a method of identifying an agent for the treatment of a Complement-mediated disease, comprising assessing the quantity of TNF-α release under suitable conditions, wherein diminished TNF-α release in the presence of the test agent indicates that the test agent is useful for treating the Complement-mediated disease (e.g., ¶ 0011). lssuree teaches a method for treating a subject with a complement-mediated disease that comprises administering an effective amount of a composition comprising an antibody or antigen-binding fragment thereof that binds to the extracellular loop of human iRhom2 (e.g., NP 078875.4, which corresponds to instant SEQ ID NO: 16; see page 40 of Applicant's disclosure), decreases the biological activity of iRhom2 and modulates formation of a complex between iRhom2 and TACE (e.g., ¶ 0006-0007; 0027; 0036-0037; 0058; 0060-0061).
Relevant to claims 34-36, the antibody may be monoclonal, lgG, chimeric or humanized; and the antibody fragment may be a Fab or (Fab)2 fragment (e.g., ¶ 0052).
It would have been obvious to one of ordinary skill in the art, before the filing date of the instantly claimed invention, to possess a humanized anti-iRhom2 antibody having an IgG isotype or an antigen-binding fragment thereof that is an scFv, Fab, or (Fab)2. The skilled artisan would have been able to do so by using known methods in the art to achieve a predictable result, as generating humanized and/or IgG antibodies is known and routine in the art. There would have been a reasonable expectation of success because humanized and IgG anti-iRhom2 antibodies have been disclosed previously.
This is a provisional nonstatutory double patenting rejection.
Claims 30-32, 34-36, and 45-46 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4-11, and 13-16 of co-pending Application No. 18/284,782 (reference application ‘782; cited in PTO-892 mailed January 28, 2025). Although the claims at issue are not identical, they are not patentably distinct from each other because the co-pending claims anticipate the instantly claimed invention. This is a new rejection necessitated by Applicant's claim amendments.
Regarding claims 30-32 and 45-46, co-pending claims 1, 5-6, and 16 recite a method for treating or preventing an inflammatory condition, comprising administering to a human subject an effective amount of a means for binding, comprising a protein binder, that binds at least within a region of Loop 1 of human iRhom2 (SEQ ID NO: 181, which shares 100% identity to instant SEQ ID NO: 16). Said means for binding inhibits or reduces TACE/ADAM17 activity and inhibits or reduces TNF-α shedding. Co-pending claim 4 recites that the inhibition or reduction of TACE/ADAM17 activity is caused by interference with iRhom2-mediated TACE/ADAM17 activation. Co-pending claims 7-8 recite that the means for binding is a monoclonal antibody or target-binding fragment thereof, and that the antibody is selected from IgG, scFv, Fab, or (Fab)2, relevant to claims 34-35. Co-pending claims 13-15 further recite methods comprising administering an effective amount of a means for binding to human iRhom2 to a human subject for reducing or inhibiting TACE/ADAM17 activity.
Co-pending claims 10-11 recite that the means for binding iRhom2 is an antibody comprising a combination of heavy chain and light chain CDRs and/or a combination of a heavy chain variable region (VH) and a light chain variable region (VL). As evidenced by the Examples of the co-pending disclosure, said antibodies were generated in mice and are therefore murine and/or humanized antibodies, anticipating claim 36.
As evidenced by the instant specification, the residues spanning positions 431-459 of human iRhom2 correspond to the juxtamembrane domain section of the large extracellular loop 1 of human iRhom2, adjacent to TMD1 (page 3; Figure 8), relevant to claim 32. Thus, the epitope recited in the instant claims is within the scope of “within a region of Loop 1” of human iRhom2 recited in the co-pending claims.
This is a provisional nonstatutory double patenting rejection.
Allowable Subject Matter
Claims 37-39 and 44 are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
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.
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/ELIZABETH A SHUPE/Examiner, Art Unit 1643
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643