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
1. 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 July 17, 2026 has been entered.
2. Claims 13-17 have been amended. Claims 13-32 are pending and under consideration.
Claim Objections
3. Claim 14 is objected to because of the following informalities: the word “or” should be inserted between “a minibody,” and “a diabody”.
Claim 26 is objected to because of the following informalities: on the last line of Applicant’s p. 11 (B CC) should be (BCC).
Appropriate correction is required.
New 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.
4. Claims 23, 24, 26, 28, 30, 31 and 32 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 23 recites the limitation "a chimeric or recombinant antibody . . . of claim 13". There is insufficient antecedent basis for this limitation in the claim because claim 13 does not recite a chimeric or recombinant antibody. Claim 24 incorporates by reference the limitations of claim 23 and thus is also rejected.
Claim 24 recites the limitation "the . . . dimeric antigen binding protein cell" in line 5. There is insufficient antecedent basis for this limitation in the claim because the antecedent portion of the claim does not recite a “dimeric antigen binding protein cell’.
Claim 26 recites “and/or” on line 3 prior to the wherein clauses. The “and/or” limitation makes it unclear whether the claim is limited by the wherein clauses, which are recited in the alternative, or not. Thus claim 26 is indefinite.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c).
In the present instance, claim 26 recites the broad recitation of a lymphocyte, and the claim also recites B-cell or B lymphocyte, T-cell or T lymphocyte, and more specific forms thereof, which are the narrower statement of the range/limitation. Claim 26 also recites the broad recitation B cell lymphoma and the claim also recites Hodgin’s or non-Hodkin’s lymphoma, and more specific forms thereof, which are the narrower statement of the range/limitation.
Claims 28 and 30 also recite the broad recitation B cell lymphoma and the claims also recites Hodgin’s or non-Hodkin’s lymphoma, and more specific forms thereof, which are the narrower statement of the range/limitation.
The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Claim 28 recites “and/or” on line 3 prior to the wherein clauses. The “and/or” limitation makes it unclear whether the claim is limited by the wherein clauses, which are recited in the alternative, or not. Thus claim 28 is indefinite.
Claim 31 recites the limitation "a chimeric or recombinant antibody of claim 13". There is insufficient antecedent basis for this limitation in the claim because claim 13 does not recite a chimeric or recombinant antibody. Claim 32 incorporates by reference the limitations of claim 31 and thus is also rejected.
Maintained 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.
5. Claims 20-32 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 essentially for the reasons of record.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 759 F.3d 1285, 111 USPQ2d 1780 (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. “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).
Scope of the claimed genus
The claims are drawn broadly drawn to an isolated or purified antibody (Ab), or antigen (Ag) binding fragment thereof, or monomeric or dimeric antigen binding protein (ABP), capable of specifically binding a human B-cell maturation antigen (BCMA) polypeptide (also called tumor necrosis factor receptor superfamily member 17 (TNFRSF17)), wherein the isolated or purified Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP comprises the VH and VL of SEQ ID NOs: 1-6, the CDR regions thereof, and variants thereof comprising one or more of the disclosed VH and VL and variants thereof. Thus, the claims are broadly drawn to a large genus of an isolated or purified Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP, capable of specifically binding a human BCMA.
State of the Relevant Art
As was well-known in the antibody art, antibodies as a class share an overall structure generally comprising two heavy chain polypeptides that each comprises a heavy chain variable region (VH) and a heavy chain constant region made up of several domain (CH1, hinge, CH2, CH3, and for some antibodies, a CH4). Each of the heavy chains pairs with a light chain polypeptide that comprises a light chain variable region (VL) and a constant region. But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure each antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level. By the time the invention was made, it is well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. See Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (of record, see Section 3) “Antibody Structure and the Antigen Binding Site” and Figure 1). Chimeric antibodies comprise the heavy and light chain variable regions of a rodent antibody linked to human constant regions and preserve the entirety of the VH and VL of the parent antibody. Id. at 1619-20. Humanized antibodies comprise only the CDRs, or in some cases an abbreviated subset of residues within the CDRs, of a parental rodent antibody in the context of human framework sequences. Id. at Section 4. All of the CDRs of the heavy and light chain, in their proper order of CDR1, then 2, then 3, and in the context of framework sequences which maintain their required conformation are generally required to produce a humanized antibody in which the heavy and light chains associate to form an antigen-binding region that binds the same antigen as the parental rodent antibody. Id. at Section 4. Almagro provides a detailed discussion regarding various methods of humanization, including rationale design approaches and empirical approaches based on random screening. Almagro, Sections 4 and 5.
Overall, at the time the invention was made, the level of skill for preparing antibodies and then selecting those antibodies with desired functional properties was high. However, even if a selection procedure was, at the time of the invention, sufficient to enable the skilled artisan to identify antibodies with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011) (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”) Absent the conserved structure provided by all six CDRs of a parental antibody in the context of appropriate VH and VL framework sequences, the skilled artisan generally would not be able to visualize or otherwise predict, a priori, what an antibody with a particular set of functional properties would look like structurally.
Summary of Species disclosed in the original specification
The specification teaches the monoclonal antibodies 9H5, 10A2, and 5C1 which comprise the VH and VL of SEQ ID NOs: 1-6 and bind BCMA. See BCMA antibody clone development- pp. 34-42.
Are the disclosed species representative of the claimed genus?
MPEP § 2163 states that a “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
The specification discloses the reduction to practice of monoclonal antibodies 9H5, 10A2, and 5C1 which comprise the VH and VL of SEQ ID NOs: 1-6 and bind human BCMA. The specification does not actually produce any other antibodies that bind BCMA or make any other forms of the monoclonal antibodies 9H5, 10A2, and 5C1, such as a single domain antibody or other antibodies or ABP that contain a plurality of CDR fragments. Antibodies produced by different methods, such as in different species or in phage, would have been generally expected to be highly structurally diverse, particularly in the CDR sequences. Thus, while applicant has described three species, the genus of antibodies very large and there is only three described species for the genus. The described species therefore cannot be considered representative of the genus an isolated or purified Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP, capable of specifically binding a human BCMA. E.g., AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014).
Identifying characteristics and structure/function correlation
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. To meet this requirement in the instant case, the specification must describe structural features that convey the claimed binding activity, a prerequisite for utility in the recited methods of treating.
As noted above, the art generally accepted that the combination of the CDRs within the VH and VL pair of an antibody were essential for binding specificity. But the specification does not describe what residues within the CDRs confer the binding activity claimed. Accordingly, the skilled artisan would not be able to discern a structure/function correlation for antibodies other than those comprising either all six CDRs (in the context of VH and VL regions) of one parental antibody, or the VH and VL of one parental antibody.
For all of the reasons presented above, one of skill in the art would not know which of the countless other antibodies encompassed by the independent claims that meet the highly general structural requirements of the claims would also be able to specifically bind to human BCMA. Neither the specification nor the dependent claims provide sufficient additional structure or a structure/function correlation to provide an adequate written description of the genera claimed. Therefore, the skilled artisan would not reasonably conclude that the inventors, at the time the application was filed, had full possession of an isolated or purified Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP, capable of specifically binding a human BCMA as broadly claimed. 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, Applicant was not in possession of the invention as claimed.
Response to Arguments
6. Applicant argues that claim 13 has been amended to overcome the above rejection.
Applicant’s argument has been considered and has been found partially persuasive The rejection of claims 13-16 is withdrawn. However, claims 20-32 are not fully limited to the antibodies of claim 13 and the rejection of those claims is maintained.
Claim 20 recites “a nucleic acid sequence encoding an Ab, or Ag binding fragment thereof,” in the alternative, which is not limited to an Ab, or Ag binding fragment of claim 13. Amendment of claim 20 to “a nucleic acid sequence encoding an Ab, or Ag binding fragment thereof, of claim 13” would help to obviate the rejection.
Claim 23 recites “a chimeric or recombinant antibody” in the alternative, which is not limited to an Ab, or Ag binding fragment of claim 13. Amendment of claim 23 to “A cell comprising the Ab, or Ag binding fragment thereof, of claim 13, or monomeric or dimeric ABP of claim 13” would help to obviate the rejection.
Regarding claim 24, the second wherein clause of claim 24 is not limited to an Ab, or Ag binding fragment of claim 13. Amendment of the wherein clause to “wherein the cell expresses or secretes the Ab or Ag binding fragment thereof of claim 13, or monomeric or dimeric ABP of claim 13 extracellularly or into the extracellular milieu, or at least the Ab or Ag binding fragment thereof of claim 13, or monomeric or dimeric ABP of claim 13 is expressed or displayed extracellularly or into the extracellular milieu” would help to overcome the rejection.
Claim 25 recites “a first Ab, or Ag binding fragment thereof, ” in the alternative in part (a), which is not limited to an Ab, or Ag binding fragment of claim 13. Amendment of claim 25 to “a first Ab, or Ag binding fragment thereof, of claim 13” would help to overcome the rejection.
Claim 26 recites on lines 4-6, “wherein the first Ab and/or second Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP comprises a VH having an amino acid sequence comprising SEQ ID NO:1, 3, or 5 and/or a VL having an amino acid sequence comprising SEQ ID NO:2, 4, or 6;”, which includes undefined VH or VL domains. Amendment of the wherein clause to “wherein the first Ab and/or second Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP comprises a VH having an amino acid sequence comprising SEQ ID NO:1, 3, or 5 and a VL having an amino acid sequence comprising SEQ ID NO:2, 4, or 6;” would help to overcome the rejection.
Claim 27 recites in lines 4-5 “the specific binding of the first Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP” which in not limited to the antibodies of claim 13. Amendment of the claim to “the specific binding of the first Ab, or Ag binding fragment thereof, of claim 13 or monomeric or dimeric ABP of claim 13” would help to overcome the rejection.
Claim 32 recites “a kit comprising: a chimeric or recombinant antibody of claim 13.” which is not limited to an Ab, or Ag binding fragment, or ABP of claim 13. Amendment of claim 32 to “A kit comprising: the isolated or purified Ab, or Ag binding fragment thereof, of claim 13, or monomeric or dimeric ABP of claim 13.” would help to obviate the rejection.
Claim Rejections - 35 USC § 102
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.
7. Claim(s) 20 and 22-31 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by US 2020/0392236 A1 (Sather et al. Dec. 17, 2020,IDS), “Sather”.
It is noted that the antibodies of claims 20, 22, 23, 24, and 31 are not limited to an Ab, or Ag binding fragment, or ABP of claim 13.
It is noted that claim 25 recites “(a) contacting the cell, tissue or organ or portion of any of the foregoing with a first Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP of claim 13” lines 4-5. Thus, the claim is interpreted to encompass the alternative of contacting with any first Ab or any Ag binding fragment thereof, which are not limited to the Ab or Ag binding fragment thereof of claim 13.
Also, the first alternative steps of claims 26 (lines 1-3) and 28 (lines 1-2) are not limited to contacting with the Ab or Ag binding fragment thereof of claim 13 or ABP of claim 13 as the second Ab or Ag binding fragment.
Sather teaches antibodies to human BCMA. See abstract and ¶¶ 0006 and 0048.
Sather teaches nucleic acid expression vectors encoding the BCMA antibodies and CARs. See ¶¶ 0069, 0070 and 0071 and 0188-0191.
Sather teaches engineered T-cells comprising the BCMA CARs and host cells for producing the antibodies. See ¶¶ 0071-0074 and 0188-0194.
Sather teaches diagnosing cancer with the anti-BCMA antibodies using ELISA assays, which use two antibodies, by detecting BCMA in cells or tissues. See ¶¶ 0204, 0395, 0409-0411, and 0523-0531.
Sather teaches that a subject may be screened for the presence of a disease or disorder associated with elevated BCMA expression, such as a BCMA-expressing cancer or tumor like lymphoma (e.g. non-Hodgkin's lymphoma (NHL), Hodgkin's lymphoma) or leukemia. Sather teaches a subject who tests positive for a BCMA-associated disease or disorder may be selected for treatment by the present methods, and may be administered a therapeutically effective amount of a BCMA-binding molecule (e.g., anti-BCMA antibody or antigen-binding fragment thereof), recombinant receptor (e.g., CAR) comprising a BCMA-binding molecule, cells containing a recombinant receptor or a pharmaceutical composition thereof as described herein. See ¶¶ 0409-0412.
Sather teaches treating the cancer, like lymphoma (e.g. non-Hodgkin's lymphoma (NHL), Hodgkin's lymphoma) or leukemia, with the anti-BCMA antibodies. See ¶¶ 0074-0076, 0406, 0409-0411 and 0415 and claims 76, 77 and 85-88.
Sather teaches kits containing the provided binding molecules (e.g., antibodies), recombinant receptors (e.g., CARs), genetically engineered cells, and/or compositions comprising the same. See ¶¶ 0532-0534.
Response to Arguments
8. Applicant argues that claim 13, from which claims 25-30 depend, has been amended to overcome the above rejection.
Applicant’s arguments have been considered, but have not been found persuasive because Claim(s) 23-31 are not limited to the antibodies or antigen binding proteins of claim 13 as set forth above.
Claim Rejections - 35 USC § 103
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
9. Claim(s) 32 is rejected under 35 U.S.C. 103 as being unpatentable over 2020/0392236 A1 (Sather et al. Dec. 17, 2020,IDS), “Sather” as applied to claims 20 and 22-31 above, and further in view of US 2025/0130233 A1 (Carreira et al. Apr. 24, 2025, effectively filed Oct. 27, 2021), “Carreira”.
Sather teaches as set forth above.
Sather additionally teaches staining cells to the BCMA antibodies detect BCMA in pathology. See ¶¶ 0531 and 0559-0560.
Sather does not teach a kit comprising components needed for an immunohistochemistry (IHC) assay.
Carreira teaches immunohistochemical methods for detection of BCMA and kits for performing the IHC methods. See ¶¶ 0003-0024, 0026, 0102, and 0106-0124, Fig. 1 and claims 1-27.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Sather and Carreira and place the anti-human BCMA antibodies in a kit with reagents for IHC because Sather additionally teaches staining cells to the BCMA antibodies detect BCMA in pathology and Carreira teaches immunohistochemical methods for detection of BCMA and kits for performing the IHC methods. One would have been motivated to place the anti-human BCMA antibodies in a kit with reagents for IHC given the teachings of Sather and Carreira well-known uses of a kit for convenience of having all reagents together in a kit, sale of the reagents, and storge.
10. Claim(s) 21 is rejected under 35 U.S.C. 103 as being unpatentable over 2020/0392236 A1 (Sather et al. Dec. 17, 2020, IDS), “Sather” as applied to claims 20 and 22-31 above, and further in view of WO 00/50616 (Iatrou et al. Aug. 31, 2000), “Iatrou”.
Sather teaches as set forth above.
Sather additionally teaches using signal sequences in the nucleic acids encoding the BCMA antibodies and CARs, such as a GM-CSF signal sequence. See ¶¶ 0067-0069.
Sather does not teach that the signal sequence is at the amino terminus.
Iatrou teaches expression cassettes for secretion of heterologous proteins from cells. See Abstract and p. 1-Field of the Invention and claims 1-22.
Iatrou teaches that all secreted proteins possess a signal peptide at their N-terminus that directs the protein to the secretory pathway of eukaryotic cells or to the cytoplasmic membrane of prokaryotic cells. See p. 3-lines 11-14.
Iatrou teaches linking the GM-CSF signal peptide to the N-terminus of a heterologous protein to direct the secretion of the protein. See p. 11-lines 8-18.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Sather and Iatrou and insert a signal peptide at the N-terminus of the BCMA antibodies and CARs of Sather because Sather teaches using signal sequences in the nucleic acids encoding the BCMA antibodies and CARs, such as a GM-CSF signal sequence, and Iatrou teaches that all secreted proteins possess a signal peptide at their N-terminus and teaches linking the GM-CSF signal peptide to the N-terminus of a heterologous protein to direct the secretion of the protein. Given that signal peptide was known to be located at the N-terminus of a protein for proper functioning, one would have been motivated to a signal peptide at the N-terminus of the BCMA antibodies and CARs of Sather.
Conclusion
11. Claims 20-32 are rejected. Claims 14 and 26 are objected to. Claims 13 and 15-19 are allowable.
12. Any inquiry concerning this communication or earlier communications from the examiner should be directed to PETER J REDDIG whose telephone number is (571)272-9031. The examiner can normally be reached M-F 8:30-5:30 Eastern Time.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Greg Emch can be reached at 571-272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/PETER J REDDIG/Primary Examiner, Art Unit 1646
