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 .
Claim Status
Claims 1-15 have been cancelled and claims 16-35 have been newly added, as requested in the preliminary amendment filed on 03/14/2024. Following the amendment, claims 16-35 are pending in the instant application.
Claims 16-35 are under examination in the instant office action.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged.
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. Additionally, it is noted that the certified copy of the foreign priority document is in English, and as such the claim to foreign priority has been perfected.
Claims 16-35 have an effective filing date of September 16, 2021 corresponding to EP21306283.9.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 06/05/2024, 06/05/2024, and 11/13/2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Interpretation
With regard to the sequence language of the instant claims, the following are noted:
The recitation of, for example, “VH-CDR1 of sequence SEQ ID NO: 10” is being interpreted such that a reference sequence must comprise and/or consist of full-length SEQ ID NO: 10 in order to meet the limitation. This interpretation pertains to claims 16-17.
The recitation of, for example, “sharing at least 70% sequence identity with the framework regions of SEQ ID NO: 24” is being interpreted such that a reference sequence must comprise framework regions sharing 70% overall identity to the exact framework sequences of SEQ ID NO: 24 in order to meet the limitation. In other words, the combined sequences for FR1, FR2, FR3, and FR4 of a reference sequence must have 70% overall identity with the combined sequences of FR1, F2, FR3, and FR4 of SEQ ID NO: 24 in order to meet the limitation. This interpretation pertains to claim 17.
The recitation of, for example, “comprising an amino acid sequence sharing at least 70% sequence identity with the amino acid sequence of any one of SEQ ID NOs: 26 to 28” is being interpreted such that a reference sequence must have at least 70% sequence identity to one of full-length SEQ ID NOs: 26, 27, or 28 in order to meet the limitation. This interpretation pertains to claims 20 and 35.
Allowable Subject Matter
It is specifically noted that an antigen-binding domain specifically binding to CD45RC, wherein said antigen-binding domain comprises: (a) a heavy chain variable region (HCVR) which comprises the following three CDRs: (i) VH-CDR1 of sequence SEQ ID NO: 10; (ii) VH-CDR2 of sequence SEQ ID NO: 11; and (iii) VH-CDR3 of sequence SEQ ID NO: 12; and (b) a light chain variable region (LCVR) which comprises the following three CDRs: (i) VL-CDR1 of sequence SEQ ID NO: 13; (ii) VL-CDR2 of sequence SEQ ID NO: 14; and (iii) VL-CDR3 of sequence SEQ ID NO: 15, wherein X in SEQ ID NO: 13 is either absent or is selected from the group consisting of Asn (N), Ser (S) and Gly (G) has been thoroughly searched and is free of the prior art.
The closest prior art made of record but not relied upon is US 12,168,694 (herein after referred to as “Guillonneau”). Guillonneau teaches isolated anti-human CD45RC antibodies or binding fragments thereof, nucleic acids and expression vector encoding the same, compositions including the same, and uses thereof as medicaments, including for the treatment of CD45RChigh-related diseases (including autoimmune diseases, undesired immune responses, monogenic diseases, and lymphoma or cancer), in particular for use in preventing and/or treating graft-versus-host disease (GVHD) (Abstract). More specifically, Guillonneau claims methods of (i) inducing immune tolerance; (ii) preventing and/or reducing transplant rejections; (iii) reducing and/or treating CD45RChigh-related conditions; and (iv) preventing and/or treating GVHD (see claims 13-17). For example, Guillonneau discloses that in a preferred embodiment, the antibody or antigen binding fragment of the invention comprises a HCVR comprising or consisting of SEQ ID NO: 123 or a HCVR comprising or consisting of a sequence of the non-CDR regions sharing at least 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or more of identity with the sequence of the non-CDR regions of the SEQ ID NO: 123 (Column 76, lines 60-67; see SEQ ID NO: 123 at Column 77). It is specifically noted that Guillonneau SEQ ID NO: 123 comprises CDRs most closely related to those instantly claimed, and comprises an exact match to instant SEQ ID NO: 10 and instant SEQ ID NO: 12, but does not comprise an exact match to instant SEQ ID NO: 11. Guillonneau further discloses that in a preferred embodiment, the antibody or antigen binding fragment of the invention comprises a LCVR comprising or consisting of SEQ ID NO: 112 with X12 being selected from Asn (N), Ser (S) and Gly (G), or a LCVR comprising or consisting of a sequence of the non-CDR regions sharing at least 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or more of identity with the sequence of the non-CDR regions of the SEQ ID NO: 112 (Column 81, Lines 45-61). It is specifically noted that Guillonneau SEQ ID NO: 112, when X12 is Asn (N), Ser (S) and Gly (G), comprises CDRs most closely related to those instantly claimed, and comprises an exact match to instant SEQ ID NO: 13, when X is Asn (N), Ser (S) and Gly (G), respectively. Guillonneau SEQ ID NO: 112 also comprises an exact match to instant SEQ ID NO: 15, but does not comprise an exact match to instant SEQ ID NO: 14, nor instant SEQ ID NO: 13 wherein X is absent. Thus, Guillonneau does not teach or render obvious an antigen-binding domain specifically binding to CD45RC, wherein said antigen-binding domain comprises: (a) a heavy chain variable region (HCVR) which comprises the following three CDRs: (i) VH-CDR1 of sequence SEQ ID NO: 10; (ii) VH-CDR2 of sequence SEQ ID NO: 11; and (iii) VH-CDR3 of sequence SEQ ID NO: 12; and (b) a light chain variable region (LCVR) which comprises the following three CDRs: (i) VL-CDR1 of sequence SEQ ID NO: 13; (ii) VL-CDR2 of sequence SEQ ID NO: 14; and (iii) VL-CDR3 of sequence SEQ ID NO: 15, wherein X in SEQ ID NO: 13 is either absent or is selected from the group consisting of Asn (N), Ser (S) and Gly (G).
Claims 16-18, 24, 26-29, and 32-33 are allowed. However, as detailed below, claims 19-23, 25, 30-31, and 34-35 suffer from deficiencies under 35 USC § 112(a) and/or 112(b).
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 25 and 30-31 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for reducing and/or treating CD45RChigh-related diseases, disorders, or conditions does not reasonably provide enablement for treating . The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims. This is a SCOPE OF ENABLEMENT rejection.
The Breadth of the Claims
Claim 25 is drawn, generally, to a method of “treating a patient in need thereof, said method comprising administering to said [patient] the antigen-binding domain of claim 16…”. Claim 30 is drawn, generally, to a method of “preventing, reducing and/or treating CD45RChigh-related diseases, disorders, or conditions in a subject in need thereof, said method comprising administering to said subject the antigen binding domain of claim 16…”. It is specifically noted that, regarding claim 25 specifically, no specific definition of “a patient in need thereof” is provided, and as such the claim is drawn to treating any patient, the full scope of which is not enabled. Claims 30-31 are drawn to preventing CD45RChigh-related diseases, disorders, or conditions (including cancer), the full scope of which is not enabled.
The State of the Prior Art/Level of Predictability in the Art
It is specifically noted that, with regard to therapeutic efficacy of therapeutics utilizing antigen-binding domains (e.g., antibodies) it is well established in the art that there must be some correlation between the disease, disorder, or condition to be treated and the specific antigen that is being targeted by said antibody in order for treatment to be reasonably predictable.
For example, cancer treatment is highly unpredictable. Even though the EGFR was identified in some cancers as a drug target, the in vitro (i.e., in a test tube) effectiveness of a drug in inhibiting the EGFR turned out to be a poor proxy for how effective that drug actually was in treating cancer in vivo (i.e., in the body). Numerous EGFR inhibitors that showed promising in vitro activity failed for a variety of reasons. These included poor pharmacokinetics due to poor absorption or rapid metabolism ( [**2]or both), undesirable drug-drug interactions, drug toxicity due to drug binding onto healthy cells, drug toxicity due to binding onto other receptors, and metabolite toxicity. Some drug candidates were limited by one or more of these shortcomings, further underscoring the unpredictable nature of cancer treatment. OSI Pharmaceuticals , LLc, v. Apotex Inc, 939 F.3d 1375, 2019. The state of the art at the time of filing was such that the functionality of an anti-tumor antibody was dependent on both its action on the intended target and whether or not the modulation of said target had an effect on any particular cancer cell. Baxevanis (Expert Opinion: Drug Discovery, Vol. 3, No. 4, Pg. 441-452, 2008) teaches that, depending on the epitope against which an antibody is directed, antibody-antigen binding may neutralize circulating targets or cell surface receptors (Pg. 444, Column 1, Paragraph, first full). They teach that presently available monoclonal antibodies (mAbs) are directed against molecular targets that are expressed on tumor cells or play an important role in the tumor microenvironment (Pg. 444, Column 1, Paragraph, first full; Table 1). Table 1 lists currently available antibodies for use in clinical oncology and illustrates that each antibody has a specific target (Table 1, Column 2) and a specific set of cancers for which it has therapeutic utility (Table 1, Column 4). Taken together, the art does not recognize a single antibody that is an effective therapy against all tumors. To further illustrate this point, Baxevanis goes on to explain the functionality of the more commonly used therapeutic antibodies. Trastuzumab targets the receptor HER-2 (HER-2/neu) which is overexpressed in some breast cancers and so is a viable treatment for said breast cancers (Pg. 444, Column 2, Lines 19-24). The basis of this variability in treatment response is due to the fact that the growth inhibitory effect of anti-HER-2 is dependent on the extent of HER-2 overexpression (pg. 443, Column 1, Paragraph, first partial). Because only a portion of breast cancer patients overexpress HER-2 and respond to trastuzumab, the selection of suitable patients is important (Pg. 445, Column 1, Lines 13-15). Rituximab is an antibody against CD20 antigen, which is expressed on most B cells including B-cell lymphomas (Pg. 445, Column 1, Lines 36-38). Therefore, it is used to treat B-cell lymphomas (Pg. 444, Table 1). It has been used to treat patients with relapsed or refractory low-grade non-Hodgkin's lymphoma (a B-cell lymphoma) (Pg. 445, Column 1, Lines 41-50). In contrast to trastuzumab and rituximab, some therapeutic antibodies show efficacy in treating multiple cancers. This stems from the fact that their target antigen is associated with multiple cancers. Cetuximab is an anti-EGFR antibody (Pg. 445, Column 1, Lines 19-20). EGFR is overexpressed in many epithelial cell tumors (Pg. 445, Column 1, Lines 20-21). The association of EGFR overexpression with multiple cell types gives cetuximab a broader therapeutic applicability than trastuzumab (Pg. 444, Table 1) as it is used to treat both renal and head and neck cancers. As a final point, the art also recognizes that the function of the therapeutic antibody must correlate with an effect on its target conducive to tumor growth inhibition or tumor lysis, resulting in patient benefit. Anti-HER-2 antibodies, like Trastuzumab, disrupt HER-2 catalytic activity (Pg. 443, Column 1, Paragraph, first partial, Sentence, ultimate; Table 1, Column 3, (S) referring to decreased protein signaling (activity); and Pg. 444, Column 2, Lines 19-22). Cetuximab also inhibits its target’s activity as it prevents EGFR dimerization and subsequent activation via phosphorylation (Pg. 445, Column 1, Lines 23-25). Since both HER-2 and EGFR activity support growth of cancer cells in which they are overexpressed, their inhibition is therapeutic to patients. Rituximab causes tumor cell lysis by antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) (Pg. 445, Column 1, Lines 38-39) and so its therapeutic benefit is provided by specifically inducing cancer cell death. Thus, the teachings of Baxevanis underline the requirement of a link between an inhibitory antibody’s target and specific cancers to make therapy of said cancer predictable to one of ordinary skill in the art. The prior art is silent as to the use of an antibody against JAM-A for the treatment of any cancer.
Breedveld (The Lancet, 2000, 355, 735-740; herein after referred to as “Breedveld”) teaches that several obstacles to achieving efficacy have been identified for this therapeutic strategy which attempts to induce an unprecedented degree of targeting specificity while using large proteins whose sizes greatly exceed those of conventional drugs; mAb are large proteins and thereby have slower kinetics of distribution than small molecules and more limited tissue-penetration properties (Pages 735-736, Factors Regulating mAb-Based Targeted Therapies). The ability of mAb to penetrate cancers or sites of inflammation is low; particularly in the case of anti-tumour therapy in homogeneous tumours, antigen expression and blood supply limits uniform antibody delivery (Page 736, Colum 1, First Partial Paragraph). The efficacy of any particular mAb depends on several variables; these include the characteristics of the targeted antigen, its function, its cell-surface density and tissue distribution, as well as characteristics of the mAb including fine specificity, avidity, and isotype (Page 736, Column 1, Last Paragraph). The mechanism(s) by which mAb achieve therapeutic effects is often not completely known; potential mechanisms include: blocking or steric hindrance of the function of the target antigen; cytotoxicity to the cell expressing the target antigen, by complement activation or cellular mechanisms; and modulation of the function of the cell by binding to an antigen capable of transducing intracellular signals (Id.). Thus, Breedveld further indicates that the efficacy of therapeutic mAbs is highly dependent upon factors associated with the specific antigen that a given mAb targets.
Furthermore, reasonable guidance with respect to preventing any cancer, for example, relies on quantitative analysis from defined populations that have been successfully pre-screened and are predisposed to particular types of cancer. This type of data might be derived from widespread genetic analysis, cancer clusters, or family histories. The essential element towards the validation of a preventive therapeutic is the ability to test the drug on subjects monitored in advance of clinical cancer and link those results with subsequent histological confirmation of the presence or absence of disease. This irrefutable link between antecedent drug and subsequent knowledge of the prevention of the disease is the essence of a valid preventive agent. Further, a preventive administration also must assume that the therapeutic will be safe and tolerable for anyone susceptible to the disease. The vaccine art teaches that compositions comprising some tumor associated antigens are effective in treatment of cancer through generation of immunogenic response to the tumor antigen (see for example, Komenaka et. al., Clinics in Dermatology, 2004, Vol. 22, Pg. 251-265, specifically page 257). However, nowhere in the art does it show that tumor antigens are effective at preventing cancer. Evans et. al. (Q. J. Med 1999: 92: 299-307) teach that vaccines against cancer are not fully established, and it is stated that adjuvant therapy to prevent or delay disease still needs experimentation. Evans et. al. further state that such cancer vaccines are at best used as a therapeutic and not as a prophylactic and that “the notion that cancer vaccines will replace standard therapeutic strategies in malignant disease still belongs to the realm of fiction” (see page 303 last paragraph). In some cases, it is known that certain cancers arise from a single cause. This cause can be viral as in the case of cervical cancer, caused predominantly by persistent cervical infection with human papillomavirus (HPV) (Schiffman et. al., The New England Journal of Medicine, Vo. 353, No. 20, Pg. 2101-2104, 2005). Schiffman et. al. teach that primary prevention through vaccination against HPV might be possible in young women (Pg. 2101, Column 3, Paragraph, first partial). However, they also teach that vaccine evaluations are ongoing (Pg. 2103, Column 3, Paragraph, first full). In addition, the most promising vaccines designed against HPV types 16 and 18 would only prevent 70 percent of cervical cancer cases at best (Pg. 2103, Column 2, Paragraph, first full). Therefore, there is still no vaccine that can definitively prevent a cancer. Current evidence points only to the potential of future prophylactic agents. The art of small molecule chemotherapeutics teach that some molecules successful at treating cancers can also reduce risk. Cuzick et. al. (The Lancet, Vol. 361, Pg. 296-300, 2003) teach that tamoxifen can reduce the risk of ER-positive breast cancer but cannot be recommended as a preventive agent (Pg. 299, Column 2, Paragraph, first). The reason it cannot be recommended centers around the need for continued research into specific subgroups of high-risk but healthy women for whom the risk-benefit ratio is sufficiently positive to recommend prophylactic tamoxifen treatment (Pg. 299, Column 2, Paragraph, first). With respect to peptide-based cancer prevention agents, the art currently does not recognize a definitive example though promising candidates are present. Hernandez-Ledesma (Peptides, Vol. 30, Pg. 426-430, 2009) teaches that lunasin, a peptide discovered in soy has demonstrated cancer-preventative capacity in vitro and mouse models (Abstract). The authors define it as a perfect candidate to exert an in vivo cancer-preventive activity, but more research is required to establish it in this role (Pg. 429, Column 2, Paragraph, first partial). Therefore, the art has only recognized the treatment of a cancer.
With regard to the current state of the art, and the state of the art as of the effective filing date of the instant application, there are no methods, pharmaceutically relevant compositions, or specific treatments that can “prevent” transplant rejection, GvHD, and/or CD45RChigh-related diseases, disorders, and conditions (e.g., autoimmune diseases, undesired immune responses, monogenic diseases, lymphoma, and cancer) as instantly claimed. More specifically, there is no indication that CD45RC antigen binding domains, antibodies or antigen binding fragments thereof, immune cell populations expressing chimeric antigen receptors (CARs) thereof, nor nucleic acids encoding such antigen binding domains, antibodies or antigen binding fragments thereof, or CARs thereof would be capable of preventing transplant rejection, GvHD, and/or CD45RChigh-related diseases, disorders, and conditions (e.g., autoimmune diseases, undesired immune responses, monogenic diseases, lymphoma, and cancer) when administered to patients.
The Amount of Direction Provided by the Inventor/Existence of Working Examples
It is specifically noted that the instant specification provides no working examples for the prevention of CD45RChigh-related diseases, disorders, and conditions (e.g., autoimmune diseases, undesired immune responses, monogenic diseases, lymphoma, and cancer). The only working example provided in the instant specification (Pages 103-105) is drawn to a murine model of GvHD, wherein adult NSG immunodeficient mice were whole-body sublethaly irradiated (irradiation dose of 2 Gy at day -1) to induce lesions in tissues that will favor the development of GvHD; the following day (day 0), 1.5 X 107 PBMCs (including CD45RChigh and CD45RClow/- T cells) from healthy volunteers were injected intravenously in these mice. Human PBMCs, and in particular T cells, react against and attack mouse tissues inducing lesions; these T cells and the lesions observed in liver, intestine, lungs and skin mimic the GvHD observed following bone marrow transplantation in humans or other GvHD experimental systems using rodents as donors and recipients. NSG mice were treated intraperitoneally with the purified anti-CD45RC antibodies ABO-21001, ABO-21007 and ABO-21009, or with PBS at 0.8 mg/kg from day 0 and every 2.5 days for 20 days. Treatment with PBMCs only (PBS) induced mice death initiated around day 11, and, as shown in Figure 1A, death of all mice by day 15. Treatment with ABO-21001 and ABO-21009 increased the survival of the mice in comparison to PBS treated mice. At day 35, an average of 40% of treated mice are still alive (Figure 1A). Treatment with ABO-21007 significantly increased the survival of mice with an average of 70% of mice that were still alive at 35 days (Figure 1A). Similarly, upon treatment with ABO-21001 or ABO-21009, NSG mice lost weight although significantly less than NSG mice treated with PBS (Figure 1B). Treatment with ABO-21007 did not lead to any weight loss. The GvHD clinical score was also the lowest in mice treated with ABO-21007 (Figure 1C). However, this data is not supportive of preventing CD45RChigh-related diseases, disorders, and conditions (e.g., autoimmune diseases, undesired immune responses, monogenic diseases, lymphoma, and cancer) as generically as instantly claimed.
In view of the lack of the predictability of the art to which the invention pertains as evidenced by the art above, the lack of guidance and direction provided by Applicant, and the absence of working examples, undue experimentation would be required to use an antigen-binding domain specifically binding to CD45RC to treat any patient population and to prevent CD45RChigh-related diseases, disorders, or conditions with a reasonable expectation of success, absent a specific and detailed description in Applicant’s specification of how to effectively practice this and absent working examples providing evidence which is reasonably predictive that the claimed antigen-binding domain(s) is/are functional for the claimed uses, commensurate in scope with the claimed invention. Thus, claims 25 and 30 are rejected here. Claim 31 is included in this rejection as it depends from and/or incorporates claim 30.
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 19-23, 25, and 34-35 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 19 currently recites, at lines 2-3, “said antibody or antigen-binding fragment comprises an antigen-binding domain according to claim 16”; this limitation renders the claim indefinite as it is unclear as to what “an antigen-binding domain according to claim 16” is intended to encompass. For example, it is unclear if the recitation is intended to refer to the antigen-binding domain exactly as defined in claim 16 or if the antigen-binding domain as defined in claim 16 may be fragmented so long as it still specifically binds CD45RC. Thus, one of ordinary skill in the art could not reasonably ascertain the metes and bounds of the claim as currently presented and the claim is therefore indefinite. Claim 20 is included in this rejection as it depends from and/or incorporates claim 19.
Claim 21 is drawn to a chimeric antigen receptor (CAR), said CAR comprising the elements listed as (i)-(iii). However, one of ordinary skill in the art would be unable to ascertain the metes and bounds of the claim as currently presented because the elements of (i)-(iii) are not listed using “and”/“or” language. As such, it is unclear if all elements (i.e., (i), (ii), and (iii)) or at least one element (i.e., (i), (ii), or (iii)) is required to meet the limitations of the claim. As such, the claim is indefinite. Claims 22-23 and 34-35 are included in this rejection as they depend from/incorporate claim 21 without remedying the deficiency outlined above. Furthermore, it is noted that claim 35 is similarly drawn to the chimeric antigen receptor (CAR) according to claim 21, said CAR comprising the elements listed as (i)-(iii). However, similar to claim 21, one of ordinary skill in the art would be unable to ascertain the metes and bounds of the claim as currently presented because the elements of (i)-(iii) are not listed using “and”/“or” language. As such, it is unclear if all elements (i.e., (i), (ii), and (iii)) or at least one element (i.e., (i), (ii), or (iii)) is required to meet the limitations of the claim. Thus, claim 35 is indefinite.
Claim 25 recites the limitation "said subject" in line 2. There is insufficient antecedent basis for this limitation in the claim because the claim does not refer to a subject prior to the recitation of “said subject”. As such, claim 5 is indefinite because it is unclear as to what “said subject” is referring to.
Conclusion
Claims 16-35 are pending. Claims 19-23, 25, 30-31, and 34-35 are rejected. Claims 16-18, 24, 26-29, and 32-33 are allowed.
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/ALYSSA RAE STONEBRAKER/Examiner, Art Unit 1642
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