DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant's arguments filed 6/23/2026 have been fully considered but they are not persuasive.
Claims 4, 8, 14, 18-19, and 26 have been cancelled. Claim 27 has been newly added.
Election/Restrictions
Applicant’s election without traverse of an antigen binding domain against CD20 (see instant claims 1 and 17) in the reply filed on 8/1/2024 is again acknowledged. CD20 is the elected antigen binding domain species in the claimed antibody constructs.
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.
Claims 1-3, 5-7, 9, 15-17, and 20-25 are rejected under 35 U.S.C. 103 as being unpatentable over Masternak et al. (U.S. Patent Application Publication 2014/0303354) in view of Lohse et al., Grosveld et al. (U.S. Patent No. 9,650,441), and Oestergaard et al. (U.S. Patent No. 11,597,772).
Masternak et al. discloses bispecific antibodies that bind to two antigens on the surface of a cell resulting in additive or synergistic increase of affinity due to an avidity mechanism. One arm binding with high affinity to a tumor associated antigen (TAA) such as CD19 and a second arm binding with lower affinity to CD47 (but sufficient to inhibit CD47/SIRPα) upon TAA co-engagement should allow preferential inhibition of CD47 in cancer versus normal cells. The CD47 antibodies 5A3M3 and 5A3M5 antibodies are disclosed. These antibodies were engineered to have decreased affinity toward the CD47 target. See at least paragraph [0382] and instant claim 25. Bispecific antibodies having tandem scFv formats are disclosed. Antibodies having IgA antibody constant regions are disclosed. See at least paragraph [0249]. Using antibody binding domains directed to other TAAs such as CD20, EGFR, HER2, CD30, HER3, and PSMA is also disclosed. The affinity of the anti-CD47 antibody for CD47 can be decreased relative to the affinity for the second antibody to its target. See at least paragraph [0016]. The bispecific antibodies can be in any format known in the art. See at least paragraph [0051]. See also at least paragraphs [0009-0010, 0013, 0040, 0051, 0092, 0396], Table 4, Example 11, and at least claims 4-6 and 17.
Lohse et al. discloses mutating amino acid positions in the IgA2m(1) constant domain to improve pharmacokinetic properties, including improved serum half-life. Removing N-linked glycosylation sites by mutating asparagine residues is disclosed. The resulting IgA2.0 constant domain mutations included N166G, P221R, N337T, I338L, T339S, and C331S as well as deletion of the C-terminal cysteine (C, dC471) and tyrosine (Y, dY472) amino acids. See at least abstract, Figures 1A-B, and pages 404-405 and 414. The hIgA2m(1) sequence containing instant SEQ ID NO: 39 and the mutated hIgA2.0 sequence are found in Figure 1A. This disclosure meets the limitations in instant claim 1 wherein the IgA heavy chain constant domain lacks at least one naturally occurring glycosylation site and at least two naturally occurring asparagine (N) amino acid residues (i.e. N166G and N337T). This disclosure meets the limitation in instant claim 20 wherein the IgA heavy chain constant domain lacks at least one naturally occurring cysteine (C) amino acid residue (i.e. C331S and dC471). This disclosure meets the limitation in instant claim 21 wherein the IgA heavy chain constant domain lacks at least one naturally occurring tyrosine (Y) amino acid residue (i.e. dY472). This disclosure meets the limitation in instant claim 22 wherein the IgA heavy chain constant domain lacks at least one naturally occurring threonine (T) amino acid residue (i.e. T339S). This disclosure meets the limitation in instant claim 23 wherein the IgA heavy chain constant domain lacks at least one naturally occurring isoleucine (I) amino acid residue (i.e. I338L). This disclosure meets the limitation in instant claim 24 wherein the IgA heavy chain constant domain lacks at least one naturally occurring proline (P) amino acid residue (i.e. P221R).
Grosveld et al. discloses bispecific antibodies of CD47 and CD20. The amino acid sequences of the anti-CD47 antibody named 2.3D11 are disclosed. See at least column 3, lines 12-20; column 4, lines 19-33; and column 18, line 41, through column 21. SEQ ID NO: 4 corresponds to instant SEQ ID NO: 26. SEQ ID NO: 6 corresponds to instant SEQ ID NO: 23. The anti-CD20 antibody Obinutuzumab is disclosed. See column 38, lines 4-5. Pharmaceutical compositions are disclosed. See at least column 30, line 50, through column 33, line 17. Binding to target and immune cells where the bispecific antibody bind the Fc receptor on the immune cell is disclosed. See at least column 6, lines 28-49, and column 37, lines 26-47. Use of heavy chain constant domains from IgA1 or IgA2 is disclosed. See at least column 4, lines 40-45. See also at least column 17, line 30, through, column 18, line 15.
Oestergaard et al. (U.S. Patent No. 11,597,772) discloses the light chain and heavy chain amino acid sequences for the anti-CD20 antibody Obinutuzumab. The VH and VL sequences are identified. See at least columns 27 and 59-62 and SEQ ID NOS: 1-2 and 5-6. The VH and VL sequences in SEQ ID NOS: 1-2 and 5-6 correspond to the VH and VL sequences of instant SEQ ID NOS: 22 and 25, respectively, for Obinutuzumab. See at least instant claims 6 and 9.
It would have been obvious to produce an antibody construct as disclosed by Masternak et al. to produce a bispecific CD47 and CD20 antibody as suggested by Grosveld et al. using the anti-CD47 antibody 2.3D11 of Grosveld et al. and the anti-CD20 antibody of Obinutuzumab as disclosed by Oestergaard et al. The CD47 antibodies 5A3M3 and 5A3M5 antibodies of Masternak et al. could also be used. Using IgA heavy chain constant domains is disclosed by Masternak et al. with Grosveld et al. specifically suggesting IgA1 or IgA2 heavy chain constant domains and Lohse et al. discloses an IgA2.0 heavy chain constant domain having mutations as recited in instant claims 1 and 20-24 that provides improved pharmacokinetic properties. IgA2.0 of Lohse et al. is a variant of IgA1 and IgA2m(1). See instant claims 15-16. Masternak et al. teaches the advantages of bispecific antibodies binding with high affinity to a tumor associated antigen (TAA) such as CD19 or CD20 and with lower affinity to CD47 (but sufficient to inhibit CD47/SIRPα).
The 2.3D11 antibody is the CD47 binding domain of claim 1, part (b). Its light chain CDR sequences are recited in instant claim 2 and its VL sequence is recited in instant claim 3. Its heavy chain CDR sequences are recited in instant claim 2 and its VH sequence is recited in instant claim 5.
Obinutuzumab (binding to CD20) is the elected antigen binding domain of instant claim 1, part (c), and instant claim 17. Its light chain CDR sequences are recited in instant claim 6 and its VL is recited in instant claim 7. Its heavy chain CDR sequences are recited in instant claim 6 and its VH sequence is recited in instant claim 9.
One would have been motivated to produce the suggested antibody construct as the prior art references suggest the usefulness of such antibody constructs and the improved pharmacokinetic properties for the IgA2.0 heavy chain constant domain of Lohse et al..
The binding affinity limitations in instant claim 1 would be characteristic properties of the antibodies suggested by the combination of Masternak et al., Lohse et al., Grosveld et al., Oestergaard et al. and as the specific antibody sequences in the instant dependent claims must provide these properties and the prior art suggests making bispecific antibodies using these sequences. This assertion is supported by the constructs exemplified in the instant specification. See at least for example instant Table 1 and Figures 6A-B. Should applicant argue that this would not be a property of the antibodies suggested by the prior art, this will be viewed as an admission that the antibody constructs of the instant claims are not adequately described or enabled.
Note that instant claim 1 includes any bispecific antibody format. Many bispecific antibody structures would have been known. Instant claim 1 does not indicate how the IgA heavy chain constant domain, the first light chain variable domain, the first heavy chain variable domain, the second light chain variable domain, and the second heavy chain variable domain are associated or assembled or fused. The N- and C-terminus limitations do not indicate any particular order of assembly of the claimed antibody construct. The instant claims include antibodies with two arms, one for CD47 and one for CD19 or CD20. The instant claims include tandem scFv (with heavy and light chain variable domains) fused to the IgA heavy chain constant domains.
Claims 1 and 10-13 are rejected under 35 U.S.C. 103 as being unpatentable over Masternak et al. (U.S. Patent Application Publication 2014/0303354) in view of Lohse et al., Grosveld et al. (U.S. Patent No. 9,650,441), and Oestergaard et al. (U.S. Patent No. 11,597,772). as applied to claims 1-3, 5-7, 9, 15-17, and 20-25 above, and further in view of Wu et al. (U.S. Patent Application Publication 2009/0215992).
Masternak et al., Lohse et al., Grosveld et al., and Oestergaard et al. are applied as above. They do not disclose the particular structure recited in instant claim 10.
Wu et al. discloses a bispecific antibody in a DVD-Ig format. See at least Figure 1A-B. This structure corresponds to that of instant claim 10 where VHB corresponds to the second VH (against CD20), VLB corresponds to the second VL (against CD20), VHA corresponds to the first VH (against CD47), and VLA corresponds to the first VL (against CD47). The use of IgA heavy chain constant domains is disclosed. See at least paragraphs [0044 and 0065]. Linkers such as GGGGSGGGGSGGGGS (corresponding to instant SEQ ID NO: 45 and comprising instant SEQ ID NO: 44) are disclosed. See at least paragraph [0013] and SEQ ID NO: 130.
It would have been obvious to produce an antibody construct as disclosed by Masternak et al. in the bispecific antibody format disclosed by Wu et al. to produce a bispecific CD47 and CD20 antibody as suggested by Grosveld et al. using the anti-CD47 antibody 2.3D11 of Grosveld et al. and the anti-CD20 antibody of Obinutuzumab as disclosed by Oestergaard et al. The CD47 antibodies 5A3M3 and 5A3M5 antibodies of Masternak et al. could also be used. Using IgA heavy chain constant domains is disclosed by Wu et al. and Masternak et al. with Grosveld et al. specifically suggesting IgA1 or IgA2 heavy chain constant domains and Lohse et al. discloses an IgA2.0 heavy chain constant domain having mutations as recited in instant claims 1 and 20-24 that provides improved pharmacokinetic properties. IgA2.0 of Lohse et al. is a variant of IgA1 and IgA2m(1). See instant claims 15-16. Masternak et al. teaches the advantages of bispecific antibodies binding with high affinity to a tumor associated antigen (TAA) such as CD19 or CD20 and with lower affinity to CD47 (but sufficient to inhibit CD47/SIRPα). Masternak et al. discloses that any known bispecific antibody format could be used and Wu et al. provides a known bispecific antibody format.
The first and second polypeptide structures and linkers of claims 10-11 are suggested by Wu et al. when the 2.3D11 (anti-CD47) and Obinutuzumab (anti-CD20) antibody sequences are used. Fusing the Obinutuzumab VH to the 2.3D11 VH with Wu's linker of SEQ ID NO: 130 would result in a sequence having at least 90% identity to instant SEQ ID NO: 29 in instant claim 12. Fusing the Obinutuzumab VL to the 2.3D11 VL with Wu’s linker of SEQ ID NO: 130 would result in a sequence having at least 90% identity to instant SEQ ID NO: 31 in instant claim 13.
Claims 1 and 27 are rejected under 35 U.S.C. 103 as being unpatentable over Masternak et al. (U.S. Patent Application Publication 2014/0303354) in view of Lohse et al., Grosveld et al. (U.S. Patent No. 9,650,441), and Oestergaard et al. (U.S. Patent No. 11,597,772). as applied to claims 1-3, 5-7, 9, 15-17, and 20-25 above, and further in view of Brinkmann et al.
Masternak et al., Lohse et al., Grosveld et al., and Oestergaard et al. are applied as above. They do not disclose the particular structure recited in instant claim 27.
Brinkmann et al. discloses a bispecific antibody in scFv-HC-Ig format. Linkers such as (G4S)2 and (G4S)3 are disclosed. The linker GGGGSGGGGSGGGGS corresponds to instant SEQ ID NO: 45 and comprises instant SEQ ID NO: 44. The linker GGGGSGGGGS also comprises instant SEQ ID NO: 44. See at least Figure 2, Box 10, construct seventh from left and pages 195-196. This construct corresponds to that of instant claim 27 reciting SEQ ID NO: 33 and SEQ ID NO: 34.
In the N- to C-terminus direction, SEQ ID NO: 33 (377 amino acids) has an scFv for the anti-CD20 antibody obinutuzumab (VH fused to linker fused to VL) fused to linker fused to VH for the anti-CD47 antibody 2.3D11.
SEQ ID NO: 22 (obinutuzumab VH) corresponds to amino acids 1-119 of SEQ ID NO: 33, SEQ ID NO: 45 (the (G4S)3 linker) corresponds to amino acids 120-134 of SEQ ID NO: 33, SEQ ID NO: 25 (obinutuzumab VL) corresponds to amino acids 135-246 of SEQ ID NO: 33, SEQ ID NO: 44 (SGGGGS linker) corresponds to amino acids 247-252 of SEQ ID NO: 33, and SEQ ID NO: 23 corresponds to amino acids 253-377 of SEQ ID NO: 33. See Tables 5, 6, 8, and 11.
In the N- to C-terminus direction, SEQ ID NO: 34 (364 amino acids) has an scFv for the anti-CD47 antibody 5A3M5 (VH fused to linker fused to VL) fused to linker fused to VH for the anti-CD20 antibody obinutuzmab.
SEQ ID NO: 24 (5A3M5 VH) corresponds to amino acids 1-116 of SEQ ID NO: 34, SEQ ID NO: 45 (the (G4S)3 linker) corresponds to amino acids 117-131 of SEQ ID NO: 34, SEQ ID NO: 27 (5A3M5 VL) corresponds to amino acids 132-239 of SEQ ID NO: 34, SEQ ID NO: 44 (SGGGGS linker) corresponds to amino acids 240-245 of SEQ ID NO: 34, and SEQ ID NO: 22 (obinutuzumab VH) corresponds to amino acids 246-364 of SEQ ID NO: 34. See Tables 5, 6, 8, and 11.
It would have been obvious to produce an antibody construct as disclosed by Masternak et al. in the bispecific antibody format disclosed by Brinkman et al. to produce a bispecific CD47 and CD20 antibody as suggested by Grosveld et al. using the anti-CD47 antibody 2.3D11 of Grosveld et al. and the anti-CD20 antibody of Obinutuzumab as disclosed by Oestergaard et al. The CD47 antibodies 5A3M3 and 5A3M5 antibodies of Masternak et al. could also be used. Using IgA heavy chain constant domains is disclosed by Masternak et al. with Grosveld et al. specifically suggesting IgA1 or IgA2 heavy chain constant domains and Lohse et al. discloses an IgA2.0 heavy chain constant domain having mutations as recited in instant claims 1 and 20-24 that provides improved pharmacokinetic properties. IgA2.0 of Lohse et al. is a variant of IgA1 and IgA2m(1). See instant claims 15-16. Masternak et al. teaches the advantages of bispecific antibodies binding with high affinity to a tumor associated antigen (TAA) such as CD19 or CD20 and with lower affinity to CD47 (but sufficient to inhibit CD47/SIRPα). Masternak et al. discloses that any known bispecific antibody format could be used and Brinkmann et al. provides a known bispecific antibody format.
The structures of SEQ ID NOS: 33 and 34 in instant claim 27 (and as described above) are suggested by the scFv-HC-Ig construct of Brinkmann et al. and using the sequences of Masternak et al., Lohse et al., Grosveld et al., and Oestergaard et al. for the different segments as discussed above would result in sequences having at least 90% identity to instant SEQ ID NOS: 33 and 34.
Applicant’s arguments are not persuasive. Applicant is arguing the references individually and not for what they collectively teach. The prior art as a whole suggests antibodies having the recited structures. The prior art as a whole provides motivation and an expectation of success for producing such antibodies. In particular, using the claimed IgA constant domains is suggested by the prior art. As a product and its properties cannot be separated, the suggested antibodies would have been expected to have the functions recited in claim 1. This assertion is supported by the constructs exemplified in the instant specification. See at least for example instant Example 4, Table 1, and Figures 6A-B.
To the degree that applicant is arguing improper hindsight reasoning, this is not persuasive. Applicant is reminded that "[a]ny judgment on obviousness is in a sense necessarily a reconstruction based on hindsight reasoning, but so long as it takes into account only knowledge which was within the level of ordinary skill in the art at the time the claimed invention was made and does not include knowledge gleaned only from applicant's disclosure, such a reconstruction is proper." In re McLaughlin, 443 F.2d 1392, 1395, 170 USPQ 209, 212 (CCPA 1971). The instant art rejection analysis does not include knowledge gleaned only from applicant's disclosure. The structures of the claimed antibodies and the reasons for assembling them into the claimed constructs is found in the prior art.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 1-3, 5-7, 9-13, 15-17, 20-25, and 27 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.
The specification discloses only two CD47 antibodies, 2.3D11 and 5A3M5. Even for embodiments where the antigen binding domain is an antibody against the antigen CD20 (the elected antigen), the specification discloses only one antibody, obinutuzumab. No suitable antibodies are disclosed for the other antigens recited in claim 17. Note that claims 2-3, 5-7, and 9-13 permit variability in the recited CDRs as they include variants. These CDRs are required for binding to the antigen. The specification does not disclose or describe the amino acid modifications (i.e. which amino acid to modify, what substitution to make) that would retain binding.
The N- and C-terminus limitations in claim 1 do not indicate any particular order or assembly of the claimed antibody construct. The particular position of each piece (first VH, first VL, second VH, second VH, IgA constant domains) within the construct affects the binding affinity of the different binding domains and thus, the activity of the overall construct. This is demonstrated by Figure 6B for constructs #2 and #4 and #6 for the antibodies Obinutuzumab and 2.3D11 and for constructs #1, #3, and #5 for the antibodies Obinutuzumab and 5A3M5. Different formats lead to different results. Only antibodies #2, #3, and #5 show an effect of CD47 blocking illustrating CD20 binding is enhanced by additional CD47 binding. See specification paragraph [0070]. These results cannot be extrapolated to predict the properties of other antibody formats or other antibodies. They cannot be extrapolated to predict the properties of variants of antibodies 2.3D11, 5A3M5, and Obinutuzumab as recited in claims 2, 4, 6, and 8. The instant claims are not limited to these formats. See for example Figures 1D-E in WO 2016/024021 (of record).
The structural variability of the claimed antibody construct genus is large. No reasonable structure-function correlation has been established that is commensurate in scope with the claims. The specification does not provide representative examples to adequately describe the claimed genus of antibody constructs having the functional features of the claims.
Applicant’s arguments are unpersuasive. The arguments do not address the structural variety of the antibody constructs claimed, including the large variety of antigen binding domains (see claims 1 and 17) and the small number of exemplified embodiments having the properties recited in the claims. Applicant’s arguments that the specification results demonstrate that any bispecific constructs containing a high affinity antigen-binding arm and a low affinity CD47-binding arm would also be expected to demonstrate superior antibody-mediated cytotoxicity does not remedy the lack of representative examples to adequately describe the claimed genus of antibody constructs and support that assertion. DVD-IgA and scFv-linked IgA formats are not representative of the large number of bispecific formats that would have been known in the art. See at least Figure 2 of Brinkmann et al. In addition, most of the claims are not limited to known or commercially available antibodies. See in particular, claim 1. Changing the format would have been expected to change binding affinities as seen in the exemplified embodiments and discussed above. Different formats lead to different results.
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.
Claim 27 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 27 is confusing. It is unclear if the first polypeptide comprises the first heavy chain variable domain as well as the second heavy chain variable domain in view of the “further comprises” language. This appears to be required given the scFv and VH structures present in SEQ ID NOS: 33 and 34 as discussed above. However, the “further comprises” language could imply a second polypeptide. The claim is further confusing in failing to indicate the presence and/or location of the light chain domain sequences as well as the IgA constant domain sequences with respect to these sequences. See by comparison the structure of claim 10 which delineates each part of the antibody of claim 1.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARIANNE P ALLEN whose telephone number is (571)272-0712. The examiner can normally be reached 7:00-3:30 EST Monday-Friday.
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/Marianne P Allen/Primary Examiner, Art Unit 1647
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