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 6-9 and 11-12 are pending in the instant application.
Claims 11-12 are new.
Claim Objections and Rejections Withdrawn
The objection to the abstract is withdrawn in view of amendment.
The objection and rejection of claim 10 is moot in view of claim cancelation.
The objection to claim 9 is withdrawn in view of claim amendment.
The rejection of claim 9 under 35 USC § 112(b) is withdrawn in view of claim
amendment.
The rejection of claim 7 under 35 USC § 112(d) is withdrawn in view of claim
amendment.
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/CN2021/137352 filed on 12/13/2021 in the absence of a certified translation of
CN202011516850.9 filed on 12/21/2020.
.
Claim Interpretation
Regarding claim 8, the claim is a product by process claim.
Claim Objections and Rejections Maintained and Necessitated by Amendment
Objections to the Claims
Claim 11 is objected to because of the following informalities:
Claim 11 does not include a conjunction of ---and--- after 3) in the claimed method.
Appropriate correction is required.
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.
The rejection of claims 6-9 under 35 U.S.C. 103 as being unpatentable over WO2019127346 ( Wu Z et al. IDS reference ) and Maass KF et al. (J Pharm Sci. 2015 104(12):4409–4416 reference of record) and evidenced by WO 2019/127346 translated ( Wu Z et al. reference of record) is maintained.
‘346 translated taught bifunctional molecules that specifically target tumor cells and can effectively recruit anti-Rha antibodies to achieve different degrees of killing of tumor cells (20%-90%) by mediating CDC or ADCC (page 7, [0076]).
‘346 translated taught an anti-HER2 nanobody, C7b, conjugated to rhamnose (Rha) in the antibody conjugates C7b-triEGRha and C7b-hexEGRha, wherein pharmaceutical compositions comprising C7b-triEGRha and C7b-hexEGRha could specifically bind cancer cells that expressed the HER2 target (page 11, [0122] and Fig. 5) and effectively induce ADCC and CDC to kill cancer cells (page 11, [0122-0126] and Fig 6A-B).
‘346 translated taught synthesis of C7b-triEGRha and C7b-hexEGRha via sortase conjugation (page 11, [0117-0118]).
‘346 translated taught conjugation of Rha to the GGG via a Rha-PEG-primary amine reactive moiety wherein n = 2 (page 10, [0109-0112])
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‘346 did not teach: A) a SMCC linked Rha hapten conjugate, but this is obvious in view of Maass.
Maass taught a method of preparing an anti-HER2 antibody drug conjugate pharmaceutical composition via cysteine conjugation to produce a Trastuzumab-Doxorubicin Conjugate, Tras-Dox (page 4411, right column, second paragraph). Maass taught a method of producing Tras-Dox with Doxorubicin–SMCC, wherein Doxorubicin–SMCC was produced by adding succinimidyl 4-[N-maleimidomethyl] cyclohexane-1-carboxylate (SMCC), doxorubicin, diisoprpylethylamine (DIPEA), and dimethylformamide (DMF) together to conjugate the primary amine of doxorubicin with SMCC (page 4411, left to right bridging paragraph and Scheme 1.)
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Maass taught the conjugate Tras-Dox effectively bound cancer cells that expressed HER2 (Supplemental page 1, supplemental Table 1 ).
Regarding claims 6-9, it would have been obvious for a person having ordinary skill in the art to take the Rha-PEG-primary amine reactive moiety wherein n = 2
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of ‘346 in the pharmaceutical compositions comprising C7b-triEGRha and: A) exchange the sortase-GGG comprising linker antibody conjugation for a SMCC linker-cysteine anti-HER2 antibody conjugation, wherein
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is added to SMCC in DIPEA and DMF in view of Maass.
This is obvious because: A) Maass taught an effective method of preparing an anti-HER2 antibody drug conjugate via cysteine conjugation to produce a Trastuzumab-Doxorubicin Conjugate, Tras-Dox, wherein SMCC, doxorubicin, DIPEA, and DMF successfully conjugated the primary amine of doxorubicin with SMCC to produce a conjugate Tras-Dox that effectively bound cancer cells that expressed HER2.
There is a reasonable expectation of success because: A) Maass taught an effective method of preparing an anti-HER2 antibody drug conjugate via cysteine conjugation to produce a Trastuzumab-Doxorubicin Conjugate, Tras-Dox, wherein SMCC, doxorubicin, DIPEA, and DMF successfully conjugated the primary amine of doxorubicin with SMCC to produce a conjugate Tras-Dox that effectively bound cancer cells that expressed HER2. Thus, the SMCC linker allowed successful conjugation to the anti-HER2 antibody and effective delivery to cancer cells.
This would produce a pharmaceutical compositions comprising an anti-HER2 antibody conjugated to the rhamnose hapten derivative of
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(claims 6-7). This pharmaceutical composition comprising the anti-HER2 antibody rhamnose hapten derivative above could naturally be used in the preparation of a drug with enhanced immune effect function of an antibody (claim 9). The synthetic pathway to produce the anti-HER2 antibody rhamnose hapten derivative above of ‘346 and Maass is:
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and would produce the hapten derivative claimed in the product by process claimed in claim 8, wherein determination of patentability is based on the product itself as taught by MPEP 2113.
Response to Arguments
Applicant argues, first, '346 teaches a different molecular platform. The Office's rejection relies on '346's teaching of an anti-HER2 nanobody (C7b) conjugated to rhamnose (Rha). However, there is a fundamental distinction: '346 teaches nanobodies (VHH, single-domain antibodies), not full-length monoclonal antibodies as recited by the claims. As disclosed in '346, the invention is directed to "bifunctional molecules based on nanobody" for tumor immunotherapy. See '346, paragraph [0009]. '346 specifically teaches that "B includes anti-EGFR nanobody, anti-HER2 nanobody, anti-PSMA nanobody." See '346, paragraph [0016]. Nanobodies are structurally and functionally distinct from monoclonal antibodies - nanobodies are single-domain antibody fragments derived from camelid heavy-chain antibodies, with a molecular weight of approximately 15 kDa, while monoclonal antibodies are full-length immunoglobulins with a molecular weight of approximately 150 kDa. Critically, nanobodies lack the Fc region that is essential for mediating ADCC and CDC immune effector functions. The present invention solves a specific problem: enhancing the Fc-mediated immune effector functions (ADCC/CDC) of existing therapeutic monoclonal antibodies without compromising their affinity or stability. See As-Filed Specification, non-limiting paragraphs [0004], [0006]. Because '346's nanobodies lack an Fc region, '346 does not address and cannot solve this problem.
In response, Applicant's arguments dated 6/10/2026 have been considered but
are not found persuasive. ‘346 translated taught an anti-HER2 nanobody, C7b, which is an antibody, conjugated to rhamnose (Rha) in the antibody conjugates C7b-triEGRha and C7b-hexEGRha, wherein pharmaceutical compositions comprising C7b-triEGRha and C7b-hexEGRha could specifically bind cancer cells that expressed the HER2 target (page 11, [0122] and Fig. 5) and effectively induce ADCC and CDC to kill cancer cells (page 11, [0122-0126] and Fig 6A-B). The claims do not require a full-length antibody. If amended to require a full-length antibody, then further search would be performed to identify prior art teachings for enhanced ADCC of full-length antibodies.
Applicant argues, second, '346 teaches a different conjugation method. '346 specifically employs enzymatic (sortase A) conjugation to achieve site-specificity. As disclosed in '346, "B is connected to linker through sortase A enzyme." See '346, paragraph [0021]. '346 further teaches that "B with LPXTGn and linker with Gn are connected through sortase A." See '346, paragraph [0022]. In contrast, the present invention uses chemical conjugation (SMCC) targeting reduced hinge region cysteines. The coupling domain is preferably SMCC or other molecules containing maleimides, and the coupling site is preferably the eight thiol groups formed by the reduction of four disulfide bonds on the antibodies. See As-Filed Specification, non-limiting paragraph [0011]. '346 does not disclose or suggest SMCC, maleimide chemistry, or hinge cysteine modification.
In response, Applicant's arguments dated 6/10/2026 have been considered but
are not found persuasive. In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). While ‘346 taught sortase conjugation, a SMCC linked Rha hapten conjugate is obvious in view of Maass. As further described in the obvious rational above, Maass taught an effective method of preparing an anti-HER2 antibody drug conjugate pharmaceutical composition via cysteine conjugation to produce a Trastuzumab-Doxorubicin Conjugate, Tras-Dox (page 4411, right column, second paragraph). Maass taught a method of effectively producing Tras-Dox with Doxorubicin–SMCC, wherein Doxorubicin–SMCC was produced by adding succinimidyl 4-[N-maleimidomethyl] cyclohexane-1-carboxylate (SMCC), doxorubicin, diisoprpylethylamine (DIPEA), and dimethylformamide (DMF) together to conjugate the primary amine of doxorubicin with SMCC (page 4411, left to right bridging paragraph and Scheme 1.), wherein the conjugate Tras-Dox effectively bound cancer cells that expressed HER2 (Supplemental page 1, supplemental Table 1 ).
Applicant argues, Third, there is no motivation to combine the applied references. '346 and Maass belong to different technical fields with different objectives. '346 focuses on nanobody-based immune recruitment using Rha haptens conjugated via sortase A, while Maass focuses on intracellular delivery of cytotoxic drugs (doxorubicin) via antibody-drug conjugates using SMCC. There is no motivation for a person of ordinary skill in the art to take the Rha hapten from '346 (used in a nanobody context for immune recruitment) and attach the Rha hapten to a full-length monoclonal antibody using Maass's SMCC method (designed for drug delivery). Specifically, '346 does not suggest that the Rha hapten should be attached via SMCC, and Maass does not suggest that the SMCC linker should be used to attach haptens for enhancing immune effector functions. The combination proposed by the Office is based on hindsight reconstruction rather than any teaching or suggestion in the applied references.
In response, Applicant's arguments dated 6/10/2026 have been considered but are not found persuasive. In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971). As described in the obvious rational above, it would have been obvious for a person having ordinary skill in the art to take the Rha-PEG-primary amine reactive moiety wherein n = 2
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of ‘346 in the pharmaceutical compositions comprising C7b-triEGRha and: A) exchange the sortase-GGG comprising linker antibody conjugation for a SMCC linker-cysteine anti-HER2 antibody conjugation, wherein
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is added to SMCC in DIPEA and DMF in view of Maass.
This is obvious with a reasonable expectation of success because: A) Maass taught an effective method of preparing an anti-HER2 antibody drug conjugate via cysteine conjugation to produce a Trastuzumab-Doxorubicin Conjugate, Tras-Dox, wherein SMCC, doxorubicin, DIPEA, and DMF successfully conjugated the primary amine of doxorubicin with SMCC to produce a conjugate Tras-Dox that effectively bound cancer cells that expressed HER2. Thus, the SMCC linker allowed successful conjugation to the anti-HER2 antibody and effective delivery to cancer cells. Thus, the conjugation via SMCC was known to be effective and produce an effective drug conjugate.
Applicant argues, fourth, the specific hapten derivative (SMCC-PEG3-Rha) recited by the claims yields unexpected results. The present invention provides experimental data demonstrating that the SMCC-PEG3-Rha derivative helps to confer significantly enhanced ADCC and CDC activity compared to other linker lengths. As shown in non-limiting Figures 3B and 4B of the specification, conjugate aCD20-PEG3-Rha exhibited the highest ADCC and CDC activities. Notably, when cells were treated with only 0.1 nM of aCD20-PEG3-Rha, the percentage of cell lysis could reach 69.3%, which is significantly higher than cells treated with 2.5 nM of Rituximab (53.2%). See As-Filed Specification, Embodiment 4. This demonstrates that the claimed combination is not a mere predictable variation but a critical and optimized solution that helps to achieve superior performance. The length and nature of the PEG3 linker are critical for maintaining antibody affinity while allowing optimal hapten presentation for natural antibody recruitment. Claims 7-9 depend from claim 6, recite additional features, and distinguish over the applied references for at least the same reasons as claim 6 and/or for the additional features recited.
In response, Applicant's arguments dated 6/10/2026 have been considered but are not found persuasive. MPEP 716.02(d) requires unexpected results to be commensurate in scope with claimed invention. Whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the "objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support." In other words, the showing of unexpected results must be reviewed to see if the results occur over the entire claimed range. In re Clemens, 622 F.2d 1029, 1036, 206 USPQ 289, 296 (CCPA 1980). The unexpected results are present for the antibody hapten derivative with the structure
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, wherein Fig. 3 shows the PEG3-Rha is unexpectedly superior to PEG1-Rha and PEG6-Rha monoclonal antibody conjugates. Currently only claim 12 is commensurate with the scope of the unexpected subject matter.
Claims 6-9 and 11 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2019/127346 ( Wu Z et al. IDS reference) and Maass KF et al. (J Pharm Sci. 2015 104(12):4409–4416 reference of record) as applied to claims 6-9 above, and further in view of WO 2018/112027 (Chuang S et al. reference of record), US 2018/0258048 (Coburn CA et al. reference of record), Rohrer T et al. (ADC Review / Journal of Antibody-drug Conjugates – June 21, 2013. DOI: 10.14229/jadc.2013.06.21.001. reference of record), Thermo Scientific TCEP HCl (https://documents.thermofisher.com/TFS-Assets/LSG/manuals/MAN0011306_TCEP_HCl_UG.pdf 2013 reference of record), and GoldBio (https://www.goldbio.com/blogs/articles/tcep-the-reducing-agent. 3/31/2020 reference of record).
‘346 and Maass are described above.
‘346 did not teach: 1) desalting the antibody in sodium borate and adding TCEP for antibody hapten conjugation but this is obvious in view of ‘027, ‘048, Rohrer, Thermo, and GoldBio.
‘027 taught to prepare the antibody conjugate Rex-3, the maleimide linker-payload was conjugated to cetuximab via its cysteine residues, wherein: 1) cetuximab was treated with a solution comprising 10 mM TCEP and sodium borate; 2) purified via Ultrafiltration; 3) the antibody was conjugated with 10 molar equivalents of the dasatinib-1 then quenched with cysteine; and 4) ultrafiltered in pH 7.4 PBS buffer to give Rex-3.
‘048 taught synthesis of effective antibody benzazepine conjugates, wherein HER2-TLR8 benzazepine conjugates were active in the presence of PBMCs and cancer cells that express HER2, as measured by TNFα production (Fig. 1)
‘048 taught synthesis of effective antibody benzazepine conjugates, wherein; 1) desalting of an antibody was performed via centrifugal filtration to exchange the antibody into a reaction buffer; 2) TCEP was added to the reaction and incubated with gentle shaking; 3) after the reduction was complete, the maleimide containing Compound-Linker 2.1 was added and incubated followed by quenching with cysteine; and 4) centrifugal filtration was performed on the conjugate (page 179, [0659-0660]).
Rohrer taught naked antibody raw material which is typically frozen at -20°C is thawed and the storage buffer is exchanged (page 6, first paragraph). Rohrer taught buffer exchange is often required to alter the pH, salt concentration, and remove excipients used to improve storage stability in the bulk antibody solution which may hinder or alter the performance of the conjugation reaction (page 6, first paragraph).
Thermo taught because TCEP does not contain thiols, it does not have to be removed from solutions before performing reactions involving maleimide labeling or cross-linking reagents (page 2, compatible applications, option 1). Thermo taught in most situations, TCEP concentrations < 10-20mM are compatible with maleimide reaction chemistry (page 2, compatible applications, option 1).
GoldBio taught TCEP is light sensitive and tubes containing TCEP should be covered with foil, which would keep them in the dark (page 7, Note 3).
Regarding instant claim 11, it would have been obvious for a person having ordinary skill in the art to prepare the antibody conjugate of the pharmaceutical composition of an anti-HER2 antibody conjugated to the rhamnose hapten derivative of ‘346 and Maass above – by:
using the method of preparation of ‘027 of conjugating the maleimide linker-payload to the antibody via its cysteine residues, wherein: 1) an antibody was treated with a solution comprising 10 mM TCEP and sodium borate; 2) purified via Ultrafiltration; 3) the antibody was conjugated with 10 molar equivalents of the maleimide linker conjugate then quenched with cysteine; and 4) ultrafiltered in pH 7.4 PBS buffer to give Rex-3;
Further modifying the method of ‘027 above to 1) desalt the antibody into the buffer of the reaction buffer in view of ‘048 and Rohrer; 2a) add TCEP to the reaction buffer in a second step and incubate with gentle shaking to reduce the cysteines of the antibody in view of ‘048; 2b) perform the reducing in the dark in view of GoldBio; and 2c) Not remove TCEP via ultrafiltration prior to the maleimide antibody conjugation reaction by in view of Thermo.
This is obvious because:
A) ‘027 taught an effective method of conjugating a maleimide linker to an antibody via the cysteine residues;
B1) initially desalting the antibody into the buffer of the reaction buffer was performed by ’048 and Rohrer taught naked antibody raw material which is typically frozen at -20°C is thawed and the storage buffer is exchanged which is often required to alter the pH, salt concentration, and remove excipients used to improve storage stability in the bulk antibody solution which may hinder or alter the performance of the conjugation reaction;
B2a) addition of TCEP to the reaction buffer and incubation with gentle shaking to reduce the cysteines of the antibody was taught by ‘048 and was effective to reduce the antibody for maleimide conjugation to produce an antibody conjugate;
B2b) GoldBio taught TCEP is light sensitive and tubes containing TCEP should be covered with foil, which would keep them in the dark;
B2c) Thermo taught because TCEP does not contain thiols, it does not have to be removed from solutions before performing reactions involving maleimide labeling reagents, wherein in most situations, TCEP concentrations < 10-20mM are compatible with maleimide reaction chemistry. Further, ‘048 did not remove the TCEP before maleimide conjugation to produce an effective conjugation.
There is a reasonable expectation of success because:
A) ‘027 taught an effective method of conjugating a maleimide linker to an antibody via the cysteine residues;
B1) initially desalting the antibody into the buffer of the reaction buffer was performed by ’048 and Rohrer taught naked antibody raw material which is typically frozen at -20°C is thawed and the storage buffer is exchanged which is often required to alter the pH, salt concentration, and remove excipients used to improve storage stability in the bulk antibody solution which may hinder or alter the performance of the conjugation reaction;
B2a) addition of TCEP to the reaction buffer and incubation with gentle shaking to reduce the cysteines of the antibody was taught by ‘048 and was effective to reduce the antibody for maleimide conjugation to produce an antibody conjugate;
B2b) GoldBio taught TCEP is light sensitive and tubes containing TCEP should be covered with foil, which would keep them in the dark;
B2c) Thermo taught because TCEP does not contain thiols, it does not have to be removed from solutions before performing reactions involving maleimide labeling reagents, wherein in most situations, TCEP concentrations < 10-20mM are compatible with maleimide reaction chemistry. Further, ‘048 did not remove the TCEP before maleimide conjugation to produce an effective conjugation.
This would produce a method of preparing the antibody conjugate of the pharmaceutical composition of an anti-HER2 antibody conjugated to the rhamnose hapten derivative, wherein:
the anti-HER2 antibody is desalted into a reaction buffer comprising sodium borate;
TCEP is added to the reaction and placed in a tube covered with foil to perform under dark and shaking conditions;
after the reduction reaction is completed, the antibody is conjugated with 10 molar equivalents of the maleimide linker conjugate
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then quenched with cysteine;
the antibody conjugate is ultrafiltered which would remove excess small molecules and obtain the corresponding antibody conjugate.
Allowable Subject Matter
Claim 12 is objected to as being dependent upon a rejected base claim, but would be allowable is rewritten in independent form, including all of the limitations of the base claim and any intervening claims.
Conclusion
Claims 6-9 and 11 are rejected.
Claim 12 is objected to.
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 JOHN J SKOKO III whose telephone number is (571)272-1107. The examiner can normally be reached M-F 8:30 - 5:00.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Julie Z Wu can be reached at (571)272-5205. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/J.J.S./Examiner, Art Unit 1643
/Karen A. Canella/Primary Examiner, Art Unit 1643
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