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. DETAILED ACTION Election/Restrictions 5. Applicant’s election of Group II in the reply filed on 9/9/2025 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). 6. Claims 20-26 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 9/9/2025. 7. Claims 27-29 are the pending claims under examination. Priority 8. USAN 17/502,238 , filed 10/15/2021 , is a Divisional of 15/893,629 , filed 02/10/2018, now U.S. Patent # 11173179 , 15 / 893 , 629 is a Continuation in Part of 15 / 739 , 596 , filed 12/22/2017, now U.S. Patent # 11655452 and having 2 RCE-type filing therein , 15 / 739 , 596 is a National Stage entry of PCT/US2016/039306, I nternational Filing Date: 06/24/2016 , PCT/US2016/039306 Claims Priority from Provisional Application 62/184,321 , filed 06/25/2015 , PCT/US2016/039306 Claims Priority from Provisional Application 62 / 235 , 840, filed 10/01/2015 , PCT/US2016/ 039306 Claims Priority from Provisional Application 62 / 244 , 435, filed 10/21/2015 . The disclosure of PCT/US2016/039306, I nternational Filing Date: 06/24/2016 , and prior-filed application 15/739,596 , filed on 12/22/2017 , and 15/893,629 , filed 02/10/2018, provide adequate support or enablement in the manner provided by the first paragraph of 35 U.S.C. 112 for one or more claims of this application. Specifically, the applications provide support for BCMA as the 1 st target antigen BCMA and CD19, CD20, CS-1 or CD38 as the 2 nd target antigen; and CD20 as the 1 st target antigen and CD19 as the 2 nd target antigen . Provisional Application 62 / 244 , 435, filed 10/21/2015 , teaches compound CAR structures comprising BCMA and/or CS1, and/or CD38 and/or 138 and/or CD19 and/or CD20 and teach es an interposed viral cleavable linker much less any one of the species of P2A, T2A, E2A or F2 A between the 1 st and 2 nd CARs. Accordingly, the effective priority date of claim s 27 -29 is granted as the filing date of 10/21/2015 . If Applicant believes the earlier applications provide support for this disclosure, Applicant should point out such support by page and line number in the reply to this Action . Information Disclosure Statement 9. As of 11/21/2025, a total of two (2) IDS are filed: 12/9/2024; and 12/9/2024. The corresponding initialed and dated 1449 form is considered and of record. Objections Specification 10. The disclosure is objected to because of the following informalities: a) The use of the term , NCBI, RediJet , Pharm Lyse , which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term . Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. b) Correct the spelling of Thosea asigna virus. Appropriate correction is required. Claim Objections 11. Claim s 2 7 - 29 are objected to because of the following informalities : Amend claim 27- 29 to replace “an antibody binding domain of _” with “an antibody binding domain [of _] that binds _.” Here “_” refers to the specific antigen recited in the claim. It is not clear or concise how an antibody binding domain is from or “of” an antigen. c ) Claims 27 are inconsistent for reciting “an antibody binding domain of _” (Claim 2 7 ) and “an antibody binding portion of _” (Claim 29 ). d ) Amend claim 29 to replace “engineering T cell” with “engineered T cell.” e ) Amend claims 2 7 - 29 to identify the engineered T- or NK-cells as autologous to the subject in need thereof. The specification supports the limitation at [0611] The majority of current clinical trials or therapies infuse autologous CAR T cells, as allogeneic CAR T cells are capable of inducing GVHD (graft-versus-host disease) in recipients. Although this autologous approach achieved remarkable clinical successes, the process of manufacturing a patient-specific T cell product is both time-consuming and expensive. Furthermore, it is not always possible to collect enough T cells from a heavily pretreated patient to successfully generate sufficient doses of CAR T cells. There is great demand for the development of an off-the-self allogeneic CAR product. NK cells are similar to T cells in that they are highly cytotoxic immune effectors. In contrast to T cells, NK cells bear the property of killing their targets through an on-specific manner. NK cells can be used as an off-the-self allogeneic product because they usually lack the potential to cause GVHD. The major disadvantage of using NK cells is their lack of persistence in vivo, with a half-life of only about a week. f) Amend claims 27-29 to c orrect the spelling of Thosea asigna virus. g) Amend claims 27-29 to recite “the cleavage site self-cleavage peptide .” h) Amend claims 27-29 to replace “a nucleotide sequence” with a “polynucleotide.” A nucleotide sequence is not the same as a polynucleotide; a polynucleotide is the long chain molecule (like DNA or RNA), while the nucleotide sequence is the specific order of the bases within that chain. Appropriate correction is required. 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 appl icant regards as his invention. 12. Claims 27-29 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. a) Claims 27-29 are indefinite and incomplete for reciting the phrase “ wherein the first and second costimulatory ”. The POSA cannot determine the metes and bounds of the invention because the phrase is incomplete . The phrase does not describ e the subject matter to which it refers n or how it further defines or modifies the first and second costimulatory domains. The phrase fails to particularly point out and distinctly claim the subject matter. Claim Rejections - 35 USC § 103 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis ( i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of 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 . 13. Claim(s) 2 7 -29 are rejected under 35 U.S.C. 102(a)(1) as being unpatentable over Milone et al., (US 2014/0322183; USPN 9745368 ; priority 2014-03-15 ) in view of Jarjour et al (US 10196444 ; priority to 2014-07-23 ) . Regarding claim s 27-29 , Milone in general teaches the advantage of dual-targeting CAR-T cells in order to improve the specificity of the lytic activity of the CAR-T and reducing the potential for depleting normal health tissue (“compositions and methods related to genetically modifying T cells to express a plurality of types of KIR-CARs, where KIR-CAR T cell activation is dependent on the binding of a plurality of types of KIR-CARs to their target receptor. Dependence on the binding of a plurality of types of KIR-CARs improves the specificity of the lytic activity of the KIR-CAR T cell, thereby reducing the potential for depleting normal healthy tissue” paragraph [0272] of the published application). Milone teaches T cells or NK cells comprising a first chimeric antigen receptor polypeptide (a) and a second chimeric engineered polypeptide (b) wherein the (a) and (b) are disposed on the same nucleic acid molecule, e.g., the same vector (paragraphs [0022]-[0023]). Milone discloses a type of chimeric antigen receptor (CAR) wherein the CAR is termed a "KIR-CAR" which is a CAR design comprising a component of a receptor naturally found on natural killer (NK) cells (abstract) comprising: ( i .) a first chimeric antigen receptor polypeptide comprising a first antigen recognition domain, a first signal peptide, a first hinge region, a first transmembrane domain, a first co-stimulatory domain, and a first signaling domain (paragraph [0005]) where the NKR-CAR comprises a transmembrane domain and an extra-cellular antigen binding domain, and further comprises a hinge domain disposed between said transmembrane domain and said extra-cellular antigen binding domain, Para. [0006]; and wherein “ the term "TCAR" comprises an antigen domain, an intracellular signaling domain, and optionally one or more costimulatory domains” (paragraph [0169]) and (ii.) a second chimeric antigen receptor polypeptide comprising a second antigen recognition domain, a second signal peptide, a second hinge region, a second transmembrane domain, a second co-stimulatory domain, and a second signaling domain (paragraph [0005]) where the NKR-CAR comprises a transmembrane domain and an extra-cellular antigen binding domain, and further comprises a hinge domain disposed between said transmembrane domain and said extra-cellular antigen binding domain, Para. [0006]; and wherein “the term "TCAR" comprises an antigen domain, an intracellular signaling domain, and optionally one or more costimulatory domains” (paragraph [0169]). Milone teaches a bicistronic lentiviral vector encoding both the mesothelin-specific KIR-based CAR (SS1-KIRS2) and the DAP12 molecule separated by the Thoseaasigna virus 2A ( T2A ) sequence was generated in order to achieve co-expression of both molecules (FIG. 2) at [0438]. Figure 2 of Milone identifies T2A interposed between the first and second CARs. Figure 2 of Malone teaches the first CAR, the T2A and the second CAR under the transcriptional control of a single promoter . AS regards claims 27-29 , Jarjour teaches and appreciates bicistronic CAR constructs comprising an interposed viral cleavable region for self-cleaving enzymes of the instant claims P2A, T2A, ERAV and FMDV: (29) For example, a cell can be modified to express two or more heterologous or exogenous nucleic acid molecules, which may be the same or different, that encode one or more fusion proteins, as disclosed herein. In certain embodiments, a host cell will contain a first nucleic acid molecule encoding a first fusion protein and a separate second nucleic acid molecule encoding a second fusion protein, or a host cell will contain a single polycistronic nucleic acid molecule that encodes a first fusion protein and second fusion protein, or single nucleic acid molecule that encodes a first fusion protein, a self-cleaving amino acid sequence and a second fusion protein. (31) In certain embodiments, the self-cleaving polypeptide site comprises a 2A or 2A-like site, sequence or domain (Donnelly et al., 2001. J. Gen. Virol . 82:1027-1041). In a particular embodiment, the viral 2A peptide is an aphthovirus 2A peptide, a potyvirus 2A peptide, or a cardiovirus 2A peptide. (32) In one embodiment, the viral 2A peptide is selected from the group consisting of: a foot-and-mouth disease virus ( FMDV) 2A peptide, an equine rhinitis A virus ( ERAV) 2A peptide, a Thosea asigna virus ( TaV ) 2A peptide, a porcine teschovirus-1 (PTV-1) 2A peptide, a Theilovirus 2A peptide, and an encephalomyocarditis virus 2A peptide. Jarjour teaches a P2A domain in SEQ ID NO: 41-49, 64-72, 75, and a T2A domain in SEQ ID NO: 74 . See the corresponding information in the Sequence Listing of Jarjour under “ < 223> other information ” for each of the sequences identified herein . Those sequences correspond to the nucleotides encoding a single nucleic acid molecule that encodes a first fusion protein, a self-cleaving amino acid sequence and a second fusion protein. Milone teaches antigens or targets for the first and second CARs will depend on the type of cancer being targeted and teaches the elected species along with others: [0301] Tumor antigens are proteins that are produced by tumor cells that elicit an immune response, particularly T-cell mediated immune responses. The selection of the antigen binding domain of the invention will depend on the particular type of cancer to be treated. Tumor antigens are well known in the art and include, for example, a glioma-associated antigen, carcinoembryonic antigen (CEA), EGFRvIII , IL-11Ra, IL-13Ra, EGFR, B7H3, Kit, CA-IX, CS-1 , MUC1, BCMA , bcr-abl , HER2, .beta.-human chorionic gonadotropin, alphafetoprotein (AFP), ALK, CD19, CD123, cyclin B1, lectin-reactive AFP, Fos-related antigen 1, ADRB3, thyroglobulin, EphA2, RAGE-1, RU1, RU2, SSX2, AKAP-4, LCK, OY-TES1, PAX5, SART3, CLL-1, fucosyl GM1, GloboH , MN-CA IX, EPCAM, EVT6-AML, TGS5, human telomerase reverse transcriptase, plysialic acid, PLAC1, RU1, RU2 (AS), intestinal carboxyl esterase, lewisY , sLe , LY6K, mut hsp70-2, M-CSF, MYCN, RhoC , TRP-2, CYP1B1, BORIS, prostase , prostate-specific antigen (PSA), PAX3, PAP, NY-ESO-1, LAGE-1a, LMP2, NCAM, p53, p53 mutant, Ras mutant, gp100, prostein , OR51E2, PANX3, PSMA, PSCA, Her2/neu, hTERT, HMWMAA, HAVCR1, VEGFR2, PDGFR-beta, legumain, HPV E6,E7, survivin and telomerase, sperm protein 17, SSEA-4, tyrosinase, TARP, WT1, prostate-carcinoma tumor antigen-1 (PCTA-1), ML-IAP, MAGE, MAGE-A1, MAD-CT-1, MAD-CT-2, MelanA /MART1, XAGE1, ELF2M, ERG (TMPRSS2 ETS fusion gene), NA17, neutrophil elastase, sarcoma translocation breakpoints, NY-BR-1, ephrinB2, CD20 , CD22, CD24, CD30, CD33, CD38 , CD44v6, CD97, CD171, CD179a, androgen receptor, insulin growth factor (IGF)-I, IGF-II, IGF-I receptor, GD2, o-acetyl-GD2, GD3, GM3, GPRC5D, GPR20, CXORF61, folate receptor ( FRa ), folate receptor beta, ROR1, Flt3, TAG72, TN Ag, Tie 2, TEM1, TEM7R, CLDN6, TSHR, UPK2, and mesothelin. In a preferred embodiment, the tumor antigen is selected from the group consisting of folate receptor ( FRa ), mesothelin, EGFRvIII , IL-13Ra, CD123, CD19 , CD33, BCMA, GD2, CLL-1, CA-IX, MUC1, HER2, and any combination thereof. AS regards claim s 27-29 , Milone teaches methods using the bicistronic construct for treating a subject, e.g., a method of providing an anti-tumor immunity in a mammal, comprising administering to the mammal an effective amount of a cytotoxic cell, e.g., a naturally or non-naturally occurring T cell, NK cell or cytotoxic T cell or NK cell line comprising a NKR-CAR described herein at [0010] . As regards claim 28, Milone teaches the method comprises treating a mammal, e.g., a human, having a disorder associated with unwanted cell proliferation, e.g., cancer . In one embodiment, said disorder is pancreatic carcinoma, mesothelioma, lung carcinoma, ovarian carcinoma, leukemia or lymphoma at [0040]. [0299] In the context of the present disclosure, "tumor antigen" or "proliferative disorder antigen" or "antigen associated with a proliferative disorder" refers to antigens that are common to specific proliferative disorders. In certain aspects, the proliferative disorder antigens of the present invention are derived from, cancers including but not limited to primary or metastatic melanoma, thymoma, lymphoma, sarcoma, lung cancer (e.g., NSCLC or SCLC), liver cancer, non-Hodgkin's lymphoma, Hodgkin's lymphoma, leukemias, multiple myeloma, glioblastoma, neuroblastoma, uterine cancer, cervical cancer, renal cancer, thyroid cancer, bladder cancer, kidney cancer and adenocarcinomas such as breast cancer, prostate cancer, ovarian cancer, pancreatic cancer, colon cancer and the like. In some embodiments, the cancer is B-cell acute lymphoid leukemia ("BALL"), T-cell acute lymphoid leukemia ("TALL"), acute lymphoid leukemia (ALL), acute myelogenous leukemia (AML); one or more chronic leukemias including but not limited to chronic myelogenous leukemia (CML), chronic lymphocytic leukemia (CLL); additional hematologic cancers or hematologic conditions including, but not limited to B cell prolymphocytic leukemia, blastic plasmacytoid dendritic cell neoplasm, Burkitt's lymphoma, diffuse large B cell lymphoma, follicular lymphoma, hairy cell leukemia, small cell- or a large cell-follicular lymphoma, malignant lymphoproliferative conditions, MALT lymphoma, mantle cell lymphoma, Marginal zone lymphoma, multiple myeloma, myelodysplasia and myelodysplastic syndrome, non-Hodgkin's lymphoma, plasmablastic lymphoma, plasmacytoid dendritic cell neoplasm, Waldenstrom macroglobulinemia, AS regards claim 29 , Milone teaches that r egardless of the type of KIR-CAR, KIR-CARs are engineered to comprise an extracellular domain having an antigen binding domain fused to a cytoplasmic domain. In one embodiment, KIR-CARs, when expressed in a T cell, are able to redirect antigen recognition based upon the antigen specificity. An exemplary antigen is CD19 because this antigen is expressed on B cell lymphoma. However, CD19 is also expressed on normal B cells, and thus CARs comprising an anti-CD19 domain may result in depletion of normal B cells. Depletion of normal B cells can make a treated subject susceptible to infection, as B cells normally aid T cells in the control of infection. The present invention provides for compositions and methods to limit the depletion of normal tissue during KIR-CAR T cell therapy. In one embodiment, the present invention provides methods to treat cancer and other disorders using KIR-CAR T cell therapy while limiting the depletion of healthy bystander cells at [0271] . The ordinary artisan would have found more than sufficient motivation to have used the claimed engineered cell in a method for treating proliferative diseases or reducing B cells in view of Milone and Jarjour , where the combination reference teach dual targeting CAR-T having the ability for regulating: a cytotoxic cell, e.g., T cell, and specificity to control off-target activity of the engineered T cell. Accordingly, where Milone solved and overcome the several caveats that would otherwise compromise a single CAR-T, the dual targeting aspect under regulatory control in view of Jarjour would have been the motivation for the ordinary artisan to create an improved engineered cell of this nature and kind. Because Milone’s teachings are vast and the techniques to create such engineered cells was available to ordinary artisan, and Jajour substantiates bicistronic CARs interposed with self-cleavable enzymes, there would have been a reasonable assurance of success in having generated an engineered cell based on the platform technology taught in Milone and Jarjour . 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 . 14. Claim s 27-29 are rejected on the ground of nonstatutory double patenting a s being unpatentable over claim s 1-7 of U.S. Patent No. 11905528 . The reference claims are not affor d ed safe harbor protection under 35 USC 121 because they do not share continuity nor a restriction/ speciation with the claims of the instant application. Although the claims at issue are not identical, they are not patentably distinct from each other because the claim sets are drawn to a compound CAR ( cCAR ) comprising a viral cleavage peptide interposed between the 1 st and 2 nd CAR. Ref claims 1-7 : 1. An ex vivo engineered T cell or NK cell co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5′ to 3′ a first polynucleotide encoding a first chimeric antigen receptor polypeptide (first CAR), a second polynucleotide encoding a second chimeric antigen receptor polypeptide (second CAR), a nucleotide encoding porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), FMDV 2A (F2A) or equine rhinitis A virus (ERAV) 2A (E2A1 disposed between the first CAR and second CAR , under the transcriptional control of a single promoter, wherein: ( i .) the first CAR polypeptide comprises a first antigen recognition domain; a first signal peptide; a first hinge region; a first transmembrane domain; a first co-stimulatory domain; and a first signaling domain; and (ii.) the second CAR comprises a second antigen recognition domain; a second signal peptide; a second hinge region; a second transmembrane domain; a second co-stimulatory domain; and a second signaling domain; wherein the first antigen recognition domain and the second antigen recognition domain are different; wherein the engineered T cell or NK cell comprises an enhancer selected from the group consisting of IL-15/IL-15sushi, IL-15/IL-15 sushi anchor, 4-1BBL, and IL-15: and wherein the engineered T cell or NK cell comprises SEQ ID NO: 1, SEQ ID NO: 28, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 50, SEQ ID NO: 52 , or SEQ ID NO: 60. 2. The engineered cell according to claim 1, wherein the engineered T cell or NK cell comprises SEQ ID NO: 60. 3. The engineered cell according to claim 1, wherein the enhancer is secreted by the engineered cell. 4. The engineered cell according to claim 1, wherein the engineered T cell is an NK T cell. 5. A method of treating a cell proliferative disease comprising administering an engineered T cell or NK cell according to claim 1 to a patient in need thereof. 6. The method according to claim 5, wherein the cell proliferative disease comprises a t-cell malignancy, leukemia, or a lymphoma. 7. The method according to claim 5, wherein the engineered T cell is an NK T cell. SEQ ID NO: 52 of ref claim 1 is for a CD20/CD19 cCAR and overlaps with the CD20xCD19 cCAR of the instant claims. Claims 27-29 27. A method for treating a cell proliferation disease, said method comprises administering to a patient in need thereof an ex vivo engineered T cell according to claim 20 or NK cell co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5' to 3’ a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a viral self-cleavage peptide disposed between the first CAR and second CAR , under the transcriptional control of a single promoter, wherein: (1) the first CAR comprises a first signal peptide, a first antigen recognition domain, a first hinge region, a first transmembrane domain, a first 4- IBB or CD28 co-stimulatory domain, and a first CD3 signaling domain that form a first fusion protein: and (11) the second CAR comprises a second signal peptide, a second antigen recognition domain, a second hinge region, a second transmembrane domain, a second 4- IBB or CD28 co- stimulatory domain, and a second CD3 signaling domain that form a second fusion protein: and wherein the first antigen recognition domain and the second antigen recognition domain are different and each bind to a different target, wherein the targets of the first antigen recognition domain and the second antigen recognition domain are a combination of an antibody binding domain of BCMA and an antibody binding domain of CD19, or a combination of an antibody binding domain of BCMA and an antibody binding domain of CD20 or a combination of an antibody binding domain of BCMA and an antibody binding domain of CS-1 (CD319) or a combination of an antibody binding domain of BCMA and an antibody binding domain scFv of CD38 or a combination of an antibody binding domain of CD20 and an antibody binding domain of CD19 , wherein the first and second costimulatory, and wherein the cleavage site is selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A) . 28 . The method according to claim 27, wherein said cell proliferation disease comprises B-cell lymphoma, T-cell lymphoma, multiple myeloma, chronic myeloid leukemia, acute myeloma leukemia, myelodysplastic syndromes, chronic myeloproliferative neoplasms, or B-cell acute lymphoblastic leukemia (B-ALL). 29 . A method for reducing antibody producing cells selected from B cells and plasma cells, said method comprises administering to a patient in need thereof an ex vivo engineering T cell or NK cell according to claim 20 co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5' to 3' a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a viral self-cleavage peptide disposed between the first CAR and second CAR , under the transcriptional control of a single promoter, wherein: (1) the first CAR comprises a first signal peptide, a first antigen recognition domain, a first hinge region, a first transmembrane domain, a first 4- IBB or CD28 co-stimulatory domain, and a first CD3 signaling domain that form a first fusion protein: and (11) the second CAR comprises a second signal peptide, a second antigen recognition domain, a second hinge region, a second transmembrane domain, a second 4- IBB or CD28 co- stimulatory domain, and a second CD3 signaling domain that form a second fusion protein: and wherein the first antigen recognition domain and the second antigen recognition domain are different and each bind to a different target, wherein the targets of the first antigen recognition domain and the second antigen recognition domain are a combination of an antibody binding domain of BCMA and an antibody binding domain of CD19, or a combination of an antibody binding domain of BCMA and an antibody binding domain of CD20 or a combination of an antibody binding domain of BCMA and an antibody binding domain of CS-1 (CD319) or a combination of an antibody binding domain of BCMA and an antibody binding domain scFv of CD38 or a combination of an antibody binding domain of CD20 and an antibody binding domain of CD19 , wherein the first and second costimulatory, and wherein the cleavage site is selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A) . 1 5 . Claim s 2 7 - 29 are rejected on the ground of nonstatutory double patenting a s being unpatentable over claim s 1-2 of U.S. Patent No. 12275787 . The reference claims are not afforded safe harbor protection under 35 USC 121 because they do not share continuity nor a restriction/ speciation with the claims of the instant application. Although the claims at issue are not identical, they are not patentably distinct from each other because the claim sets are drawn to a compound CAR ( cCAR ) comprising a viral cleavage peptide interposed between the 1 st and 2 nd CAR. Ref claims 1-2 1. A method for treating an autoimmune disease, said method comprising administering to a patient in need thereof an ex vivo engineered T cell or NK cell co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5′ to 3′ a nucleotide encoding a promoter selected from human elongation factor-1 alpha (EF-1α) or spleen focus forming virus (SFFV), a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a first cleavage peptide , and a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR), wherein the engineered cell further comprises a nucleotide encoding secreted IL-15/IL-15sushi or a functional fragment thereof, wherein the nucleotide encoding said enhancer is attached to the nucleotide encoding the first CAR or the nucleotide encoding the second CAR by a nucleotide encoding a second cleavage peptide that flanks either end of the two distinct encoded CAR units, wherein: the first CAR comprises a first signal peptide, a first antibody binding domain, a first hinge region, a first transmembrane domain, a first co-stimulatory domain, and a first signaling domain; and the second CAR comprises a second signal peptide, a second antibody binding domain, a second hinge region, a second transmembrane domain, a second co-stimulatory domain, and a second signaling domain; and wherein the first antibody binding domain and the second antibody binding domain are different and each bind to a different target, wherein the targets of the first and second antibody binding domains irrespective of order are CD19 and BMCA (CD269) , wherein the first and second co-stimulatory domains are intracellular, and wherein the first and second cleavage peptides are selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A) , and wherein said autoimmune disease is systemic lupus erythematosus (SLE). 2. The method according to claim 1, wherein the co-stimulatory domain is CD28. Claims 2 7 - 29 27. A method for treating a cell proliferation disease, said method comprises administering to a patient in need thereof an ex vivo engineered T cell according to claim 20 or NK cell co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5' to 3’ a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a viral self-cleavage peptide disposed between the first CAR and second CAR , under the transcriptional control of a single promoter, wherein: (1) the first CAR comprises a first signal peptide, a first antigen recognition domain, a first hinge region, a first transmembrane domain, a first 4- IBB or CD28 co-stimulatory domain, and a first CD3 signaling domain that form a first fusion protein: and (11) the second CAR comprises a second signal peptide, a second antigen recognition domain, a second hinge region, a second transmembrane domain, a second 4- IBB or CD28 co- stimulatory domain, and a second CD3 signaling domain that form a second fusion protein: and wherein the first antigen recognition domain and the second antigen recognition domain are different and each bind to a different target, wherein the targets of the first antigen recognition domain and the second antigen recognition domain are a combination of an antibody binding domain of BCMA and an antibody binding domain of CD19 , or a combination of an antibody binding domain of BCMA and an antibody binding domain of CD20 or a combination of an antibody binding domain of BCMA and an antibody binding domain of CS-1 (CD319) or a combination of an antibody binding domain of BCMA and an antibody binding domain scFv of CD38 or a combination of an antibody binding domain of CD20 and an antibody binding domain of CD19 , wherein the first and second costimulatory, and wherein the cleavage site is selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A) . 28. The method according to claim 27, wherein said cell proliferation disease comprises B-cell lymphoma, T-cell lymphoma, multiple myeloma, chronic myeloid leukemia, acute myeloma leukemia, myelodysplastic syndromes, chronic myeloproliferative neoplasms, or B-cell acute lymphoblastic leukemia (B-ALL). 29. A method for reducing antibody producing cells selected from B cells and plasma cells, said method comprises administering to a patient in need thereof an ex vivo engineering T cell or NK cell according to claim 20 co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5' to 3' a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a viral self-cleavage peptide disposed between the first CAR and second CAR , under the transcriptional control of a single promoter, wherein: (1) the first CAR comprises a first signal peptide, a first antigen recognition domain, a first hinge region, a first transmembrane domain, a first 4- IBB or CD28 co-stimulatory domain, and a first CD3 signaling domain that form a first fusion protein: and (11) the second CAR comprises a second signal peptide, a second antigen recognition domain, a second hinge region, a second transmembrane domain, a second 4- IBB or CD28 co- stimulatory domain, and a second CD3 signaling domain that form a second fusion protein: and wherein the first antigen recognition domain and the second antigen recognition domain are different and each bind to a different target, wherein the targets of the first antigen recognition domain and the second antigen recognition domain are a combination of an antibody binding domain of BCMA and an antibody binding domain of CD19 , or a combination of an antibody binding domain of BCMA and an antibody binding domain of CD20 or a combination of an antibody binding domain of BCMA and an antibody binding domain of CS-1 (CD319) or a combination of an antibody binding domain of BCMA and an antibody binding domain scFv of CD38 or a combination of an antibody binding domain of CD20 and an antibody binding domain of CD19 , wherein the first and second costimulatory, and wherein the cleavage site is selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A) . 1 6 . Claim s 2 7 - 29 are rejected on the ground of nonstatutory double patenting a s being unpatentable over claim s 1-5 of U.S. Patent No. 11820819 . The reference claims are not afforded safe harbor protection under 35 USC 121 because they do not share continuity nor a restriction/ speciation with the claims of the instant application. Although the claims at issue are not identical, they are not patentably distinct from each other because the claim sets are drawn to a compound CAR ( cCAR ) comprising a viral cleavage peptide interposed between the 1 st and 2 nd CAR. Ref claims 1-5 1. A method for treating leukemia or lymphoma in a patient in need thereof, said method comprising: administering to said patient in need thereof a composition comprising an engineered T cell or NK cell co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5′ to 3′ a promoter selected from human elongation factor-1 alpha (EF-1α) or spleen focus forming virus (SFFV), a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a first, self-cleavage peptide, a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR) a nucleotide encoding a second self-cleavage peptide, and a third polynucleotide encoding a fusion protein consisting of IL-15 linked to a soluble domain of IL-15Rα (sushi) and secreted as a soluble IL-15/IL-15 sushi complex wherein: ( i ) the first CAR comprises a first signal peptide, a first antibody binding domain, a first hinge region, a first transmembrane domain, a first CD28 or 4-1BB co-stimulatory domain, and a first signaling domain; and (ii) the second CAR comprises a second signal peptide, a second antibody binding domain, a second hinge region, a second transmembrane domain, a second CD28 or 4-1BBz co-stimulatory domain, and a second signaling domain; and wherein the first antibody binding domain and the second antibody binding domain are different from each other, and each bind to a different target, wherein the targets of the first and second antibody binding domains irrespective of order are CD33 and CLL-1, CD123 and CD33, BCMA and CD19 or BCMA and CS-1 , wherein the first and second co-stimulatory domains are intracellular, and wherein the cleavage site is selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A) . 2. The method according to claim 1, wherein the leukemia is acute myeloid leukemia (AML). 3. A method for treating multiple myeloma in a patient in need thereof, said method comprising: administering to said patient in need thereof a composition comprising an engineered T cell or NK cell co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5′ to 3′ a promoter selected from human elongation factor-1 alpha (EF-1α) or spleen focus forming virus (SFFV), a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a first, self-cleavage peptide, a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR) a nucleotide encoding a second self-cleavage peptide, and a third polynucleotide encoding a fusion protein consisting of IL-15 linked to a soluble domain of IL-15Rα (sushi) and secreted as a soluble IL-15/IL-15 sushi complex wherein: ( i ) the first CAR comprises a first signal peptide, a first antibody binding domain, a first hinge region, a first transmembrane domain, a first CD28 or 4-1BB co-stimulatory domain, and a first signaling domain; and (ii) the second CAR comprises a second signal peptide, a second antibody binding domain, a second hinge region, a second transmembrane domain, a second CD28 or 4-1BBz co-stimulatory domain, and a second signaling domain; and wherein the first antibody binding domain and the second antibody binding domain are different from each other, and each bind to a different target, wherein the targets of the first and second antibody binding domains irrespective of order are BCMA and CD19 or BCMA and CS-1 , wherein the first and second co-stimulatory domains are intracellular, wherein the promoter is strong spleen focus forming virus promoter (SFFV) or elongation factor-1 alpha (EF-1α), and wherein the cleavage site is selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A). 4. A method for depleting antibody producing B cells and/or plasma cells in a patient with an autoimmune condition, said method comprising: administering to said patient in need thereof a composition comprising an engineered T cell or NK cell co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5′ to 3′ a promoter selected from human elongation factor-1 alpha (EF-1α) or spleen focus forming virus (SFFV), a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a first, self-cleavage peptide, a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR) a nucleotide encoding a second self-cleavage peptide, and a third polynucleotide encoding a fusion protein consisting of IL-15 linked to a soluble domain of IL-15Rα (sushi) and secreted as a soluble IL-15/IL-15 sushi complex wherein: ( i ) the first CAR comprises a first signal peptide, a first antibody binding domain, a first hinge region, a first transmembrane domain, a first CD28 or 4-1BB co-stimulatory domain, and a first signaling domain; and (ii) the second CAR comprises a second signal peptide, a second antibody binding domain, a second hinge region, a second transmembrane domain, a second CD28 or 4-1BBz co-stimulatory domain, and a second signaling domain; and wherein the first antibody binding domain and the second antibody binding domain are different from each other, and each bind to a different target, wherein the wherein the targets of the first and second antibody binding domains irrespective of order are BCMA and CD19 or BCMA and CS-1 , wherein the first and second co-stimulatory domains are intracellular, and wherein the cleavage site is selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A) , and wherein said patient's autoimmune condition improves as a result of said depletion of antibody producing B cells and/or plasma cells. 5. The method according to claim 4, wherein the autoimmune condition is selected from systemic scleroderma, multiple sclerosis, psoriasis, dermatitis, inflammatory bowel disease, systemic lupus erythematosus, pemphigus vulgaris, vasculitis, rheumatoid arthritis, Sjorgen's syndrome, polymyositis, pulmonary alveolar proteinosis, granulomatosis, vasculitis, Addison's disease, antigen-antibody complex mediated disease, and anti-glomerular basement membrane disease. Claims 2 7 - 29 27. A method for treating a cell proliferation disease, said method comprises administering to a patient in need thereof an ex vivo engineered T cell according to claim 20 or NK cell co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5' to 3’ a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a viral self-cleavage peptide disposed between the first CAR and second CAR , under the transcriptional control of a single promoter, wherein: (1) the first CAR comprises a first signal peptide, a first antigen recognition domain, a first hinge region, a first transmembrane domain, a first 4- IBB or CD28 co-stimulatory domain, and a first CD3 signaling domain that form a first fusion protein: and (11) the second CAR comprises a second signal peptide, a second antigen recognition domain, a second hinge region, a second transmembrane domain, a second 4- IBB or CD28 co- stimulatory domain, and a second CD3 signaling domain that form a second fusion protein: and wherein the first antigen recognition domain and the second antigen recognition domain are different and each bind to a different target, wherein the targets of the first antigen recognition domain and the second antigen recognition domain are a combination of an antibody binding domain of BCMA and an antibody binding domain of CD19 , or a combination of an antibody binding domain of BCMA and an antibody binding domain of CD20 or a combination of an antibody binding domain of BCMA and an antibody binding domain of CS-1 (CD319) or a combination of an antibody binding domain of BCMA and an antibody binding domain scFv of CD38 or a combination of an antibody binding domain of CD20 and an antibody binding domain of CD19 , wherein the first and second costimulatory, and wherein the cleavage site is selected from the group consisting of porcine teschovirus-1 2A (P2A), thoseaasigna virus 2A (T2A), equine rhinitis A virus (ERAV) 2A (E2A), and FMDV 2A (F2A) . 28. The method according to claim 27, wherein said cell proliferation disease comprises B-cell lymphoma, T-cell lymphoma, multiple myeloma, chronic myeloid leukemia, acute myeloma leukemia, myelodysplastic syndromes, chronic myeloproliferative neoplasms, or B-cell acute lymphoblastic leukemia (B-ALL). 29. A method for reducing antibody producing cells selected from B cells and plasma cells, said method comprises administering to a patient in need thereof an ex vivo engineering T cell or NK cell according to claim 20 co-expressing two distinct chimeric antigen receptor (CAR) units at the cell surface, wherein the engineered T cell or NK cell comprises a nucleotide sequence comprising from 5' to 3' a first polynucleotide encoding a first chimeric antigen receptor polypeptide (CAR), a second polynucleotide encoding a second chimeric antigen receptor polypeptide (CAR), a nucleotide encoding a viral self-cleavage peptide disposed between the first CAR and second CAR , under the transcriptional control of a single promoter, wherein: (1) the first CAR comprises a first signal peptide, a first antigen recognition domain, a first hinge region, a first transmembrane domain, a first 4- IBB or CD28 co-stimulatory domain, and a first CD3 signaling domain that form a first fusion protein: and (11) the second CAR comprises a second signal peptide, a second antigen recognition domain, a second hinge region, a second transmembrane domain, a second 4- IBB or CD28 co- stimulatory domain, and a second CD3 signaling domain that form a second fusion protein: and wherein the first antigen recognition domain and the