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
Claims 16-39 are pending in the instant application and are being examined on the merits.
Priority
Should applicant desire to obtain the benefit of foreign priority under 35 U.S.C. 119(a)-(d) prior to declaration of an interference, a certified English translation of the foreign application must be submitted in reply to this action. 37 CFR 41.154(b) and
41.202(e). Failure to provide a certified translation may result in no benefit being accorded for the non-English application. The effective priority date is the filing date of
PCT/CN2022/073943 filed on 1/26/2022 in the absence of a certified translation of
CN202110123809.3. filed on 1/29/2021.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 21-22 and 35-39 are rejected under 35 U.S.C. 101 because the claimed invention is directed to non-statutory subject matter. The claims do not fall within at least one of the four categories of patent eligible subject matter because the claims are directed to the “use” of the compound of formula (F) or antibody-drug conjugate. The claims are not directed toward a: 1) composition of matter; 2) machine; 3) manufacture; or 4) process, but rather a “use” of a compound of formula (F) or antibody-drug conjugate, wherein no active method steps are present to suggest a process is being claimed. "Use" claims that do not purport to claim a process, machine, manufacture, or composition of matter fail to comply with 35 U.S.C. 101 MPEP 2173.05(q).
Claim Rejections – 35 USC § 112(b)
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 21-22 and 35-39 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.
Regarding instant claims 21-22 and 35-39, the meets and bound of the claims are indefinite. MPEP 2173.05(q) states attempts to claim a process without setting forth any steps involved in the process generally raises an issue of indefiniteness. Recitation of a use without any active, positive steps delimiting how this use is actually practiced is indefinite.
Claim Rejections – 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 26-28 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Regarding claim 26, a human antibody is claimed, but the antibody requires the antibody is comprised of VH and VL CDRs present in claim 24, which are from a murine antibody as defined in the specification on page 26 in Table 2. Thus, the claim represents an expansion of scope because a murine antibody can’t be human; CDR grafting would produce a humanized antibody. Claims 27-28 are dependent on claim 26 and would also allow selection of a human antibody. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections – 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 35-39 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claims 35-39 claim a method of preventing a BCMA-mediated disease but the specification does not show an effective method of preventing a BCMA mediated disease of cancer or autoimmune disease;
Claims 35-36, and 38-39 do not require the BCMA mediated disease of cancer or autoimmune disease to express BCMA. Only claim 37 requires BCMA expression.
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, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention.
Scope of the claimed genus
Regarding claims 35-39, the claims are drawn to use of an ADC in the preparation of a medicament for treating or preventing a BCMA-mediated disease (claim 35), wherein the BCMA-mediated disease or condition is cancer or autoimmune disease (claim 36), wherein the cancer expresses BCMA (claim 37), wherein the cancer is myeloma (claim 38), wherein the autoimmune disease is lupus erythematosus (claim 39).
Summary of Species disclosed in the original specification
1 and 2) The instant specification taught treatment of NCI-929 myeloma cells that express BCMA, but did not teach effective prevention of a disease wherein the disease was not first established or treatment of a disease that did not express BCMA.
State of the Relevant Art
Cho taught B cell maturation antigen (BCMA), a transmembrane glycoprotein in the tumor necrosis factor receptor superfamily 17 (TNFRSF17), is expressed at significantly higher levels in all patient multiple myeloma (MM) cells but not on other normal tissues except normal plasma cells (Cho S-F et al. (Front Immunol 2018 9:1821 1-15. doi: 10.3389/fimmu.2018.01821) abstract). Cho taught majorities of studies indicate that BCMA transcript, protein, and the serum BCMA level are significantly higher in MM cell lines and patient MM cells, when compared with normal donors (page 4, left column, second paragraph). Cho taught BCMA mRNA and protein are more highly expressed on malignant than normal plasma cells, as validated by multiple gene expression profiling and immunohistochemistry (IHC) studies (page 3, right column, last paragraph). Cho did not teach a method of targeting BCMA for prevention. Thus, while targeting of BCMA is known for diseases that express high levels of BCMA, targeting BCMA for prevention of disease is not known to be effective.
The anti-BCMA ADC would require expression of BCMA to target the toxin to the cell. Effectively targeting cells that do not express BCMA with an anti-BCMA ADC is not known to the prior art.
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.
Given the variability encompassed by the genus of zero described species of disease prevention or diseases that did not express BCMA, the species cannot be considered representative of the genus.
Therefore, the skilled artisan would not reasonably conclude that the inventors, at the time the application was filed, had full possession of 1) a method of preventing a BCMA-mediated disease; or 2) treatment of a BCMA mediated disease of cancer or autoimmune disease that does not express BCMA as broadly claimed.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
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.
Claims 16-23, 31, and 33-34 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2020/063676 (Xu J et al.) and evidenced by translated WO 2020/063676 (Xu J et al.)
‘676 translated taught ADC-29 with a structure of
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(pages 78-79, [0991-0994]) was effective in a method of treating cancer when a pharmaceutical composition comprising ADC-29 and a pharmaceutically acceptable excipient of PBS was administered to a subject with cancer (Fig. 6), wherein n was about 7, wherein the antibody 1F9DS effectively targeted the drug conjugate to B7H3 expressing cancer cells. ‘676 translated taught a method of producing an ADC-29 wherein the antibody was reacted with compound 9 (pages 78-79, [0991-0994]), wherein the structure of compound 9 was
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(page 45, [0507]).
‘676 translated taught was effective in a method of treating cancer when a pharmaceutical composition of ADC-29 was administered to a subject with cancer (Fig. 6), wherein n was about 7, wherein the antibody 1F9DS effectively targeted the drug conjugate to B7H3 expressing cancer cells.
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‘676 translated taught ADC-15 and ADC-16 (pages 73-74 [0921-0929]) were dose-dependently effective against cancer cells, wherein n was about 7 to 8, wherein the antibody trastuzumab effectively targeted the drug conjugate to HER2 expressing cancer cells (page 82 [1052-1054]). Thus, ADCs comprising: 1) a linker comprising a methyl cyclopropyl group in different planes between the oxygen and carbonyl; and 2) polyethylene glycol linkers attached to GGFG linked compounds, are effective.
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‘676 translated taught ADC-19 with a structure of:
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which comprises a linker comprising a methyl cyclopropyl group between the oxygen and carbonyl (page 75 [0941]), is stable in human and monkey plasma, and 1% BSA (Fig. 1A), while ADC-18 with a structure of:
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, which does not comprise a linker with a methyl cyclopropyl group between the oxygen and carbonyl (page 75 [0941]), is less stable in human and monkey plasma (Fig. 1B).
‘676 translated taught an ADC wherein the methyl cyclopropyl linker moiety was a flat planar bond
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(page 14 [0187]).
‘676 translated taught W as containing a C1-C8 heteroalkyl with O as the heteroatom for the formula (Pc-La-Y-Dr)
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, which would include -(CH2)2-O-(CH2)2-O-(CH2)2- (pages 9-10, [0155-0167]).
‘676 did not teach a single embodiment of a compound of formula (F) or an ADC of formula (I), but this is obvious in view of the teachings of ‘676.
Regarding claims 21, 23, 31, and 34, it would have been obvious for a person having ordinary skill in the art to take the method of ‘676 for treating cancer in a subject by administering a pharmaceutical composition comprising ADC-29 and a pharmaceutically acceptable excipient of PBS – and: 1) exchange the stereochemistry of the methyl cyclopropyl group to be a flat planar bond; 2) exchange the alkyl group attached to the maleimide for -(CH2)2-O-(CH2)2-O-(CH2)2-; 3) exchange the drug to antibody ration number n for n of 8, as taught by ‘676.
This is obvious because: 1a) ‘676 taught the methyl cyclopropyl linker as a flat planar bond; 1-3) ‘676 translated taught ADC-15 and ADC-16 were dose-dependently effective against cancer cells, wherein n was about 7 to 8, wherein the antibody effectively targeted the drug conjugate to antibody target expressing cancer cells. Thus, ADCs comprising: i) a linker comprising a methyl cyclopropyl group in different planes between the oxygen and carbonyl; ii) polyethylene glycol linkers attached to GGFG linked compounds; and iii) an n of 8, are effective; and 2) ‘676 translated taught W as containing a C1-C8 heteroalkyl with O as the heteroatom for the formula (Pc-La-Y-Dr)
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, which would include -(CH2)2-O-(CH2)2-O-(CH2)2-; 3)
There is a reasonable expectation of success because: 1-3) ‘676 translated taught ADC-15 and ADC-16 were dose-dependently effective against cancer cells, wherein n was about 7 to 8, wherein the antibody effectively targeted the drug conjugate to antibody target expressing cancer cells. Thus, ADCs comprising: i) a linker comprising a methyl cyclopropyl group in different planes between the oxygen and carbonyl; ii) polyethylene glycol linkers attached to GGFG linked compounds; and iii) an n of 8, are effective; Further, a linker comprising a methyl cyclopropyl group between the oxygen and carbonyl, is stable in human and monkey plasma.
This would produce a method for treating cancer in a subject by administering a pharmaceutical composition comprising an ADC of:
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(claim 21, 23, and 31) and a pharmaceutically acceptable excipient of PBS (claim 34). This meets the claim limitations of claims 21, 23, 31, and 34.
Regarding claims 16-20, 22, and 33, it would have been obvious for a person having ordinary skill in the art to take the ADC of ‘676 above and: 1) produce the ADC above by a method of reacting a maleimide containing compound with an antibody of 1F9DS as taught by ‘676 which would require the maleimide compound
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and the antibody 1F9DS.
This is obvious with a reasonable expectation of success because: 1) ‘676 taught a method of producing ADC-29 wherein the antibody was reacted with compound 9, wherein the structure of compound 9 was
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and the method effectively produced the ADC.
This would produce a method of producing and ADC wherein the method comprised reacting the antibody 1F9DS with the compound
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(claim 16-20) to produce the ADC of
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(claims 22 and 33). This meets the claim limitations of claims 16-20, 22, and 33.
Claims 16-39 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2020/063676 (Xu J et al.) as applied to claims 16-23, 31, and 33-34 above, and further in view of WO 2021/018168 (Hua H et al.) and evidenced by translated WO 2020/063676 (Xu J et al.) and translated WO 2021/018168 (Hua H et al.).
‘676 is described above.
‘676 did not teach an anti-BCMA ADC or treatment with an anti- BCMA, but this is obvious in view of ‘168.
‘168 translated taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 (page 16, Table 5). ‘168 taught an ADC comprising Ab2 was effective when administered to subjects with cancer, wherein the cancer was NCI-929 myeloma (page 21-22, Table 10, [0290-0295]). ‘168 translated taught BCMA is highly expressed in multiple myeloma (page 2, [0003]). ‘168 translated taught cancers and autoimmune diseases involving B cells can be considered abnormal B cell function, so a possible strategy to control these diseases is to use antibodies that target pathological B cells (page 2, [0002]). ‘168 translated taught the autoimmune disease systemic lupus erythematosus involves B cells (page 2, [0002]). ‘168 translated taught the use of antibody-drug conjugates for the treatment of BCMA-mediated diseases or conditions, wherein the autoimmune disease is lupus erythematosus (page 7, [0106]).
Regarding claims 24-30, 32, and 35-39, it would have been obvious for a person having ordinary skill in the art to take the method for treating cancer in a subject by administering a pharmaceutical composition comprising an ADC of:
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and a pharmaceutically acceptable excipient of ‘676 – and:
1) exchange the 1F9DS targeting antibody for the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19;
2) treat the BCMA mediated cancer myeloma that expressed BCMA; and
3) treat the BCMA mediated autoimmune disease lupus erythematosus that expressed BCMA, in view of ‘168
This is obvious because: 1-2) ‘168 taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 and was effective when administered to subjects with myeloma and BCMA is highly expressed in multiple myeloma; 3a) ‘168 taught autoimmune diseases involving B cells can be considered abnormal B cell function, so a possible strategy to control these diseases is to use antibodies that target pathological B cells, wherein the autoimmune disease systemic lupus erythematosus involves B cells; and 3b) ‘168 taught the use of antibody-drug conjugates for the treatment of BCMA-mediated diseases or conditions, wherein the autoimmune disease is lupus erythematosus.
There is a reasonable expectation of success because: 1-2) ‘168 taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 and was effective when administered to subjects with myeloma and BCMA is highly expressed in multiple myeloma; 3) Abnormal B cells of subjects with the autoimmune disease systemic lupus erythematosus that express BCMA would be targeted by the ADC and killed which would treat the disease.
This would produce a method of treating BCMA mediated diseases that expressed BCMA of myeloma (claims 35-38) or the autoimmune disease systemic lupus erythematosus (claim 39) in a subject by administering a pharmaceutical composition comprising an ADC of:
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wherein y is 8 (claim 25) and a pharmaceutically acceptable excipient, wherein the antibody Ab2 is comprised of an humanized (claim 26) anti-BCMA antibody Ab2 comprised a heavy chain of ‘168 SEQ ID NO:16 and a light chain of ‘168 SEQ ID NO:19, which is identical to a heavy chain of instant SEQ ID NO:16 and a light chain of instant SEQ ID NO:19 (claims 29-30 and 32) and is further comprised of a heavy chain constant region of instant SEQ ID NO:22 and a light chain constant region of instant SEQ ID NO:23 (claim 27), a VH of instant SEQ ID NO:10 and a light chain of instant SEQ ID NO:13 (claim 28) and a VH comprising instant SEQ ID NO:3-5 and a VL comprising instant SEQ ID NO:6-8 (claim 24).
Claims 16-23, 31, and 33-34 are rejected under 35 U.S.C. 103 as being unpatentable over CN 111689980 A (Qin W et al.), Talele TT et al. (J. Med. Chem. 2016, 59, 19, 8712–8756), and US 2017/0252458 (Albone EF et al.), and evidenced by translated CN 111689980 A (Qin W et al.)
‘980 translated taught conjugation of compound 11 with the structure of
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(page 8) to an antibody Ab-C which resulted in an ADC of C-11 (pages 13-14 bridging paragraph). ‘980 translated taught ADC C-11 was dose-dependently effective against cancer cells in cell based assays and that a method of administration of a pharmaceutical composition comprising ADC C-11 and a pharmaceutically acceptable diluent to a subject with cancer was effective in vivo (page 14, paragraphs 2-5 and the second-forth tables). ‘980 translated taught compound 2
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(page 7) and compound 28
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(page 11) were dose-dependently effective against cancer cells (page 13 Table). ‘980 translated taught the antibody drug conjugate as equation II Ab-(-L-D)m wherein m is 1-20, wherein the linking unit L comprises a (PEG)n2 wherein n2 is 1-20 (page 3).
‘980 did not teach: 1) methyl cyclopropyl group to be a flat planar bond in an ADC; and 2) a single embodiment of a -(CH2)2-O-(CH2)2-O-(CH2)2- linker attached to the maleimide, but this is obvious in view of Talele and ‘458.
Talele taught exchange of an aryl cyclohexane for a cyclopropyl group leads to a more effective compound (Fig. 2). Talele taught the cyclopropyl ring addresses multiple roadblocks that can occur during drug discovery such as (a) enhancing potency, (b) reducing off-target effects, (c) increasing metabolic stability, (d) increasing brain permeability, (e) decreasing plasma clearance, (f) contributing to an entropically more favorable binding to the receptor, (g) conformational restriction of peptides/ peptidomimetics to prevent proteolytic hydrolysis, and (h) altering drug pKa to reduce its P-glycoprotein efflux ratio.
‘458 taught an ADC, MORAb003-ER1231679, comprising an antibody MORAb003 and the structure:
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, wherein MORAb003-ER1231679 effectively kills cancer cells dose-dependently (page 115, Table 48). ‘458 taught MORAb003-ER1231679 had a drug to antibody conjugate ratio of about 4 (page 112, Table 47).
Regarding claims 21, 23, 31, and 34, it would have been obvious for a person having ordinary skill in the art to take the method of ‘980 for treating cancer in a subject by administering a pharmaceutical composition comprising ADC C-11 and a pharmaceutically acceptable diluent – and:
exchange the methyl group in the ADC linker for a methyl cyclopropyl group with a flat planar bond in view of ‘980 and Talele
exchange the linker connecting the maleimide and the GGFG linker for -(CH2)2-O-(CH2)2-O-(CH2)2- in view of ‘458;
exchange the drug to antibody ratio number n for n of between 1 and 20 which includes 4, as taught by ‘980.
This is obvious because: 1a) ‘980 taught the exatecan compounds that have a methyl or methyl benzene are dose-dependently active against cancer cells, wherein the bond is in different planes; 1b) Talele taught exchange of an aryl cyclohexane for a cyclopropyl group leads to a more effective compound and has several benefits; 2a) MORAb003-ER1231679 taught an linker of -(CH2)2-O-(CH2)2-O-(CH2)2- connecting the maleimide and the peptide linker is effective; 2b) ‘980 taught (PEG)n linker embodiments within the ADC; and 3) ‘980 translated taught the antibody drug conjugate as equation II Ab-(-L-D)m wherein m is 1-20 and ‘458 taught an ADC of MORAb003-ER1231679 with a drug to antibody ratio of 4 was effective.
There is a reasonable expectation of success because: 1a) ‘980 taught the exatecan compounds that have a methyl or methyl benzene are dose-dependently active against cancer cells, wherein the bond is in different planes; 1b) Talele taught exchange of an aryl cyclohexane for a cyclopropyl group leads to a more effective compound and has several benefits; 2) MORAb003-ER1231679 taught an linker of -(CH2)2-O-(CH2)2-O-(CH2)2- connecting the maleimide and the peptide linker is effective; 3) ‘458 taught an ADC of MORAb003-ER1231679 with a drug to antibody ratio of 4 was effective.
This would produce a method for treating cancer in a subject by administering a pharmaceutical composition comprising an ADC of:
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(claim 21, 23, and 31) and a pharmaceutically acceptable diluent (claim 34). This meets the claim limitations of claims 21, 23, 31, and 34.
Regarding claims 16-20, 22, and 33, it would have been obvious for a person having ordinary skill in the art to take the ADC of ‘980, Talele, and ‘458 above and: 1) produce the ADC above by a method of reacting a maleimide containing compound with an antibody of Ab-C as taught by ‘980 which would require the maleimide compound
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and the antibody Ab-C.
This is obvious with a reasonable expectation of success because: 1) ‘980 taught a method of producing ADC C-11 wherein the antibody was reacted with compound 11 and the method effectively produced the ADC.
This would produce a method of producing and ADC wherein the method comprised reacting the antibody Ab-C with the compound
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(claim 16-20) to produce the ADC of
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(claims 22 and 33). This meets the claim limitations of claims 16-20, 22, and 33.
Claims 16-39 are rejected under 35 U.S.C. 103 as being unpatentable over CN 111689980 A(Qin W et al.), Talele TT et al. (J. Med. Chem. 2016, 59, 19, 8712–8756), and US 2017/0252458 (Albone EF et al.) as applied to claims 16-23, 31, and 33-34 above, and further in view of WO 2021/018168 ( Hua H et al.) and evidenced by translated WO 2021/018168 (Hua H et al.).
‘980, Talele, and ‘458 are described above.
‘980, Talele, and ‘458 did not teach an anti-BCMA ADC or treatment with an anti- BCMA, but this is obvious in view of ‘168.
‘168 translated taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 (page 16, Table 5). ‘168 taught an ADC comprising Ab2 was effective when administered to subjects with cancer, wherein the cancer was NCI-929 myeloma (page 21-22, Table 10, [0290-0295]). ‘168 translated taught BCMA is highly expressed in multiple myeloma (page 2, [0003]). ‘168 translated taught cancers and autoimmune diseases involving B cells can be considered abnormal B cell function, so a possible strategy to control these diseases is to use antibodies that target pathological B cells (page 2, [0002]). ‘168 translated taught the autoimmune disease systemic lupus erythematosus involves B cells (page 2, [0002]). ‘168 translated taught the use of antibody-drug conjugates for the treatment of BCMA-mediated diseases or conditions, wherein the autoimmune disease is lupus erythematosus (page 7, [0106]).
Regarding claims 24-30, 32, and 35-39, it would have been obvious for a person having ordinary skill in the art to take the method for treating cancer in a subject by administering a pharmaceutical composition comprising an ADC of:
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and a pharmaceutically acceptable diluent of ‘980, Talele, and ‘458 – and:
1) exchange the Ab-C targeting antibody for the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19;
2) treat the BCMA mediated cancer myeloma that expressed BCMA; and
3) treat the BCMA mediated autoimmune disease lupus erythematosus that expressed BCMA, in view of ‘168
This is obvious because: 1-2) ‘168 taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 and was effective when administered to subjects with myeloma and BCMA is highly expressed in multiple myeloma; 3a) ‘168 taught autoimmune diseases involving B cells can be considered abnormal B cell function, so a possible strategy to control these diseases is to use antibodies that target pathological B cells, wherein the autoimmune disease systemic lupus erythematosus involves B cells; and 3b) ‘168 taught the use of antibody-drug conjugates for the treatment of BCMA-mediated diseases or conditions, wherein the autoimmune disease is lupus erythematosus.
There is a reasonable expectation of success because: 1-2) ‘168 taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 and was effective when administered to subjects with myeloma and BCMA is highly expressed in multiple myeloma; 3) Abnormal B cells of subjects with the autoimmune disease systemic lupus erythematosus that express BCMA would be targeted by the ADC and killed which would treat the disease.
This would produce a method of treating BCMA mediated diseases that expressed BCMA of myeloma (claims 35-38) or the autoimmune disease systemic lupus erythematosus (claim 39) in a subject by administering a pharmaceutical composition comprising an ADC of:
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wherein y is 4 (claim 25) and a pharmaceutically acceptable excipient, wherein the antibody Ab2 is comprised of an humanized (claim 26) anti-BCMA antibody Ab2 comprised a heavy chain of ‘168 SEQ ID NO:16 and a light chain of ‘168 SEQ ID NO:19, which is identical to a heavy chain of instant SEQ ID NO:16 and a light chain of instant SEQ ID NO:19 (claims 29-30 and 32) and is further comprised of a heavy chain constant region of instant SEQ ID NO:22 and a light chain constant region of instant SEQ ID NO:23 (claim 27), a VH of instant SEQ ID NO:10 and a light chain of instant SEQ ID NO:13 (claim 28) and a VH comprising instant SEQ ID NO:3-5 and a VL comprising instant SEQ ID NO:6-8 (claim 24).
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.
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Claims 16-23, 31, and 33-34 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5-6, 11-13, 54, 61-70 of copending Application No. 17/596239 in view of US 2017/0252458 (Albone EF et al.).
Copending claims 1 and 54 of ‘239 taught an ADC comprising the structure:
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, wherein y is from 1-20, wherein the Ab targets B7-H7 , wherein copending claim 61 further taught the ADC in a pharmaceutical composition with a pharmaceutically acceptable carrier, wherein copending claims 5-6, 11-13, and 64-70 further taught antibody details, wherein claim 62 taught a method from treating a disease related to B7-H7 in a subject comprising administering to the subject the ADC of copending claim 1, wherein the cancer being treated is myeloma in copending claim 63.
The claims of ‘239 did not teach: 1) a -(CH2)2-O-(CH2)2-O-(CH2)2- linker attached to the maleimide, but this is obvious in view of ‘458.
‘458 taught an ADC, MORAb003-ER1231679, comprising an antibody MORAb003 and the structure:
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, wherein MORAb003-ER1231679 effectively kills cancer cells dose-dependently (page 115, Table 48). ‘458 taught MORAb003-ER1231679 had a drug to antibody conjugate ratio of about 4 (page 112, Table 47). ‘458 taught cysteine conjugation using maleimides for MORAb003 (pages 107-108, [0421-0422] and Fig. 1)
Regarding claims 21, 23, 31, and 34, it would have been obvious for a person having ordinary skill in the art to take copending claims 1, 54, 61-63 of ‘239 of a method from treating a disease related to B7-H7 in a subject comprising administering to the subject a pharmaceutical composition with a pharmaceutically acceptable carrier comprising an ADC comprising the structure:
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, wherein y is from 1-20, wherein the Ab targets B7-H7, wherein the cancer being treated is myeloma – and:
exchange the linker connecting the maleimide and the GGFG linker for -(CH2)2-O-(CH2)2-O-(CH2)2- in view of ‘458;
exchange the drug to antibody ratio number n for 4, as taught by ‘458.
This is obvious because: 1) ‘458 taught an ADC of MORAb003-ER1231679 with a linker of -(CH2)2-O-(CH2)2-O-(CH2)2- connecting the maleimide and the peptide linker is effective; and 3) ‘458 taught an ADC of MORAb003-ER1231679 with a drug to antibody ratio of 4 was effective.
There is a reasonable expectation of success because: 1) ‘458 taught an ADC of MORAb003-ER1231679 with a linker of -(CH2)2-O-(CH2)2-O-(CH2)2- connecting the maleimide and the peptide linker is effective; and 3) ‘458 taught an ADC of MORAb003-ER1231679 with a drug to antibody ratio of 4 was effective.
This would produce a method for treating cancer in a subject by administering a pharmaceutical composition comprising an ADC with an anti-B7-H7 antibody of MORAb003 and a structure of:
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(claim 21, 23, and 31) and a pharmaceutically acceptable carrier (claim 34). This meets the claim limitations of claims 21, 23, 31, and 34.
Regarding claims 16-20, 22, and 33, it would have been obvious for a person having ordinary skill in the art to take the method of ADC of ‘458 above and: 1) produce the ADC above by a method of reacting a maleimide containing compound with an antibody of MORAb003 as taught by ‘458 which would require the maleimide compound
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and the anti-B7-H7 antibody MORAb003.
This is obvious with a reasonable expectation of success because: 1) ‘458 taught a method of producing MORAb003-ER1231679 wherein the antibody was reacted with ER1231679 and the method effectively produced the ADC.
This would produce a method of producing and ADC wherein the method comprised reacting the antibody MORAb003 with the compound
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(claim 16-20) to produce the ADC of
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(claims 22 and 33). This meets the claim limitations of claims 16-20, 22, and 33.
This is a provisional nonstatutory double patenting rejection.
Claims 16-39 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5-6, 11-13, 54, 61-70 of copending Application No. 17/596239 in view of US 2017/0252458 (Albone EF et al.) and WO 2021/018168 (Hua H et al.) and evidenced by translated WO 2021/018168 (Hua H et al.).
The claims of copending ‘239 in view of ‘458 teach the limitations of claims 16-23, 31, and 33-34 for the reasons set forth above.
Copending ‘239 and ‘458 are described above.
Copending ‘239 did not teach an anti-BCMA ADC or treatment with an anti- BCMA, but this is obvious in view of ‘168.
‘168 translated taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 (page 16, Table 5). ‘168 taught an ADC comprising Ab2 was effective when administered to subjects with cancer, wherein the cancer was NCI-929 myeloma (page 21-22, Table 10, [0290-0295]). ‘168 translated taught BCMA is highly expressed in multiple myeloma (page 2, [0003]). ‘168 translated taught cancers and autoimmune diseases involving B cells can be considered abnormal B cell function, so a possible strategy to control these diseases is to use antibodies that target pathological B cells (page 2, [0002]). ‘168 translated taught the autoimmune disease systemic lupus erythematosus involves B cells (page 2, [0002]). ‘168 translated taught the use of antibody-drug conjugates for the treatment of BCMA-mediated diseases or conditions, wherein the autoimmune disease is lupus erythematosus (page 7, [0106]).
Regarding claims 24-30, 32, and 35-39, it would have been obvious for a person having ordinary skill in the art to take the method of copending claims 1, 54, 61-63 of ‘239 and ‘458 for a method for treating cancer in a subject by administering a pharmaceutical composition comprising an ADC with an anti-B7-H7 antibody of MORAb003 and a structure of:
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and a pharmaceutically acceptable carrier – and:
1) exchange the Ab-C targeting antibody for the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19;
2) treat the BCMA mediated cancer myeloma that expressed BCMA; and
3) treat the BCMA mediated autoimmune disease lupus erythematosus that expressed BCMA, in view of ‘168
This is obvious because: 1-2) ‘168 taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 and was effective when administered to subjects with myeloma and BCMA is highly expressed in multiple myeloma; 3a) ‘168 taught autoimmune diseases involving B cells can be considered abnormal B cell function, so a possible strategy to control these diseases is to use antibodies that target pathological B cells, wherein the autoimmune disease systemic lupus erythematosus involves B cells; and 3b) ‘168 taught the use of antibody-drug conjugates for the treatment of BCMA-mediated diseases or conditions, wherein the autoimmune disease is lupus erythematosus.
There is a reasonable expectation of success because: 1-2) ‘168 taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 and was effective when administered to subjects with myeloma and BCMA is highly expressed in multiple myeloma; 3) Abnormal B cells of subjects with the autoimmune disease systemic lupus erythematosus that express BCMA would be targeted by the ADC and killed which would treat the disease.
This would produce a method of treating BCMA mediated diseases that expressed BCMA of myeloma (claims 35-38) or the autoimmune disease systemic lupus erythematosus (claim 39) in a subject by administering a pharmaceutical composition comprising an ADC of:
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wherein y is 4 (claim 25) and a pharmaceutically acceptable excipient, wherein the antibody Ab2 is comprised of an humanized (claim 26) anti-BCMA antibody Ab2 comprised a heavy chain of ‘168 SEQ ID NO:16 and a light chain of ‘168 SEQ ID NO:19, which is identical to a heavy chain of instant SEQ ID NO:16 and a light chain of instant SEQ ID NO:19 (claims 29-30 and 32) and is further comprised of a heavy chain constant region of instant SEQ ID NO:22 and a light chain constant region of instant SEQ ID NO:23 (claim 27), a VH of instant SEQ ID NO:10 and a light chain of instant SEQ ID NO:13 (claim 28) and a VH comprising instant SEQ ID NO:3-5 and a VL comprising instant SEQ ID NO:6-8 (claim 24).
This is a provisional nonstatutory double patenting rejection.
Claims 21, 23, and 31 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 18/694370. Although the claims at issue are not identical, they are not patentably distinct from each other because:
Regarding claims 21, 23, and 31, copending claim 12 of ‘370 taught an ADC comprising the structure:
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, wherein y is from 1-20, wherein the antibody targets Trop-2. This meets the claim limitation of instant claims 21, 23, and 31.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 16-39 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 18/694370 in view of WO 2021/018168 (Hua H et al.) and evidenced by translated WO 2021/018168 (Hua H et al.).
The claims of copending ‘370 teach the limitations of claims 21, 23, and 31 for the reasons set forth above.
Copending claims 1-12 taught species of an ADC of formula (I)
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wherein y is from 1-20. Copending claim 12 of ‘370 taught an ADC comprising the structure:
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, wherein y is from 1-20, wherein the antibody targets Trop-2, wherein copending claim 14 further taught the ADC in a pharmaceutical composition with a pharmaceutically acceptable carrier.
Copending claim 13 taught a method for preparing an ADC of formula (I) comprising the steps
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.
Copending claim 15 taught a method from treating a TROP-2 related disease in a subject comprising administering to the subject an effective amount of the ADC of copending claim 1 with a pharmaceutically acceptable carrier, wherein the cancer being treated is myeloma in copending claim 16.
The claims of ‘370 did not teach: 1) an anti-BCMA ADC or treatment with an anti- BCMA, but this is obvious in view of ‘168.
‘168 translated taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 (page 16, Table 5). ‘168 taught an ADC comprising Ab2 was effective when administered to subjects with cancer, wherein the cancer was NCI-929 myeloma (page 21-22, Table 10, [0290-0295]). ‘168 translated taught BCMA is highly expressed in multiple myeloma (page 2, [0003]). ‘168 translated taught cancers and autoimmune diseases involving B cells can be considered abnormal B cell function, so a possible strategy to control these diseases is to use antibodies that target pathological B cells (page 2, [0002]). ‘168 translated taught the autoimmune disease systemic lupus erythematosus involves B cells (page 2, [0002]). ‘168 translated taught the use of antibody-drug conjugates for the treatment of BCMA-mediated diseases or conditions, wherein the autoimmune disease is lupus erythematosus (page 7, [0106]).
Regarding claims 24-30, 32, and 34-39, it would have been obvious for a person having ordinary skill in the art to take copending claims 11, 14-16 of ‘370 of a method from treating a disease related to Trop-2 in a subject comprising administering to the subject a pharmaceutical composition with a pharmaceutically acceptable carrier comprising an ADC comprising the structure:
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, wherein y is from 1-20, wherein the Ab targets Trop-2, wherein the cancer being treated is myeloma – and:
1) exchange the targeting antibody for the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19;
2) treat the BCMA mediated cancer myeloma that expressed BCMA; and
3) treat the BCMA mediated autoimmune disease lupus erythematosus that expressed BCMA, in view of ‘168
This is obvious because: 1-2) ‘168 taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 and was effective when administered to subjects with myeloma and BCMA is highly expressed in multiple myeloma; 3a) ‘168 taught autoimmune diseases involving B cells can be considered abnormal B cell function, so a possible strategy to control these diseases is to use antibodies that target pathological B cells, wherein the autoimmune disease systemic lupus erythematosus involves B cells; and 3b) ‘168 taught the use of antibody-drug conjugates for the treatment of BCMA-mediated diseases or conditions, wherein the autoimmune disease is lupus erythematosus.
There is a reasonable expectation of success because: 1-2) ‘168 taught the anti-BCMA antibody Ab2 comprised a heavy chain of SEQ ID NO:16 and a light chain of SEQ ID NO:19 and was effective when administered to subjects with myeloma and BCMA is highly expressed in multiple myeloma; 3) Abnormal B cells of subjects with the autoimmune disease systemic lupus erythematosus that express BCMA would be targeted by the ADC and killed which would treat the disease.
This would produce a method of treating BCMA mediated diseases that expressed BCMA of myeloma (claims 35-38) or the autoimmune disease systemic lupus erythematosus (claim 39) in a subject by administering a pharmaceutical composition comprising an ADC of:
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wherein y is 1-20, which includes 4 (claim 25) and a pharmaceutically acceptable carrier (claim 34), wherein the antibody Ab2 is comprised of an humanized (claim 26) anti-BCMA antibody Ab2 comprised a heavy chain of ‘168 SEQ ID NO:16 and a light chain of ‘168 SEQ ID NO:19, which is identical to a heavy chain of instant SEQ ID NO:16 and a light chain of instant SEQ ID NO:19 (claims 29-30 and 32) and is further comprised of a heavy chain constant region of instant SEQ ID NO:22 and a light chain constant region of instant SEQ ID NO:23 (claim 27), a VH of instant SEQ ID NO:10 and a light chain of instant SEQ ID NO:13 (claim 28) and a VH comprising instant SEQ ID NO:3-5 and a VL comprising instant SEQ ID NO:6-8 (claim 24).
Regarding claims 16-20, 22, and 33, it would have been obvious for a person having ordinary skill in the art to take the method of ADC of ‘370 and ‘168 above and: 1) produce the ADC above by a method of reacting a maleimide containing compound with an antibody of Ab2 as taught by ‘370 copending claim 13 which would require the maleimide compound
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and the anti-BCMA antibody Ab2.
This is obvious with a reasonable expectation of success because: 1) ‘370 taught a method of producing an ADC wherein the antibody was reacted with a maleimide comprising structure and maleimides are known to react with antibodies to form an ADC.
This would produce a method of producing and ADC wherein the method comprised reacting the antibody Ab2 with the compound
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(claim 16-20) to produce the ADC of
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(claims 22 and 33). This meets the claim limitations of claims 16-20, 22, and 33.
This is a provisional nonstatutory double patenting rejection.
Conclusion
Claims 16-39 are rejected
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/J.J.S./Examiner, Art Unit 1643
/Karen A. Canella/Primary Examiner, Art Unit 1643