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
1. The Amendment filed July 30, 2026 in response to the Office Action of April 30, 2026 is acknowledged and has been entered. Claim 9 has been cancelled. Claims 1, 3, 6, 8, 10, 11, and 18 have been amended. New claim 21 has been added.
2. Claims 1-8 and 10-21 are currently being examined.
Priority
3. The priority date of claims 1-8 and 10-21 is March 03, 2021 based on the disclosure of priority application CN 202110235660.8.
New Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
4. Claim 10 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 10 recites the limitation "the stabilizer" in line 1. There is insufficient antecedent basis for this limitation in the claim because amended claim 1 does not recite stabilizer.
New Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
5a. Claim(s) 1-8, 10, 11, and 14-21 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2021/043221 A1 (Chen et al. March 11, 2021, IDS), “Chen-221” in view of US 2023/0078678 A1 (Lueras et al. March 16, 2023, filed Feb. 12, 2021), “Lueras”.
5b. Claim(s) 1-8, 10, 11, and 14-21 are rejected under 35 U.S.C. 103 as being unpatentable over US 2022/0289833 A1 (Chen et al Sep. 15, 2022, of record), “Chen-833” in view of US 2023/0078678 A1 (Lueras et al. March 16, 2023, filed Feb. 12, 2021), “Lueras”.
Chen-833 is the publication of the national stage application of Chen-221. Thus, Chen-833 and Chen-221 have the same disclosure. Chen-833 will be cited for both Chen-833 and Chen-221 in both rejections.
Chen-833 teaches in the claims:.
1. An isolated monoclonal antibody, or an antigen-binding portion thereof, binding to thymic stromal lymphopoietin (TSLP), comprising (i) a heavy chain variable region comprising a VH CDR1 region, a VH CDR2 region and a VH CDR3 region, wherein the VH CDR1 region, the VH CDR2 region and the VH CDR3 region comprise amino acid sequences of (1) SEQ ID NOs: 1, 2 and 3, respectively; (2) SEQ ID Nos: 37, 38, and 39, respectively; or (3) SEQ ID Nos: 47, 48, and 49, respectively, and/or (ii) a light chain variable region comprising a VL CDR1 region, a VL CDR2 region and a VL CDR3 region, wherein the VL CDR1 region, the VL CDR2 region and the VL CDR3 region comprise amino acid sequences of (1) SEQ ID NOs: 4, 5 and 6, respectively; (2) SEQ ID NOs: 40, 41 and 42, respectively; or (3) SEQ ID NOs: 50, 51 and 52, respectively.
2. The isolated monoclonal antibody, or the antigen-binding portion thereof, of claim 1, wherein the heavy chain variable region comprises an amino acid sequence having at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94% 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NOs: 7, 8, 9 (X1=R, X2=V, X3=R; X1=R, X2=V, X3=V; X1=R, X2=A, X3=R; X1=K, X2=A, X3=R; X1=K, X2=A, X3=V), 43 or 53.
3. The isolated monoclonal antibody, or the antigen-binding portion thereof, of claim 1, wherein the light chain variable region comprises an amino acid sequence having at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94% 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NOs: 10, 11 (X1=S, X2=V; X1=A, X2=I; X1=S, X2=I), 44 or 54.
4. The isolated monoclonal antibody, or an antigen-binding portion thereof, of claim 1, wherein the heavy chain variable region and the light chain variable region comprise amino acid sequences having at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90°/a, 91%, 92%, 93%, 94% 95%, 96%, 97%, 98%, 99% or 100% identity to (1) SEQ ID NOs: 7 and 10, respectively; (2) SEQ ID NOs: 8 and 11 (X1=S, X2=V), respectively; (3) SEQ ID NOs: 9 (X1=R, X2=V, X3=R) and 11 (X1=S, X2=V), respectively; (4) SEQ ID NOs: 9 (X1=R, X2=V, X3=V) and 11 (X1=S, X2=V), respectively; (5) SEQ ID NOs: 9 (X1=R, X2=A, X3=R) and 11 (X1=S, X2=V), respectively; (6) SEQ ID NOs: 9 (X1=K, X2=A, X3=R) and 11 (X1=S, X2=V), respectively; (7) SEQ ID NOs: 9 (X1=K, X2=A, X3=V) and 11 (X1=S, X2=V), respectively; (8) SEQ ID NOs: 8 and 11 (X1=A, X2=I), respectively; (9) SEQ ID NOs: 9 (X1=R, X2=V, X3=R) and 11 (X1=A, X2=I), respectively; (10) SEQ ID NOs: 9 (X1=R, X2=V, X3=V) and 11 (X1=A, X2=I), respectively; (11) SEQ ID NOs: 9 (X1=R, X2=A, X3=R) and 11 (X1=A, X2=I), respectively; (12) SEQ ID NOs: 9 (X1=K, X2=A, X3=R) and 11 (X1=A, X2=I), respectively; (13) SEQ ID NOs: 9 (X1=K, X2=A, X3=V) and 11 (X1=A, X2=I), respectively; (14) SEQ ID NOs: 8 and 11 (X1=S, X2=I), respectively; (15) SEQ ID NOs: 9 (X1=R, X2=V, X3=R) and 11 (X1=S, X2=I), respectively; (16) SEQ ID NOs: 9 (X1=R, X2=V, X3=V) and 11 (X1=S, X2=I), respectively; (17) SEQ ID NOs: 9 (X1=R, X2=A, X3=R) and 11 (X1=S, X2=I), respectively; (18) SEQ ID NOs: 9 (X1=K, X2=A, X3=R) and 11 (X1=S, X2=I), respectively; (19) SEQ ID NOs: 9 (X1=K, X2=A, X3=V) and 11 (X1=S, X2=I), respectively; (20) SEQ ID NOs: 43 and 44, respectively; or (21) SEQ ID NOs: 53 and 54, respectively.
5. The isolated monoclonal antibody, or an antigen-binding portion thereof, of claim 1, comprising a heavy chain constant region having an amino acid sequence of SEQ ID NOs: 12, 13 or 57, linked to the heavy chain variable region, and a light chain constant region having an amino acid sequence of SEQ ID NO: 14, linked to the light chain variable region.
6. The isolated monoclonal antibody, or the antigen-binding portion thereof, of claim 1, which (i) binds human TSLP; (ii) binds to monkey TSLP; and/or (iii) blocks human TSLP-human TSLPR/IL7R interaction.
7. The isolated monoclonal antibody, or the antigen-binding portion thereof, of claim 1, which is a mouse, chimeric or humanized antibody.
8. The isolated monoclonal antibody, or the antigen-binding portion thereof, of claim 1, which is an IgG1, IgG2 or IgG4 isotype.
12. A pharmaceutical composition comprising a therapeutically effective amount of the isolated monoclonal antibody, or antigen-binding portion thereof, of claim 1, and a pharmaceutically acceptable carrier.
15. A method for treating a disease associated with TSLP overexpression in a subject in need thereof, comprising administering to the subject the pharmaceutical composition of claim 12.
16. The method of claim 15, wherein the disease is asthma, ulcerative colitis, atopic dermatitis or psoriasis.
17. The method of claim 16, wherein the disease is asthma.
SEQ ID NOs: 1-11 of Chen-833 comprise the claimed SEQ ID NOs: 1-11. See Table 1 of Chen-833 and Appendix of the Office Action of 04/30/2026.
Chen-833 teaches the heavy chain constant region may comprise human IgG1 constant region having the amino acid sequences set forth in SEQ ID NOs: 12 or 57, or human IgG4 constant region having the amino acid sequence set forth in SEQ ID NO: 13, or a fragment thereof. The light chain constant region may comprise human kappa constant region having the amino acid sequence set forth in SEQ ID NO: 14, or a fragment thereof. See ¶ 0018.
SEQ ID NO: 14 of Chen-833 comprises the claimed SEQ ID NO: 14. See Appendix of the Office Action of 04/30/2026.
SEQ ID NO: 57 of Chen-833 comprises the claimed SEQ ID NO: 37. See Appendix of the Office Action of 04/30/2026.
Chen-833 teaches as set forth above, but does that the pharmaceutical compositions comprises a buffering agent, a surfactant and a stabilizer or a lyophilized formulation.
Lueras teaches aqueous compositions comprising (a) an anti-TSLP antibody at a concentration greater than about 140 mg/mL, (b) a surfactant, and (c) at least one basic amino acid or a salt thereof. Also provided are aqueous compositions comprising aqueous compositions comprising (a) an anti-TSLP antibody at a concentration greater than about 140 mg/mL, (b) a surfactant, and (c) at least one calcium salt or magnesium salt. Related articles of manufacture, pre-filled syringes, and vials comprising the compositions of the present disclosure are also provided. See abstract and ¶¶ 0007-0025.
Regarding claims 1, 10, 18, and 21, Lueras teaches that the compositions can comprise proline in an amount of about 50 mM to about 150 mM, or about 50 mM to about 250 mM or from 0 to 250 mM. See ¶¶ 0010, 0012-0014 and 0099-0104 and claims 16 and 21. Lueras teaches the compositions comprise pharmaceutically acceptable ingredients. See ¶¶ 0085-0087 and 0112.
Regarding claims 3 and 21, Lueras teaches the composition comprises the anti-TSLP antibody at a concentration greater than about 100 mg/mL and less than about 300 mg/mL or less than about 250 mg/mL, optionally, at about 160 mg/mL to about 250 mg/mL, e.g., about 180 mg/mL to about 225 mg/mL, about 180 mg/mL to about 200 mg/mL or about 160 mg/mL to about 250 mg/mL See ¶ 0108 and claims 1 and 52-57.
Regarding claims 4, 5, 6, 18 and 21, Lueras teaches the compositions can comprise histidine, histidine acetate or sodium acetate in an amount of about 50 mM to about 150 mM, about 15 mM to about 300 mM, or about 50 mM to about 300 mM at pH 5.5-6.5. See ¶¶ 0008, 0010, 0015, 0040, 0090, 0100, 0102, 0114, 0225 and 0226 and Fig. 13B.
Regarding claims 7, 8, 18 and 21, Lueras teaches the surfactant is polysorbate 20 or polysorbate 80 present at a concentration less than or about 0.005% (w/v) to about 0.015% (w/v), optionally, about 0.010% (w/v)±0.0025% (w/v) surfactant, e.g., about 0.005% (w/v), 0.010% (w/v), or 0.015% (w/v) surfactant or 0.01% (w/v). See ¶¶ 0011-0014, 0093, 0097 and 0106 and claims 23-25 and 30-32.
Regarding claims 11, 18 and 21, Lueras teaches the aqueous composition described herein has a pH of about 4.5 to about 6.75 or about 4.7, 4.8, 4.9, 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6 or 5.7. See ¶¶ 0010, 0015 and 0114.
Regarding claim 14, Lueras teaches articles of manufacture, pre-filled syringes, and vials comprising the compositions of the present disclosure. See abstract and ¶¶ 0017, 0020, 0121 and 0122.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Chen-221 or Chen-833 and Lueras and make pharmaceutical compositions of the TSLP antibodies of Chen-221 or Chen-833 with the pharmaceutical composition components of Lueras because Lueras teaches the pharmaceutical compositions stabilize the TSLP antibodies (See ¶¶ 0007 and Examples 12 and 13). Thus, one would have been motivated to make pharmaceutical compositions of the TSLP antibodies of Chen-221 or Chen-833 with the pharmaceutical composition components of Lueras to increase the stability of the antibodies. One of skill in the art would have been motivated to optimize the concentration of the antibodies and buffers to produce the most stable composition.
The applied Chen-221 reference has a common applicant with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2).
The Chen-221 rejection under 35 U.S.C. 103 might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C.102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B); or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement. See generally MPEP § 717.02.
Response to Arguments
6. Applicant argues that the Chen-221 or Chen-833 references are not prior art because they have priority to CN 202110235660.8.
Applicant’s argument has been considered, but has not been found persuasive. Although the Chen-221 or Chen-833 references have priority to CN 202110235660.8, the filing date of the Chen-221 or Chen-833 references is September 03, 2020, which is prior to the filing date of CN 202110235660.8, March 03, 2021. Thus, the Chen-221 or Chen-833 references qualify as prior art under 35 U.S.C. 102(a)(2). Therefore, the rejections set forth above are proper.
7a. Claim(s) 12 and 13 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2021/043221 A1 (Chen et al. March 11, 2021, IDS), “Chen-221” in view of US 2023/0078678 A1 (Lueras et al. March 16, 2023, filed Feb. 12, 2021), “Lueras” as applied to claims 1-8, 10, 11, and 14-21 above, and further in view of US 2020/0352857 A1 (Gu et al. Nov. 12, 2020), “Gu”.
7b. Claim(s) 12 and 13 are rejected under 35 U.S.C. 103 as being unpatentable over US 2022/0289833 A1 (Chen et al Sep. 15, 2022), “Chen-833” in view of US 2023/0078678 A1 (Lueras et al. March 16, 2023, filed Feb. 12, 2021), “Lueras” as applied to claims 1-8, 10, 11, and 14-21 above, and further in view of US 2020/0352857 A1 (Gu et al. Nov. 12, 2020), “Gu”.
Chen-833 is the publication of the national stage application of Chen-221. Thus, Chen-833 and Chen-221 have the same disclosure. Chen-833 will be cited for both Chen-833 and Chen-221 in both rejections.
Chen-833 and Lueras teach as set forth above, but do not teach lyophilization of the compositions.
Gu teaches reduced viscosity protein formulations comprising antibodies, like anti-TSLP antibodies. See abstract and ¶¶ 0001, 0021, and 0031 and Table 2..
Gu teaches the formulations can comprise proline, histidine, polysorbate 20 or polysorbate 80. See ¶¶ 0020, 0022, and 0090. Gu teaches that proline, histidine, polysorbate 20 and polysorbate 80 are common excipients of liquid and lyophilized protein formulations for stabilization against the stresses of manufacturing, shipping and storage. See ¶¶ 0101-0103 and Table A.
Gu teaches lyophilization of the pharmaceutical formulations. See ¶¶ 0022-0031 and 0037.
Gu teaches pharmaceutical formulations include liquid (e.g., aqueous) solutions that may be directly administered, and lyophilized powders that may be reconstituted into solutions by adding a diluent before administration. See ¶ 0042.
Gu teaches lyophilized proteins are generally more stable than proteins in solution. See ¶ 0004.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Chen-221 or Chen-833, Lueras and Gu and make lyophilized forms of the pharmaceutical compositions of the TSLP antibodies of Chen-221 or Chen-833 and Lueras because Gu teaches making lyophilized forms of TSLP antibody formulations comprising proline, histidine, polysorbate 20 or polysorbate 80 to stabilize the formulations against the stresses of manufacturing, shipping and storage. One would have been motivated to make lyophilized forms of the pharmaceutical compositions of the TSLP antibodies of Chen-221 or Chen-833 and Lueras because Gu teaches lyophilized proteins are generally more stable than proteins in solution.
Conclusion
8. All other objections and rejections recited in the Office Action of May 12, 2016 are withdrawn in view of Applicant’s amendments and arguments and because U.S. Patent No. 12,479,912 B2 (Chen et al. Nov. 25, 2025) and co-pending Application No. 19/388,619 (Chen et al.) have no common applicant, inventor or owner and thus do not qualify for nonstatutory double patenting.
9. No claims allowed.
10. 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.
11. Any inquiry concerning this communication or earlier communications from the examiner should be directed to PETER J REDDIG whose telephone number is (571)272-9031. The examiner can normally be reached on M-F 8:30-5:30 Eastern Time
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Gregory Emch, can be reached at 571-272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/Peter J Reddig/
Primary Examiner, Art Unit 1646
