DETAILED ACTION
Election/Restrictions
Applicant's election with traverse of Group I in the reply filed on 1/26/2026 is acknowledged. The traversal is on the ground(s) that the amended claims to recite a combination of a T-cell expressing MICA/B-CAR and an anti-CD38 antibody is not taught by Sentman and therefore do not share a technical feature. These arguments have been carefully considered but not found to be persuasive. In view of the amendments to Claim 1, Sentman in view of Cheney (WO2014/140904, teachings set for below) provide motivation to combine an anti-CD38 antibody such as daratumumab to the T-cell expressing MICA/B-CAR taught by Sentman. Therefore, the restriction requirement is maintained and made final. Applicant’s further elect the following species: “an iPSC-derived T cell comprising a MICA/B-CAR, an exogenous CD16, a TCR knockout, a CD38 knockout, and a CD58 knockout”, “CD16 comprising F176V and S197P in the ectodomain thereof” and “IL2”. Applicant’s arguments regarding the election of species is moot in view of the lack of unity maintained.
Claims 22, 25, 33-35 and 42 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 1/26/2026.
Claims 1-16, 18-20 and newly added claims 36-41 will be examined on the merits.
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA . An action on the merits follows.
Claim Interpretation
Applicant’s claims have been interpreted according to their broadest reasonable interpretation. With this in mind, the following comments are made. Many of the claims recite numerous limitations which are all in the alternative. Furthermore some of the dependent claims further limit a specific limitation referred to in the alternative and therefore is not required. For example, Claim 5 refers to the composition of claim 3 “wherein the exogenous CD16”, however part (ii) recited in Claim 3 is recited in the alternative and therefore is not a required limitation, rendering the limitations of Claim 5 not required as well. This analysis has been used in determining the scope of invention encompassed by each of the claims 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 2 is 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 written description rejection.
The claims are drawn to a composition comprising a MICA/B-CAR defined either by function (binding to the cell surface; binding to the conserved a3 domain, etc) or by heavy chain variable region or light chain variable region with percent identity less than 100%. This reads on alterations within the CDR regions which affect antigen binding.
The 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).
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 was 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. E.g., Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (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 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.
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 CDR sequences of one antibody do not predict the CDR sequence/structure of any and all other binding variant antibodies yet to be discovered. The instant application does not provide adequate written description for any and all MICA/B antibodies that function as claimed yet to be discovered, even those that bind known epitopes. Furthermore, although screening applications are well known in the art to identify MICA/B binding antibodies, screening is only a wish or plan for the future invention of undiscovered, unknown antibodies (the court found in (Rochester v. Searle, 358 F.3d 916, Fed Cir., 2004) that screening assays are not sufficient to provide adequate written description for an invention because they are merely a wish or plan for obtaining the claimed chemical invention). Based on the disclosed antibody sequences, one could not readily envision or predict the CDR sequences of any and all other future, undiscovered MICA/B targeting antibodies that can function as claimed. A definition by function does not suffice to define the genus because it is only an indication of what the antibody does, rather than what it is. A description of a genus of antibodies may be achieved by means of a recitation of a representative number of antibodies, defined by sequence, falling within the scope of the genus or of a recitation of structural features common to the members of the genus, which features constitute a substantial portion of the genus. The written description requirement can be met by showing that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics ....i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. The court found that if the disclosed species only abide in a corner of the genus, one has not described the genus sufficiently to show that the inventor invented, or had possession of, the genus. He only described a portion of it. The specifically defined antibody sequences claimed or disclosed in the specification are not representative of nor predictive of any and all other antibody sequences for the broadly claimed genus. Applicants are directed to the recent and relevant decision in AbbVie Deutschland GmbH v. Janssen Biotech, Inc. (Fed. Cir. 2014). The court found that if the disclosed species only abide in a corner of the genus, one has not described the genus sufficiently to show that the inventor invented, or had possession of, the genus. He only described a portion of it. Therefore, claims which do not define the antibodies with 100% identity to specific variable or CDR sequences or do not defined all 6 CDR regions or both VH and VL in one claim, are rejected for not adequately providing written description for the entire genus instantly claimed. Furthermore, it is also well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al. (Proc Natl Acad Sci USA 1982 Vol 79 page 1979). Rudikoff et al. teach that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function. MacCallum et al. J. Mol. Biol. (1996) 262, 732-745, analyzed many different antibodies for interactions with antigen and state that although CDR3 of the heavy and light chain dominate, a number of residues outside the standard CDR definitions make antigen contacts (see page 733, right col) and non-contacting residues within the CDRs coincide with residues as important in defining canonical backbone conformations (see page 735, left col.). Pascalis et al. (The Journal of Immunology (2002) 169, 3076-3084) demonstrate that grafting of the CDRs into a human framework was performed by grafting CDR residues and maintaining framework residues that were deemed essential for preserving the structural integrity of the antigen binding site (see page 3079, right col.). Although abbreviated CDR residues were used in the constructs, some residues in all 6 CDRs were used for the constructs (see page 3080, left col.). The fact that not just one CDR is essential for antigen binding or maintaining the conformation of the antigen binding site, is underscored by Casset et al. (BBRC 2003, 307:198-205), which constructed a peptide mimetic of an anti-CD4 monoclonal antibody binding site by rational design and the peptide was designed with 27 residues formed by residues from 5 CDRs (see entire document). Casset et al. also states that although CDR H3 is at the center of most if not all antigen interactions, clearly other CDRs play an important role in the recognition process (page 199, left col.) and this is demonstrated in this work by using all CDRs except L2 and additionally using a framework residue located just before the H3 (see page 202, left col.). Vajdos et al. (J. Mol. Biol. (2002) 320, 415-428), additionally state that antigen binding is primarily mediated by the CDRs more highly conserved framework segments which connect the CDRs are mainly involved in supporting the CDR loop conformations and in some cases framework residues also contact antigen (page 416, left col.). Chen et al. (J. Mol. Bio. (1999) 293, 865-881) describe high affinity variant antibodies binding to VEGF wherein the results show that the antigen binding site is almost entirely composed of residues from heavy chain CDRs, CDR-H1, H2, H3 (page 866). Wu et al. (J. Mol. Biol. (1999) 294, 151-162) state that it is difficult to predict which framework residues serve a critical role in maintaining affinity and specificity due in part to the large conformational change in antibodies that accompany antigen binding (page 152 left col.) but certain residues have been identified as important for maintaining conformation. Padlan et al. (PNAS 1989, 86:5938-5942) described the crystal structure of an antibody-lysozyme complex where all 6 CDRs contribute at least one residue to binding and one residue in the framework is also in contact with antigen. Lastly, Lamminmaki et al. (JBC 2001, 276:36687-36694) describe the crystal structure of an anti-estradiol antibody in complex with estradiol where, although CDR3 of VH plays a prominent roll, all CDRs in the light chain make direct contact with antigen (even CDR2 of VL, which is rarely directly involved in hapten binding).
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 MICA/B binding members. 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. 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 of variant antibodies, Applicant was not in possession of the invention as claimed. Applicant is invited to amend the claims to recite 100% identity to both the VH and VL paired.
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.
Claims 1-16, 18-20, 36-41 are rejected under 35 U.S.C. 103 as being unpatentable over Valamehr et al. (US Patent Application Publication 2018/0155717, June 7, 2018) in view of Sentman et al. (U.S. Patent Application Publication 2018/0085400, March 29, 2018), Cheney (WO2014/140904 A2), Ferrari de Andrade et al. (WO2018/217688) and Wang et al. (Clin. Cancer Res., Vol. 24(16), 4006-4017, 2018) all references cited on IDS filed 1/26/2022.
Valamehr et al. teaches methods of genome engineering iPSCs, including human iPSCs to comprise one or more genetic modifications at selected genomic sites, where the genetic modifications include the introduction of one or more exogenous polynucleotide of interest operably linked to promoter (Valamehr et al., paragraph 5-11). In particular, Valamehr et al. teaches iPSCs whose genome comprises an exogenous polynucleotide encoding at least one chimeric antigen receptor (CAR) which has been inserted into the constant region of the TCR TRAC locus and wherein the endogenous TCR locus is knocked out (Valamehr et al., paragraphs 22, 331-336, and claims 24-27). Valamehr et al. teaches that the CAR expressing iPSCs can contain further genomic modifications including deletion of genes or insertion of genes in order to increase resistance to immune detection and improve immune effector ability (Valamehr et al., paragraphs 28, 223-224, 323, 330-331). Valamehr et al. also teaches pharmaceutical compositions comprising the genome modified iPSCs or their NK cell derivatives for use in adoptive cell therapy of autoimmune disorders, hematological malignancies such as leukemias, solid tumors, or virus infection (Valamehr et al., paragraphs 44-45, and 226-227). In addition, Valamehr et al. teaches that the one or more exogenous gene(s) can be introduced into a safe harbor locus such as the AAVS1, CCR5, ROSA26, collagen, HTRP, H11, B2M GADPH, TCR, or RUNX1 loci (Valamehr et al., paragraph 8). Valamehr et al. further teaches differentiating the CAR-iPSCs into various hematopoietic cell types including CD34+ hematopoietic cells and effector cells such as NK cells and T cells (Valamehr et al., paragraphs 192 and 336).
While Valamehr et al. teaches to genetically modify iPSCs to express a CAR, Valamehr et al. does not teach that the CAR is an anti-MICA/B CAR or the specific components of the anti-MICA/B CAR. Sentman et al. supplements Valamehr et al. by teaching CAR whose extracellular binding domain is an scFV are derived from an anti-MICA or anti-MICB antibody, or from an antibody that binds both MICA and MICB, i.e. MICA/B (Sentman et al., paragraphs 6-9, 20-21, and 48). Sentman et al. further teaches cells expressing the anti-MIC CAR and the treatment of various diseases including cancer comprising administering the cells expressing the anti-MICA/B CAR in combination with a second therapeutic agent, such as a cytotoxic agent, an anti-angiogenic agent, or a CHOP chemotherapeutic regimen (Sentman et al., paragraphs 179-180). In particular, Sentman teaches MICA/B CAR where the structure of the CAR comprises an anti-MICA/B scFV, a hinge, a transmembrane domain, and one or more intracellular domains, where the hinge and transmembrane domains are CD28 hinge and transmembrane domain sequences, and the intracellular domains include the CD3 zeta intracellular signaling domain and the CD28 cytoplasmic domain (Sentman et al., paragraph 7, 51, 135, 154-155, 182, and 201). Sentman et al. also clearly teaches the use of a pharmaceutical composition comprising recombinant T cells comprising nucleic acid encoding a recombinant MICA CAR comprising an anti-MICA scFv fused to the hinge, transmembrane and intracellular domains of CD28 and the intracellular domain of CD3 zeta for the treatment of disease (Sentman et al., paragraph 182). Sentman et al. also specifically teaches to generate anti-MICA/B scFV, which comprise in the amino to carboxy direction an anti-MICA/B heavy chain variable region- a linker- and the anti-MICA/B light chain variable region (HV-LV), for use in the construction of an anti-MICA/B CAR (Sentman et al., Figures 1A-1D, and paragraph 75-84). Cheney et al. further supplements Valamehr et al., Sentman et al., and Green et al. by teaching anti-MICA/B antibodies which binds to the alpha-3 domain of MICA/B, including scFV antibodies (Cheney et al., paragraphs 9, 18, 77, and 242). Cheney et al. teaches that the antibodies are useful for treating various diseases include cancer (Cheney et al., paragraphs 21-23). Cheney et al. also teaches that the anti-MICA/B antibody can be combined with other therapeutic agents including daratumumab (Cheney et al., paragraph 298). While both Sentman et al. and Cheney et al. teaches anti-MICA/B antibodies, and in the case of Cheney et al. anti-MICA/B antibodies which bind to the alpha-3 domain of MICA/B, neither reference teaches an anti-MICA/B antibody with the specific light and heavy chain CDR 1, 2, and 3 sequences recited in the instant claims. Ferrari de Andrade et al. supplements Valamehr et al., Sentman et al., and Cheney et al. by teaching an anti-MICA/B antibody, 7C6, which has a light chain sequence, SEQ ID NO:7, which is identical to instant SEQ ID NO:33, and a heavy chain sequence, SEQ ID NO:8, which is identical to instant SEQ ID NO:34 ( Ferrari de Andrade et al., SEQ ID NOS 7 and 8, see also Fig. 21 which has the CDR 1, 2, and 3 sequences highlighted). Ferrari de Andrade et al. teaches that the 7C6 antibody binds to MICA/B and specifically the alpha-3 domain, prevents MICA/B shedding from human cancer cells, stabilizes MICA/B on the surface of cancer cells, and can be used as a cancer therapeutic, alone or in combination with other therapeutic molecules such as an anti-PD-1 or anti-CTLA4 antibody, or a chemotherapeutic agent (Ferrari de Andrade et al., pages 2, 4, 79-80, and 84-85). Ferrari de Andrade et al. further teaches the 7C6 which is an scFv (Ferrari de Andrade et al., page 4).
Thus, in view of the specific teachings of Valamehr et al. to make and use genetically modified iPSCs encoding a CAR for treating cancer, the teachings and motivation provided by Sentman et al. to make and use genetically modified cells expressing CAR comprising an anti-MICA and/or MICB scFV, where the CAR comprising the MICA/B scFv-a CD28 hinge-a CD28 transmembrane domain-a CD28 intracellular domain-and a CD3 zeta intracellular domain, and the further teachings of Cheney et al. and Ferrari de Andrade et al. for anti-cancer therapeutic scFV which recognize the alpha-3 domain of MICA and/or MICAB, specifically the 7C6 antibody taught by Ferrari de Andrade et al., it would have been prima facie obvious to the skilled artisan at the time of filing to make and use a genetically modified iPSC or derivative NK cell according to Valamehr et al. whose genome has been modified to include an inserted sequence encoding a CAR comprising an scFV specific for the alpha3 domain of MICA/B and comprising SEQ ID NOS: 33 and 34 in an HV-LV orientation, and both a CD28 and CD3zeta intracellular domains with a reasonable expectation of success.
In regards to deletion of CD38 in the iPSCs or derivative NK cells, while Valamehr et al., Sentman et al., and Cheney et al. do not specifically teach to make iPSCs or use iPSCs in methods of making derivative cells such as NK cells where the iPSCs express a CAR specific for anti-MICA/B as claimed and further comprise a deletion of CD38, Valamehr et al. does teach that the genetically modified CAR iPSCs useful for generating derivative cells such as NK cells can include one or more additional genetic modifications, including deletions of genes, in order to increase resistance to immune detection and improve immune effector ability (Valamehr et al., paragraphs 28, 223-224, 323, 330-331). Cheney et al., as noted above, further teaches the therapeutic combination of an anti-MICA/B therapy and a chemotherapeutic such as daratumumab. Wang et al. supplements Valamehr et al., Sentman et al., Cheney et al., and Ferrari de Andrade et al. by teaching that treatment of multiple myeloma with daratumumab, an anti-CD38 antibody, has the unwelcome side effect of killing NK cells, including adoptively transferred NK cells (Wang et al., 4006). Wang et al., however, teaches that adoptive transfer of CD38-/low NK cells prevents their “fratricide” by daratumumab induced ADCC (Wang et al., pages 4006 and 4010-4012). Wang et al. also demonstrates that CD38 -/low NK cells exhibited increased cytotoxicity against multiple myeloma cells (Wang et al., page 4012). Therefore in view of daratumumab “fratricide” of CD38+ NK cells and the further increased cytotoxicity of CD38 negative NK on multiple myeloma, and the detailed teachings of Valamehr et al. for deleting genes in iPSCs in order to improve immune effector activity, it would have been prima facie obvious to the skilled artisan at the time of filing to further genetically modified the anti-MICA/B CAR expressing iPSCs or derivative NK cells taught by Valamehr et al. in view of Sentman et al., Green et al., Cheney et al., and Ferrari de Andrade et al. to delete CD38 in order to produce derivative CD38 negative NK cells or an iPSC cell capable of generating CD38 negative NK cells with increased therapeutic potential in combination with daratumumab with a reasonable expectation of success.
Conclusion
Claims 1-16, 18-20, 36-41 are rejected.
No Claim is allowed.
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/Meera Natarajan/Primary Examiner, Art Unit 1643
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