RESPONSE TO APPLICANT’S AMENDMENT
1. Applicant’s amendment, filed 7/16/2026, is acknowledged.
2. Claims 1, 3, 5-6, 11-12, 16, 24, 26, 41, 46, 50, 65, 67, and 94-100 are pending.
3. Claims 1, 3, 5-6, 11-12, 16, 24(5), 26(iv), 41(b), 50, 65, 67, 95-96, 98(a), and 99-100 are under examination as they read on the elected a conjugate molecule comprising a CD39 inhibitory protein capable of interfering interaction between CD39 and its substrate and a TGF inhibitory portion capable of interfering interaction between TGF and its receptor and the species:
(a) a particular CD39-binding agent: an antibody or an antigen-binding fragment thereof that specifically recognizes CD39;
(b) a particular TGFβ-binding agent: a TGFβ-binding domain;
(c) a particular TGFβ-binding domain: ECD of TGFPRII (SEQ ID NO: 164), derived from the same TGFP receptor (i.e. TGFβRII);
(d) a particular linker: a peptide linker;
(e) a particular CD39-binding domain: an anti-CD39 antibody moiety comprises a heavy chain variable region and a light chain variable region;
(f) a particular order of linking TGFβ-binding domain to the anti-CD39 antibody moiety at a specific position and a particular fusion protein: the TGFβ- binding domain is linked to the anti-CD39 antibody moiety at carboxyl terminus of the heavy chain constant region of the anti-CD39 antibody moiety; the fusion protein comprises two or more TGFβ-binding domains which are all linked to the heavy chain constant region of the anti-CD39 antibody moiety;
(g) a specific anti-CD39 antibody moiety comprising 6 CDRs: SEQ ID NO: 4, 151 (i.e., 136, N59Q), 16, 22, 28, 34; the VH and VL sequences that read on the elected CDRs are SEQ ID NO: 47/56 (mAb23), 140/143 (hu23H5L5), and 147/111 (hu23.207); as the elected SEQ ID NO: 151 (X58IDPAX59X6oNIKYDPKFQG) comprises X amino acid, Applicants further elect X58=R, X59=Q, X60=G (i.e., SEQ ID NO: 136) for the Examiner's search purpose, filed on 02/04/2026, is acknowledged.
It is noted that none of the elected VH of SEQ ID NOs: 47/140/147 read on the CDR of SEQ ID NO: 151, wherein X58 is R, X59 is Q and X60 is G. Accordingly claims 43, 45 is withdrawn.
Qy 1 RIDPAQGNIKYDPKFQG 17 SEQ ID NO: 51/RQG
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Db 50 RIDPANGNIKYDPKFQG 66 SEQ ID NO: 47
Qy 1 RIDPAQGNIKYDPKFQG 17 SEQ ID NO: 51/RQG
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Db 50 RIDPANGNIKYDPKFQG 66 SEQ ID NO: 140
Qy 1 RIDPAQGNIKYDPKFQG 17 SEQ ID NO: 51/RQG
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Db 50 KIDPANGNIKYDPKFQG 66 SEQ ID NO: 147
4. Claims 43, 45-46, 68, 73, 91, 94, 97 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions.
5. Claims 1, 3, 5-6, 11-12, 16, 24(5), 26(iv), 41(b), 50, 65, 67, 95-96, 98(a), and 99-100 are under examination as they read on the elected conjugate molecule (i.e., ES014-1) above.
6. Claim 11 is objected to under 37 CFR 1.75(c) because it is improper dependent claim since it fails to refer back to an earlier claim. Rather claim 25 refers back to a proceeding claim 96. 37 CFR 1.75(c) states: (c) One or more claims may be presented in dependent form, referring back to and further limiting another claim or claims in the same application.
7. The rejection of claims 1, 3, 5, 6, 20, 35-36, 38-41, 43, 45-46, 50, 65 and 67 under 35 U.S.C. 102(a)(2) as being anticipated by US 20210388105 A1 (Applicant refers to is as “195 Publication” instead of “105 publication” is here by withdrawn in view of Applicant argues that the `105 publication is co-owned by Elpiscience (Suzhou) Biopharma, Ltd. And Elpiscience Biopharma, Ltd., which are the same as the Applicants of the instant Application. Thus US 20210388105 is disqualified as art under 102(b)(2)(C) exception.
8. The following new grounds of rejections are necessitated by the amendment submitted 7/16/2026.
9. The following is a quotation of 35 U.S.C. 112(b) (Pre AIA , 35 U.S.C. 112, second paragraph):
(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.
10. Claims 6, 16, 24, 96 and 98(a) are rejected under 35 U.S.C. 112(b), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention.
the recitation “a TGFβ-binding domain” recited in claim 6 is ambiguous. Claim 6 depends form claim 1 which recites “a TGFβ inhibitory portion”, it is not clear how the “a TGFβ inhibitory portion” is now “a TGFβ-binding domain”.
The recitation “a CD39-bindign domain” in claims 6 and 16 is ambiguous. Claim 6 and 16 directly or indirectly depends from claim 1, which recited “an anti-CD39 antibody moiety”, it is not clear how the anti-CD39 antibody moiety is not “a TGFβ-binding domain”. It is noted that “a CD39-bindign domain” is broader than “an anti-CD39 antibody moiety”. Accordingly, claim 6 does not further limit claim 1.
The recitation “the TGFβ-binding domain” in claim 24 lacks sufficient antecedent basis in base claim 1. Claim 1 recites” a TGFβ inhibitory portion”.
The recitation “the TGFβ-binding domain comprises an extracellular domain (ECD) of a TGFβ receptor” in claim 96 ambiguous. Claim 96 depends from claim 12, however claim 96 fails to limit the recitation “the TGFβ-binding domain comprises two or more ECDs of a TGFβ receptor” recited in base claim 12.
the recitation “derived from” in claim 98(a) is indefinite because it is unclear what changes or how many changes could have occurred to result in a derivative. Derivation only describes the source and not the result.
11. The following is a quotation of 35 U.S.C. 112(a) (Pre-AIA 35 U.S.C. 112, first paragraph):
(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.
12. Claims 1, 3, 5-6, 11-12, 16, 24(5), 26(iv), 41(b), 50, 65, 67, 95-96, 98(a), and 99-100 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention for the same reasons set forth in the previous Office Action mailed 04/16/2026.
Claim 1 encompasses a broad genus of conjugate molecules comprising a genus of 24 anti-CD39 antibody moieties, and a genus of a TGFβ inhibitory portions capable of interfering interaction between TGFβ and its receptors.
Claim 3 encompasses a genus TGFβ antagonist of TGFβ including a genus TGFβ-binding agents.
Claim 5 encompasses a broad genus antibody that specifically recognizes CD39 and a genus antibody that specifically recognizes TGFβ.
Claims 6, 94, 11, 12, 19, 24, 26, 95-96, 98 encompass a broad genus of fusion protein comprising a genus of CD39-binding domains linked to a genus of TGFP- binding domain, a genus of TGFβ-binding domain binds to human TGFβ2, a genus of ECD of a TGFβ receptor II.
Claims 16 and 99 encompass a genus of linkers.
Claim 65 encompasses a genus of additional conjugate moieties.
Claim 95-94 encompasses a genus of TGFβ receptors including TGFβRI, TGFβRII or TGFβRIII.
Applicant’s arguments, filed 7/16/2026, have been fully considered, but have not been found convincing.
Applicant submits that claim 1 has been amended to specify the CD39 inhibitory portion is an anti-CD39 antibody moiety comprising all six CDRs (i.e., three HCDR sequences and three LCDR sequences). Applicants invite the Examiner to note that, the anti-CD39 antibody or antigen-binding fragments thereof having such six CDRs have been granted in the Applicants' another U.S. patent US Claim 1 has been amended to specify the CD39 inhibitory portion is an anti-CD39 antibody moiety comprising all six CDRs (i.e., three HCDR sequences and three LCDR sequences). Applicants invite the Examiner to note that, the anti-CD39 antibody or antigen-binding fragments thereof having such six CDRs have been granted in the Applicants' another U.S. patent US12312410B2.
Claim 11 has been amended to remove the recitation "or an amino acid sequence having at least 85% sequence identity thereof yet retaining binding specificity to TGFβ".
Therefore, the written description rejection for claims 1, 3, 5-6, 11-12, 16, 24, 26, 46, 50, 65, 67 are rendered moot in view of such amendments.
Claim 41 further limits the six CDR sequences of the anti-CD39 antibody moiety of the claimed conjugate molecule. Claim 41(a) recites the six CDR sequences (i.e., SEQ ID NOs: 4, 10, 16, 22, 28, and 34) of mAb23; claim 41(b) recites the six CDR sequences of several humanized mAb23 antibodies. Applicants respectfully submit that, in addition to antibody products having all six CDRs of SEQ ID NOs: 4, 10, 16, 22, 28, and 34, the other claimed antibody products in amended claim 41 are also described with sufficient identifying characteristics using precise definitions such that one skilled in the art could visualize or recognize the identity of the claimed subject matter.
The amended claim 1 is directed to an antibody or an antigen-binding fragment thereof comprising all six CDRs of SEQ ID NOs: 4, 151, 16, 22, 28, and 34. As shown in the table below, SEQ ID NO: 151 is a formula comprising the sequence of SEQ ID NO: 10, and generalized from the sequences of SEQ ID NOs: 10, 134~139. Each of SEQ ID NOs: 134~138 has one amino acid mutation compared to SEQ ID NO: 10, and the mutation occurs at the NG motif (N55G56) which liable to deamidation in HCDR2 of humanized antibody hu23.H5L5. In particular, SEQ ID NO: 134, 135 and 136 has N55G, N55S and N55Q mutation compared to SEQ ID NO: 10, respectively; SEQ ID NO: 137 and 138 has G56A and G56D mutation compared to SEQ ID NO: 10, respectively.
This is not found convening. The Examiner will consider extending the search to cover additional species upon identifying allowable subject matter. The instant claims recite up to 24 different antibody combinations of murine and human without identifying the antibody frameworks. Importantly, Applicant did not address the genus of TGFβ inhibitory portion capable of interfering interaction between TGFβ and TGFβ receptors in claim 1, an antagonist of TGFβ in claim 3, a TGFβ-binding agent in claim 3, an anti-TGFβ antibody in claim 5, a TGFβ-binding domain in claim 6, ECD of TGFβ receptors in claims 12 and 96, all possible ways of linking TGFβ-binding domains to anti-CD39 antibodies in claims 24 and 26. All possible ways of linking TGFβ-binding domains to diabody, fab, fab`, Fd, . . or a multispecific antibody of anti-CD39 antibodies in claim 50, additional conjugate moieties in claim 65, the TGFβ-binding domain binds human TGFβRI, TGFβRII and/or TGFβRIII in claim 95 and mixing and matching ECDs from different TGFβ receptors in claim 98.
The amended claim 1 is directed to an antibody or an antigen-binding fragment thereof comprising all six CDRs of SEQ ID NOs: 4, 151, 16, 22, 28, and 34. As shown in the table below, SEQ ID NO: 151 is a formula comprising the sequence of SEQ ID NO: 10, and generalized from the sequences of SEQ ID NOs: 10, 134~139. Each of SEQ ID NOs: 134~138 has one amino acid mutation compared to SEQ ID NO: 10, and the mutation occurs at the NG motif (N55G56) which liable to deamidation in HCDR2 of humanized antibody hu23.H5L5. In particular, SEQ ID NO: 134, 135 and 136 has N55G, N55S and N55Q mutation compared to SEQ ID NO: 10, respectively; SEQ ID NO: 137 and 138 has G56A and G56D mutation compared to SEQ ID NO: 10, respectively [0433].
This is not found persuasive because SEQ ID NO: 10 (N55) is obtained from the mouse mAb23, while SEQ ID NO: 134-136 has a single mutation at N55G, N55S and N55Q and SEQ ID NO: 137 and 138 has a single mutation at G56A and G56D. Claim 1 encompasses up to 24 different mutations as well as up to 3 mutations in the VH-CDR2. The specification fails to provide representative number of species that fall within the claimed genus. No HCDR2 having two or three mutations are provided that retains CD39 binding.
13. The rejection of claims 1, 3, 5-6, 11-12, 16, 19-20, 24, 26, 50, 65, and 67 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by US 20210107969 A1 is hereby withdrawn in view of applicant amendment and argument.
14. 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. Claims 1, 3, 5-6, 11-12, 16, 24(5), 26(iv), 41(b), 50, 65, 67, 95-96, 98(a), and 99-100 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-24 of U.S. Patent No. US 12312410 (Applicant points to the issued patent in response WD rejection) in view of by US 20210107969 A1.
The `410 patent claims:
An antibody or an antigen-binding fragment thereof capable of specifically binding to human CD39, comprising a heavy chain variable region comprising HCDR1, HCDR2 and HCDR3 and a light chain variable region comprising LCDR1, LCDR2 and LCDR3, wherein:
a) the HCDR1 comprises the amino acid sequence of DTFLH (SEQ ID NO: 4); and
b) the HCDR2 comprises the amino acid sequence of X58IDPAX59X60NIKYDPKFQG (SEQ ID NO: 151); and
c) the HCDR3 comprises the amino acid sequence of SPYYYGSGYRIFDV (SEQ ID NO: 16); and
d) the LCDR1 comprises the amino acid sequence of SAFSSVNYMH (SEQ ID NO: 22); and
e) the LCDR2 comprises the amino acid sequence of TTSNLAS (SEQ ID NO: 28); and
f) the LCDR3 comprises the amino acid sequence of QQRSTYPFT (SEQ ID NO: 34); wherein X58 is R or K, X59 is N, G, S or Q, X60 is G, A or D, wherein: a) the HCDR1 comprises the sequence of SEQ ID NO: 4, the HCDR2 comprises the sequence of SEQ ID NO: 10, the HCDR3 comprises the sequence of SEQ ID NO: 16; the LCDR1 comprises the sequence of SEQ ID NO: 22, the LCDR2 comprises the sequence of SEQ ID NO: 28, and the LCDR3 comprises the sequence of SEQ ID NO: 34; or b) the HCDR1 comprises the sequence of SEQ ID NO: 4, the HCDR2 comprises a sequence selected from the group consisting of SEQ ID NOs: 134, 135, 136, 137, 138, and 139, the HCDR3 comprises the sequence of SEQ ID NO: 16; the LCDR1 comprises the sequence of SEQ ID NO: 22, the LCDR2 comprises the sequence of SEQ ID NO: 28, and the LCDR3 comprises the sequence of SEQ ID NO: 34, comprising a heavy chain variable region comprising a sequence selected from the group consisting of SEQ ID NOs: 47, 60, 62, 64, 66, 68, 70, 72, 74, 140, 141, 142, 146, 147, 39, and a homologous sequence thereof having at least 80% sequence identity yet retaining specific binding affinity to human CD39, and a light chain variable region comprising a sequence selected from the group consisting of SEQ ID NOs: 56, 61, 63, 65, 67, 69, 71, 73, 75, 143, 144, 145, 111, 112, 63, and a homologous sequence thereof having at least 80% sequence identity yet retaining specific binding affinity to human CD39, further comprising an Fc region, which is humanized, which is a monoclonal antibody, a bispecific antibody, a multi-specific antibody, a recombinant antibody, a chimeric antibody, a labeled antibody, a bivalent antibody, an anti-idiotypic antibody or a fusion protein, which is linked to one or more conjugate moieties.
The claims of the `410 patent differs from the claimed invention only in the recitation that the conjugate is comprising TGFβ-binding domain.
The `969 publication teaches the use of the TGFβ inhibitor, anti-CD39-TGFbRII (ECD), a-CD39-TGFbRI or anti-CD39-TGFbRecd in the treatment of cancer [0333] [0335] [0338] [0575], wherein the anti-CD39 antibody (clone IPH5201) comprises SEQ ID NOs: 18 (VL) and 432 (VH) of anti-CD39 (see page 202 under anti-CD39-TGFbRecd). The `969 pub teaches that the fusion proteins comprise one or more of the following ECDs: (1) a ligand-binding sequence of an extracellular domain of TGFbR (e.g., TGFbRII ECD), wherein the ECD binds TGFb1, TGFb2, and/or TGFb3 [0016]. The `969 pub teaches that TGFbRII-ECD can be SEQ ID NO: 177-180 [0058].
The `969 pub teaches two or more ECDs may be fused in serial. In one aspect, the fusion protein comprises a targeting polypeptide and two or more ECDs are fused in serial on the same chain of the targeting polypeptide. Two or more ECDs are fused in serial on the light chain of a targeting polypeptide that is an antibody. The two or more ECDs are connected by linkers. For example, the light chain of a fusion protein of the invention might be N terminus-antibody light chain-linker-ECD #1-linker-ECD #1-C terminus. The ECD may be fused to both the N and C termini of the same chain. For example, the light chain of a fusion protein of the invention might be N terminus-ECD #1-linker-antibody light chain-linker-ECD #1-C terminus [0014] [0182], wherein the linker comprises the polypeptide sequence (GGGGS)n, (GGGGS)3 (SEQ ID NO: 200), (GGGGS)4 (SEQ ID NO: 201) [0015].
The `969 pub teaches that Y (ECD) is fused to the C terminus of the light chain of the antibody. In other embodiments, Y is fused to the C terminus of the heavy chain of the antibody. In some embodiments, Y is fused to the N terminus of the light chain of the antibody. In other embodiments, Y is fused to the N terminus of the heavy chain of the antibody [0010].
Two or more ECDs may be fused in serial. The fusion protein comprises a targeting polypeptide and two or more ECDs are fused in serial on the same chain of the targeting polypeptide. Two or more ECDs are fused in serial on the light chain of a targeting polypeptide that is an antibody. The two or more ECDs are connected by linkers. The light chain of a fusion protein of the invention might be N terminus-antibody light chain-linker-ECD #1-linker-ECD #1-C terminus. The ECD may be fused to both the N and C termini of the same chain. For example, the light chain of a fusion protein of the invention might be N terminus-ECD #1-linker-antibody light chain-linker-ECD #1-C terminus [0182].
The structure of the fusion protein is N (terminus)-ECD #1-ECD #2-C (terminus), N-ECD #2-ECD #1-C, N-ECD #1-linker-ECD #2-C or N-ECD #2-linker-ECD #1-C, N-ECD #1-Fc-ECD #2-C or N-ECD #2-linker-ECD #1-C, N-ECD #1-Fc-linker-ECD #2-C, or N-ECD #2-Fc-linker-ECD #1-C [0014] [0181] .
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The `969 publication teach that the bsAb is bivalent in a 1+1 format (i.e., one binding site for each target)m wherein the bispecific antibody may be a tandem VHH nanobody fusion, tandem scFvs (e.g., BiTE), DART, diabody, F(ab)2, or scFv-Fab fusion [0207]-[0209].
The `969 publication provides for compositions comprising the previously described molecule or fusion protein and a pharmaceutical carrier [0593].
Those of skill in the art would have had a reason to use the anti-CD39 antibodies, humanized C23 such as hu23.H5L5 or , mAb23 taught by the `410 patent as a substitute for the anti-CD39 antibody taught by the `969 publication in the method of cancer treatment taught by `969 publication because like the anti-CD39 antibody taught by the `969 publication, the C23 such as hu23.H5L5 or , mAb23 binds CD39.
15. No claim is allowed.
16. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Sun et al. Creating an immune-favorable tumor microenvironment by a novel anti-CD39/TGFβ-Trap Bispecific Antibody. Poster Abst ID: 792, Journal for Immunotherapy of Cancer, Vol. 9, No. Suppl 2, pp. A827-A827, Nov. 01, 2021 (Year: 2021)
16. 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 extension fee 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 date of this final action.
17. Any inquiry concerning this communication or earlier communications from the examiner should be directed to MAHER M HADDAD whose telephone number is (571)272-0845. The examiner can normally be reached on Monday-Friday from7:00AM to 4:30PM. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Misook Yu, can be reached at telephone number 571-272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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August 18, 2026
/MAHER M HADDAD/ Primary Examiner, Art Unit 1644
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